[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLN-86 AND MET-603. TISSUE=Intestine; DOI=10.1016/0014-5793(88)80502-7; PubMed=2901990 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J., Cowell G.M., Koenigshoefer E., Danielsen E.M., Moeller J., Laustsen L., Hansen O.C., Welinder K.G., Engberg J., Hunziker W., Spiess M., Sjoestroem H., Noren O.; "Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA."; FEBS Lett. 238:307-314(1988).
[2]	NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-21, AND VARIANT GLN-86. PubMed=2564851 [NCBI, ExPASy, EBI, Israel, Japan] Look A.T., Ashmun R.A., Shapiro L.H., Peiper S.C.; "Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N."; J. Clin. Invest. 83:1299-1307(1989).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature04601; PubMed=16572171 [NCBI, ExPASy, EBI, Israel, Japan] Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; "Analysis of the DNA sequence and duplication history of human chromosome 15."; Nature 440:671-675(2006).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Pancreas; 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 [GENOMIC DNA] OF 1-15. TISSUE=Intestinal epithelium; PubMed=1675638 [NCBI, ExPASy, EBI, Israel, Japan] Shapiro L.H., Ashmun R.A., Roberts W.M., Look A.T.; "Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells."; J. Biol. Chem. 266:11999-12007(1991).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-479 AND 524-967, AND VARIANT GLN-86. TISSUE=Peripheral blood; Eiz-Vesper B., Fuchs N., Gottschalk D., Mueller K., Reuter S., Blasczyk R.; "Genomic organisation of aminopeptidase N."; Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[7]	PROTEIN SEQUENCE OF 2-20 AND 70-81. PubMed=7576235 [NCBI, ExPASy, EBI, Israel, Japan] Watanabe Y., Iwaki-Egawa S., Mizukoshi H., Fujimoto Y.; "Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N."; Biol. Chem. Hoppe-Seyler 376:397-400(1995).
[8]	PROTEIN SEQUENCE OF 2-18. DOI=10.1016/0014-5793(93)80199-5; PubMed=8102610 [NCBI, ExPASy, EBI, Israel, Japan] Nunez L., Amigo L., Rigotti A., Puglielli L., Mingrone G., Greco A.V., Nervi F.; "Cholesterol crystallization-promoting activity of aminopeptidase-N isolated from the vesicular carrier of biliary lipids."; FEBS Lett. 329:84-88(1993).
[9]	CHARACTERIZATION, AND SUBUNIT. PubMed=6149934 [NCBI, ExPASy, EBI, Israel, Japan] Tokioka-Terao M., Hiwada K., Kokubu T.; "Purification and characterization of aminopeptidase N from human plasma."; Enzyme 32:65-75(1984).
[10]	GLYCOSYLATION. PubMed=1705556 [NCBI, ExPASy, EBI, Israel, Japan] O'Connell P.J., Gerkis V., d'Apice A.J.F.; "Variable O-glycosylation of CD13 (aminopeptidase N)."; J. Biol. Chem. 266:4593-4597(1991).
[11]	INTERACTION WITH HCOV-229E SPIKE GLYCOPROTEIN, AND CHARACTERIZATION OF HCOV-229E RECEPTOR FUNCTION. DOI=10.1038/357420a0; PubMed=1350662 [NCBI, ExPASy, EBI, Israel, Japan] Yeager C.L., Ashmun R.A., Williams R.K., Cardellichio C.B., Shapiro L.H., Look A.T., Holmes K.V.; "Human aminopeptidase N is a receptor for human coronavirus 229E."; Nature 357:420-422(1992).
[12]	IDENTIFICATION OF SOLUBLE FORM. PubMed=7902291 [NCBI, ExPASy, EBI, Israel, Japan] Favaloro E.J., Browning T., Facey D.; "CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated."; Exp. Hematol. 21:1695-1701(1993).
[13]	CHARACTERIZATION OF CMV RECEPTOR FUNCTION. PubMed=8105105 [NCBI, ExPASy, EBI, Israel, Japan] Soderberg C., Giugni T.D., Zaia J.A., Larsson S., Wahlberg J.M., Moller E.; "CD13 (human aminopeptidase N) mediates human cytomegalovirus infection."; J. Virol. 67:6576-6585(1993).
[14]	IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR HCOV-229E INFECTION. PubMed=8887485 [NCBI, ExPASy, EBI, Israel, Japan] Kolb A.F., Maile J., Heister A., Siddell S.G.; "Characterization of functional domains in the human coronavirus HCV 229E receptor."; J. Gen. Virol. 77:2515-2521(1996).
