[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Liver; DOI=10.1073/pnas.92.9.4011; PubMed=7732023 [NCBI, ExPASy, EBI, Israel, Japan] Abu-Elheiga L., Jayakumar A., Baldini A., Chirala S.S., Wakil S.J.; "Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms."; Proc. Natl. Acad. Sci. U.S.A. 92:4011-4015(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-366 (ISOFORMS 2 AND 3), AND NUCLEOTIDE SEQUENCE [MRNA] OF 1-120 (ISOFORM 4). TISSUE=Adipocyte; DOI=10.1073/pnas.1332670100; PubMed=12810950 [NCBI, ExPASy, EBI, Israel, Japan] Mao J., Chirala S.S., Wakil S.J.; "Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region."; Proc. Natl. Acad. Sci. U.S.A. 100:7515-7520(2003).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-2271. DOI=10.1093/carcin/bgh273; PubMed=15333468 [NCBI, ExPASy, EBI, Israel, Japan] Sinilnikova O.M., Ginolhac S.M., Magnard C., Leone M., Anczukow O., Hughes D., Moreau K., Thompson D., Coutanson C., Hall J., Romestaing P., Gerard J.-P., Bonadona V., Lasset C., Goldgar D.E., Joulin V., Venezia N.D., Lenoir G.M.; "Acetyl-CoA carboxylase alpha gene and breast cancer susceptibility."; Carcinogenesis 25:2417-2424(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-113 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [MRNA] OF 1-93 (ISOFORM 3). TISSUE=Mammary gland, and Testis; DOI=10.1016/j.bbalip.2003.09.005; PubMed=14643797 [NCBI, ExPASy, EBI, Israel, Japan] Travers M.T., Vallance A.J., Clegg R.A., Thomson R., Price N.T., Barber M.C.; "Characterisation of an N-terminal variant of acetyl-CoA carboxylase-alpha: expression in human tissues and evolutionary aspects."; Biochim. Biophys. Acta 1634:97-106(2003).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 (ISOFORM 1). TISSUE=Testis; DOI=10.1016/j.ygeno.2004.10.001; PubMed=15607423 [NCBI, ExPASy, EBI, Israel, Japan] Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C., Joulin V.; "Asymmetric expression of transcripts derived from the shared promoter between the divergently oriented ACACA and TADA2L genes."; Genomics 85:71-84(2005).
[7]	PROTEIN SEQUENCE OF 1-18; 39-45; 77-86; 99-111; 121-132; 153-170; 218-224; 267-276; 278-288; 323-335; 568-579; 589-615; 646-657; 748-755; 818-838; 985-992; 997-1008; 1083-1096; 1147-1169; 1192-1199; 1233-1247; 1283-1294; 1317-1325; 1327-1334; 1372-1385; 1401-1420; 1508-1514; 1553-1564; 1668-1687; 1714-1731; 1750-1759; 1782-1798; 1824-1833; 1838-1856; 1905-1916; 1922-1929; 1978-2009; 2063-2072; 2104-2111; 2115-2127; 2139-2161; 2200-2209; 2213-2218; 2221-2229 AND 2261-2293, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-80, AND MASS SPECTROMETRY. TISSUE=Hepatoma; Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.; Submitted (JUL-2007) to UniProtKB.
[8]	INTERACTION WITH BRCA1. DOI=10.1038/sj.onc.1205915; PubMed=12360400 [NCBI, ExPASy, EBI, Israel, Japan] Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D.; "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains."; Oncogene 21:6729-6739(2002).
[9]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29; SER-48; SER-50; SER-53; SER-56; THR-58 AND SER-60, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[11]	INTERACTION WITH BRCA1. DOI=10.1074/jbc.M504652200; PubMed=16326698 [NCBI, ExPASy, EBI, Israel, Japan] Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F., Billaud M., Lenoir G.M., Venezia N.D.; "BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase."; J. Biol. Chem. 281:3172-3181(2006).
[12]	PHOSPHORYLATION AT SER-1263, AND MUTAGENESIS OF SER-78; SER-344; SER-432; SER-1201; SER-1263; SER-1585; SER-1952 AND SER-2211. DOI=10.1016/j.jmb.2006.04.010; PubMed=16698035 [NCBI, ExPASy, EBI, Israel, Japan] Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.; "ACCA phosphopeptide recognition by the BRCT repeats of BRCA1."; J. Mol. Biol. 359:973-982(2006).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1042; SER-2099 AND TYR-2108, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan] Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1844, AND MASS SPECTROMETRY. DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan] Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Anal. Sci. 24:161-166(2008).
[15]	INVOLVEMENT IN ACACA DEFICIENCY. PubMed=6114432 [NCBI, ExPASy, EBI, Israel, Japan] Blom W., de Muinck Keizer S.M.P.F., Scholte H.R.; "Acetyl-CoA carboxylase deficiency: an inborn error of de novo fatty acid synthesis."; N. Engl. J. Med. 305:465-466(1981).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-488, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-25; SER-29 AND SER-48, AND MASS SPECTROMETRY. DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan] Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.; "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."; Mol. Cell 31:438-448(2008).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29 AND SER-80, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[20]	VARIANT [LARGE SCALE ANALYSIS] GLN-1687. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.; "The consensus coding sequences of human breast and colorectal cancers."; Science 314:268-274(2006).

Comments

FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO₃^- = ADP + phosphate + malonyl-CoA.
CATALYTIC ACTIVITY: ATP + biotin-carboxyl-carrier protein + CO₂ = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
COFACTOR: Biotin.
COFACTOR: Binds 2 manganese ions per subunit.
ENZYME REGULATION: By phosphorylation (By similarity).
PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1 .
SUBUNIT: Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis.
INTERACTION:
O60218:AKR1B10; NbExp=3; IntAct=EBI-717681, EBI-1572139;
P38398:BRCA1; NbExp=2; IntAct=EBI-717681, EBI-349905;
SUBCELLULAR LOCATION: Cytoplasm.

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative promoter usage.

Name	1
Isoform ID	Q13085-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	E5A
Isoform ID	Q13085-2
Features which should be applied to build the isoform sequence: VSP_026099.

Name	3
Synonyms	E5B
Isoform ID	Q13085-3
Features which should be applied to build the isoform sequence: VSP_026098.

Name	4
Isoform ID	Q13085-4
Features which should be applied to build the isoform sequence: VSP_026100.

TISSUE SPECIFICITY: Expressed in brain, placental, skeletal muscle, renal, pancreatic and adipose tissues; expressed at low level in pulmonary tissue; not detected in the liver.
PTM: Phosphorylation on Ser-1263 is required for interaction with BRCA1.
DISEASE: Defects in ACACA are a cause of ACACA deficiency [MIM:200350]; also called ACAC or ACC deficiency. ACACA deficiency is an inborn error of de novo fatty acid synthesis. The disorder is associated with severe brain damage, persistent myopathy and poor growth.
SIMILARITY: Contains 1 ATP-grasp domain.
SIMILARITY: Contains 1 biotin carboxylation domain.
SIMILARITY: Contains 1 biotinyl-binding domain.
SIMILARITY: Contains 1 carboxyltransferase domain.
WEB RESOURCE: Name=Wikipedia; Note=Acetyl-CoA carboxylase entry; URL="http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U19822; AAC50139.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY315619; AAP94114.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY315620; AAP94115.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY315621; AAP94116.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY315623; AAP94118.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY315625; AAP94120.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY315627; AAP94122.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY237919; AAP69841.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC137287; AAI37288.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ534888; CAD59556.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ534889; CAD59557.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ564444; CAD92089.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00011569; -.
IPI00396015; -.
IPI00396018; -.
IPI00847501; -.

PIR

I38928; I38928.

RefSeq

NP_942131.1; -.
NP_942133.1; -.
NP_942134.1; -.
NP_942135.1; -.
NP_942136.1; -.

UniGene

Hs.160556

3D structure databases

HSSP

Q00955; 1OD4. [HSSP ENTRY / PDB]

ModBase

Q13085.

Protein-protein interaction databases

IntAct

Q13085; 10.

PTM databases

PhosphoSite

Q13085; -.

Enzyme and pathway databases

BRENDA

6.3.4.14; 247.
6.4.1.2; 247.

Reactome

REACT_1505; Integration of energy metabolism.
REACT_602; Lipid and lipoprotein metabolism.

Organism-specific databases

GC17M032516; -.

HGNC:84; ACACA.

CAB013715; -.

200350; gene+phenotype. [NCBI / EBI]

PharmGKB

PA24421; -.

Gene expression databases

ArrayExpress

Q13085; -.