[15]	FUNCTION, AND GLYCOSYLATION. DOI=10.1006/excr.1996.3455; PubMed=9056417 [NCBI, ExPASy, EBI, Israel, Japan] Noren K., Hansen G.H., Clausen H., Noren O., Sjostrom H., Vogel L.K.; "Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13) is normally expressed at the cell surface and has full enzymatic activity."; Exp. Cell Res. 231:112-118(1997).
[16]	IDENTIFICATION OF RESIDUES CRITICAL FOR HCOV-229E INFECTION. PubMed=9367365 [NCBI, ExPASy, EBI, Israel, Japan] Kolb A.F., Hegyi A., Siddell S.G.; "Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N."; J. Gen. Virol. 78:2795-2802(1997).
[17]	IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR TGEV INFECTION. PubMed=9634079 [NCBI, ExPASy, EBI, Israel, Japan] Hegyi A., Kolb A.F.; "Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N."; J. Gen. Virol. 79:1387-1391(1998).
[18]	FUNCTION, AND ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC. PubMed=10605003 [NCBI, ExPASy, EBI, Israel, Japan] Dong X., An B., Salvucci Kierstead L., Storkus W.J., Amoscato A.A., Salter R.D.; "Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells."; J. Immunol. 164:129-135(2000).
[19]	ROLE IN ANGIOGENESIS, AND CHARACTERIZATION OF RECEPTOR FOR TUMOR-HOMING PEPTIDES FUNCTION. PubMed=10676659 [NCBI, ExPASy, EBI, Israel, Japan] Pasqualini R., Koivunen E., Kain R., Lahdenranta J., Sakamoto M., Stryhn A., Ashmun R.A., Shapiro L.H., Arap W., Ruoslahti E.; "Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis."; Cancer Res. 60:722-727(2000).
[20]	FUNCTION, AND INDUCTION BY ESTRADIOL AND IL-8. DOI=10.1016/S0015-0282(01)01779-4; PubMed=11384645 [NCBI, ExPASy, EBI, Israel, Japan] Seli E., Senturk L.M., Bahtiyar O.M., Kayisli U.A., Arici A.; "Expression of aminopeptidase N in human endometrium and regulation of its activity by estrogen."; Fertil. Steril. 75:1172-1176(2001).
[21]	MUTAGENESIS OF 288-ASP--SER-295 AND ASN-818. DOI=10.1128/JVI.75.20.9741-9752.2001; PubMed=11559807 [NCBI, ExPASy, EBI, Israel, Japan] Wentworth D.E., Holmes K.V.; "Molecular determinants of species specificity in the coronavirus receptor aminopeptidase N (CD13): influence of N-linked glycosylation."; J. Virol. 75:9741-9752(2001).
[22]	FUNCTION OF SOLUBLE FORM. PubMed=12473585 [NCBI, ExPASy, EBI, Israel, Japan] van Hensbergen Y., Broxterman H.J., Hanemaaijer R., Jorna A.S., van Lent N.A., Verheul H.M., Pinedo H.M., Hoekman K.; "Soluble aminopeptidase N/CD13 in malignant and nonmalignant effusions and intratumoral fluid."; Clin. Cancer Res. 8:3747-3754(2002).
[23]	INTERACTION WITH HCOV-229E SPIKE GLYCOPROTEIN. DOI=10.1128/JVI.77.4.2530-2538.2003; PubMed=12551991 [NCBI, ExPASy, EBI, Israel, Japan] Bonavia A., Zelus B.D., Wentworth D.E., Talbot P.J., Holmes K.V.; "Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E."; J. Virol. 77:2530-2538(2003).
[24]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265, AND MASS SPECTROMETRY. TISSUE=Bile; DOI=10.1074/mcp.M400015-MCP200; PubMed=15084671 [NCBI, ExPASy, EBI, Israel, Japan] Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; "A proteomic analysis of human bile."; Mol. Cell. Proteomics 3:715-728(2004).
[25]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-234; ASN-265; ASN-681 AND ASN-818, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.; "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."; J. Proteome Res. 4:2070-2080(2005).
[26]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-928, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; J. Proteome Res. 6:4150-4162(2007).
[27]	VARIANTS TYR-242 AND PRO-243. PubMed=9452074 [NCBI, ExPASy, EBI, Israel, Japan] Lendeckel U., Wex T., Arndt M., Frank K., Franke A., Ansorge S.; "Identification of point mutations in the aminopeptidase N gene by SSCP analysis and sequencing."; Hum. Mutat. Suppl. 1:S158-S160(1998).