Bgee

Q13085; -.

GermOnline

ENSG00000132142; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003989;	Molecular function: acetyl-CoA carboxylase activity (traceable author statement from ProtInc).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009374;	Molecular function: biotin binding (inferred from electronic annotation from InterPro).
GO:0004075;	Molecular function: biotin carboxylase activity (inferred from electronic annotation from EC).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006633;	Biological process: fatty acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013537; AcCoA_COase_cen.
IPR011761; ATP-grasp.
IPR013816; ATP_grasp_subdomain_2.
IPR011764; BC.
IPR001882; Biotin_BS.
IPR005482; Biotin_COase_C.
IPR000089; Biotin_lipoyl.
IPR005479; CarbamoylP_synth_lsu_ATP-bd.
IPR005481; CarbamoylP_synth_lsu_N.
IPR000022; Carboxyl_trans.
IPR011763; COA_CT_C.
IPR011762; COA_CT_N.
IPR013817; Pre-ATP_grasp.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
G3DSA:3.40.50.20; Pre-ATP_grasp; 1.

Pfam

PF08326; ACC_central; 1.
PF02785; Biotin_carb_C; 1.
PF00364; Biotin_lipoyl; 1.
PF01039; Carboxyl_trans; 1.
PF00289; CPSase_L_chain; 1.
PF02786; CPSase_L_D2; 1.
Pfam graphical view of domain structure.

PROSITE

PS50975; ATP_GRASP; 1.
PS50979; BC; 1.
PS00188; BIOTIN; 1.
PS50968; BIOTINYL_LIPOYL; 1.
PS50989; COA_CT_CTER; 1.
PS50980; COA_CT_NTER; 1.
PS00866; CPSASE_1; 1.
PS00867; CPSASE_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q13085; -.

Genome annotation databases

Ensembl

ENSG00000132142; Homo sapiens. [Contig view]

GeneID

31; -.

KEGG

hsa:31; -.

Phylogenomic databases

HOVERGEN

Q13085; -.

Other

DB00121; Biotin.

111; -.

ACACA; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Alternative promoter usage; ATP-binding; Biotin; Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis; Ligase; Lipid synthesis; Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 2346`	`2346`	`Acetyl-CoA carboxylase 1.`	`PRO_0000146764`
`DOMAIN`	`117 618`	`502`	`Biotin carboxylation.`
`DOMAIN`	`275 466`	`192`	`ATP-grasp.`
`DOMAIN`	`752 818`	`67`	`Biotinyl-binding.`
`DOMAIN`	`1698 2194`	`497`	`Carboxyltransferase.`
`NP_BIND`	`315 320`	`6`	`ATP (Potential).`
`ACT_SITE`	`441 441`		`By similarity.`
`METAL`	`424 424`		`Manganese 1 (By similarity).`
`METAL`	`437 437`		`Manganese 1 (By similarity).`
`METAL`	`437 437`		`Manganese 2 (By similarity).`
`METAL`	`439 439`		`Manganese 2 (By similarity).`
`BINDING`	`1823 1823`		`Coenzyme A (By similarity).`
`BINDING`	`2127 2127`		`Coenzyme A (By similarity).`
`BINDING`	`2129 2129`		`Coenzyme A (By similarity).`
`MOD_RES`	`1 1`		`N-acetylmethionine.`
`MOD_RES`	`5 5`		`Phosphoserine.`
`MOD_RES`	`23 23`		`Phosphoserine.`
`MOD_RES`	`25 25`		`Phosphoserine.`
`MOD_RES`	`29 29`		`Phosphoserine.`
`MOD_RES`	`48 48`		`Phosphoserine.`
`MOD_RES`	`50 50`		`Phosphoserine.`
`MOD_RES`	`53 53`		`Phosphoserine.`
`MOD_RES`	`56 56`		`Phosphoserine.`
`MOD_RES`	`58 58`		`Phosphothreonine.`
`MOD_RES`	`60 60`		`Phosphoserine.`
`MOD_RES`	`78 78`		`Phosphoserine (By similarity).`
`MOD_RES`	`80 80`		`Phosphoserine.`
`MOD_RES`	`488 488`		`Phosphoserine.`
`MOD_RES`	`786 786`		`N6-biotinyllysine (By similarity).`
`MOD_RES`	`1042 1042`		`Phosphothreonine.`
`MOD_RES`	`1201 1201`		`Phosphoserine (By similarity).`
`MOD_RES`	`1263 1263`		`Phosphoserine.`
`MOD_RES`	`1844 1844`		`Phosphoserine.`
`MOD_RES`	`2099 2099`		`Phosphoserine.`
`MOD_RES`	`2108 2108`		`Phosphotyrosine.`
`VAR_SEQ`	`1 78`		`Missing (in isoform 3).`	`VSP_026098`
`VAR_SEQ`	`1 75`		`MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLD` `LLEEKEGSLSPASVGSDTLSDLGISSLQDGLALHI -> MEGSPEENKEMRYYMLQ (in isoform 2).`	`VSP_026099`
`VAR_SEQ`	`1 1`		`M -> MWWSTLMSILRARSFWKWISTQTVRIIRAVRAHFGGIM (in isoform 4).`	`VSP_026100`
`VARIANT`	`838 838`	`1`	`R -> W (in dbSNP:rs2287351 [NCBI]).`	`VAR_042941`
`VARIANT`	`1687 1687`	`1`	`R -> Q (in a colorectal cancer sample; somatic mutation).`	`VAR_036514`
`VARIANT`	`2271 2271`	`1`	`A -> V (rare polymorphism; frequency <0.004; may play a role in breast cancer susceptibility).`	`VAR_028929`
`MUTAGEN`	`78 78`		`S->A: No effect on interaction with BRCA1.`
`MUTAGEN`	`344 344`		`S->A: No effect on interaction with BRCA1.`
`MUTAGEN`	`432 432`		`S->A: No effect on interaction with BRCA1.`
`MUTAGEN`	`1201 1201`		`S->A: No effect on interaction with BRCA1.`
`MUTAGEN`	`1263 1263`		`S->A: Abolishes interaction with BRCA1.`
`MUTAGEN`	`1585 1585`		`S->A: No effect on interaction with BRCA1.`
`MUTAGEN`	`1952 1952`		`S->A: No effect on interaction with BRCA1.`
`MUTAGEN`	`2211 2211`		`S->A: No effect on interaction with BRCA1.`
`CONFLICT`	`66 66`		`S -> A (in Ref. 1; AAC50139).`
`CONFLICT`	`79 79`		`M -> W (in Ref. 1; AAC50139).`
`CONFLICT`	`89 89`		`R -> G (in Ref. 1; AAC50139).`
`CONFLICT`	`182 182`		`P -> A (in Ref. 1; AAC50139).`
`CONFLICT`	`234 234`		`S -> N (in Ref. 1; AAC50139).`
`CONFLICT`	`299 299`		`Q -> K (in Ref. 1; AAC50139).`
`CONFLICT`	`303 303`		`E -> K (in Ref. 1; AAC50139).`
`CONFLICT`	`364 364`		`A -> V (in Ref. 2; AAP94122).`
`CONFLICT`	`446 446`		`H -> Q (in Ref. 1; AAC50139).`
`CONFLICT`	`494 494`		`D -> N (in Ref. 1; AAC50139).`
`CONFLICT`	`554 554`		`D -> G (in Ref. 1; AAC50139).`
`CONFLICT`	`622 622`		`Q -> R (in Ref. 1; AAC50139).`
`CONFLICT`	`640 640`		`A -> G (in Ref. 1; AAC50139).`
`CONFLICT`	`814 814`		`V -> I (in Ref. 2; AAP94122).`
`CONFLICT`	`1061 1061`		`N -> S (in Ref. 1; AAC50139).`
`CONFLICT`	`1094 1095`		`EL -> DV (in Ref. 1; AAC50139).`
`CONFLICT`	`1225 1225`		`S -> A (in Ref. 1; AAC50139).`
`CONFLICT`	`1257 1257`		`S -> C (in Ref. 1; AAC50139).`
`CONFLICT`	`1297 1297`		`C -> G (in Ref. 1; AAC50139).`
`CONFLICT`	`1320 1320`		`V -> A (in Ref. 1; AAC50139).`
`CONFLICT`	`1444 1444`		`N -> S (in Ref. 1; AAC50139).`
`CONFLICT`	`1474 1474`		`F -> L (in Ref. 1; AAC50139).`
`CONFLICT`	`1665 1666`		`TF -> SL (in Ref. 1; AAC50139).`
`CONFLICT`	`1677 1677`		`I -> V (in Ref. 1; AAC50139).`
`CONFLICT`	`1741 1741`		`P -> S (in Ref. 1; AAC50139).`
`CONFLICT`	`1762 1762`		`S -> G (in Ref. 1; AAC50139).`
`CONFLICT`	`1822 1822`		`C -> S (in Ref. 1; AAC50139).`
`CONFLICT`	`1875 1875`		`M -> T (in Ref. 1; AAC50139).`
`CONFLICT`	`1888 1888`		`D -> G (in Ref. 1; AAC50139).`
`CONFLICT`	`1997 1997`		`I -> V (in Ref. 1; AAC50139).`
`CONFLICT`	`2013 2013`		`Q -> H (in Ref. 1; AAC50139).`
`CONFLICT`	`2058 2058`		`D -> H (in Ref. 1; AAC50139).`
`CONFLICT`	`2075 2075`		`C -> S (in Ref. 1; AAC50139).`
`CONFLICT`	`2098 2099`		`SS -> PT (in Ref. 1; AAC50139).`
`CONFLICT`	`2158 2159`		`TA -> PT (in Ref. 1; AAC50139).`
`CONFLICT`	`2166 2166`		`N -> S (in Ref. 1; AAC50139).`
`CONFLICT`	`2234 2234`		`N -> S (in Ref. 1; AAC50139).`
`CONFLICT`	`2321 2321`		`H -> R (in Ref. 2; AAP94122).`