Comments

FUNCTION: Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types including small intestinal and tubular epithelial cells, macrophages, granulocytes and synaptic membranes from the CNS. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.
CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Homodimer. Interacts with the S1 domain of HCoV-229E spike protein.
SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Cytoplasm, cytosol (Potential). Note=A soluble form has also been detected.
TISSUE SPECIFICITY: Expressed in epithelial cells of the kidney, intestine, and respiratory tract; granulocytes, monocytes, fibroblasts, endothelial cells, cerebral pericytes at the blood-brain barrier, synaptic membranes of cells in the CNS. Also expressed in endometrial stromal cells, but not in the endometrial glandular cells. Found in the vasculature of tissues that undergo angiogenesis and in malignant gliomas and lymph node metastases from multiple tumor types but not in blood vessels of normal tissues. A soluble form has been found in plasma. It is found to be elevated in plasma and effusions of cancer patients.
INDUCTION: Estradiol and IL-8 decrease enzymatic activity in vitro in endometrial stromal cells by 40% and 30%, respectively.
DOMAIN: Amino acids 260-353 are essential to mediate susceptibility to infection with HCoV-229E (in porcine/human chimeric studies) and more specifically amino acids 288-295 (mutagenesis studies).
PTM: Sulfated (By similarity).
PTM: N- and O-glycosylated.
PTM: May undergo proteolysis and give rise to a soluble form.
DISEASE: Defects in ANPEP may be a cause of various types of leukemia or lymphoma.
MISCELLANEOUS: Found to serve as a receptor for tumor-homing peptides, more specifically NGR peptides. It could serve thus as a target for delivering drugs into tumors. Concentration in human hepatic bile, varies from 17.3 to 57.6 micrograms/ml.
SIMILARITY: Belongs to the peptidase M1 family [view classification].

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

X13276; CAA31640.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M22324; AAA51719.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC018988; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AC079075; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
BC058928; AAH58928.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M55522; AAA83399.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ421875; CAD19098.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ421876; CAD19098.2; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ426050; CAD19802.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ427985; CAD20931.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ427986; CAD20931.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ427987; CAD20931.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ427988; CAD20931.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A30325; A30325.

NP_001141.2; -.

3D structure databases

ModBase

P15144.

Protein family/group databases

MEROPS

M01.001; -.

Organism-specific databases

HIX0038141; -.

HGNC:500; ANPEP.

CAB002417; -.

151530; gene. [NCBI / EBI]

PharmGKB

PA24815; -.

GeneCards

P15144.

Gene expression databases

ArrayExpress

P15144; -.

CleanEx

HS_ANPEP; -.

GermOnline

ENSG00000166825; Homo sapiens.

Ontologies

GO:0005793;	Cellular component: ER-Golgi intermediate compartment (inferred from direct assay from UniProtKB).
GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0004177;	Molecular function: aminopeptidase activity (traceable author statement from ProtInc).
GO:0008237;	Molecular function: metallopeptidase activity (traceable author statement from ProtInc).
GO:0004872;	Molecular function