Sequence information

Length: 2346 AA [This is the length of the unprocessed precursor]

Molecular weight: 265554 Da [This is the MW of the unprocessed precursor]

CRC64: F1F0A518F8824FFC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVGSDTLS 

        70         80         90        100        110        120 
DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK 

       130        140        150        160        170        180 
VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG 

       190        200        210        220        230        240 
GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL 

       250        260        270        280        290        300 
GDKIASSIVA QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA 

       310        320        330        340        350        360 
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV 

       370        380        390        400        410        420 
QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV FEHMEQCAVK LAKMVGYVSA 

       430        440        450        460        470        480 
GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY 

       490        500        510        520        530        540 
GVSPWGDSPI DFEDSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY 

       550        560        570        580        590        600 
FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 

       610        620        630        640        650        660 
ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN FLHSLERGQV 

       670        680        690        700        710        720 
LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG 

       730        740        750        760        770        780 
SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA 

       790        800        810        820        830        840 
EIEVMKMVMT LTAVESGCIH YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ 

       850        860        870        880        890        900 
STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ 

       910        920        930        940        950        960 
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV 

       970        980        990       1000       1010       1020 
FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD 

      1030       1040       1050       1060       1070       1080 
MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELL NILTELTQLS KTTNAKVALR 

      1090       1100       1110       1120       1130       1140 
ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH 

      1150       1160       1170       1180       1190       1200 
SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM 

      1210       1220       1230       1240       1250       1260 
SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFSDSP 

      1270       1280       1290       1300       1310       1320 
PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDRLAAMFRE FTQQNKATLV 

      1330       1340       1350       1360       1370       1380 
DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ 

      1390       1400       1410       1420       1430       1440 
LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE 

      1450       1460       1470       1480       1490       1500 
YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG 

      1510       1520       1530       1540       1550       1560 
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA 

      1570       1580       1590       1600       1610       1620 
YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSTQA 

      1630       1640       1650       1660       1670       1680 
FLPSPPLPSD MLTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI 

      1690       1700       1710       1720       1730       1740 
GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD 

      1750       1760       1770       1780       1790       1800 
PEDPYKGYRY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS 

      1810       1820       1830       1840       1850       1860 
GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR 

      1870       1880       1890       1900       1910       1920 
EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS YMPKSVHSSV PLLNSKDPID 

      1930       1940       1950       1960       1970       1980 
RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG 

      1990       2000       2010       2020       2030       2040 
IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL 

      2050       2060       2070       2080       2090       2100 
MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI 

      2110       2120       2130       2140       2150       2160 
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSTAE 

      2170       2180       2190       2200       2210       2220 
RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG VISDILDWKT SRTFFYWRLR 

      2230       2240       2250       2260       2270       2280 
RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE 

      2290       2300       2310       2320       2330       2340 
EDGVHSVIEE NIKCISRDYV LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST 


MDSPST

Q13085 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools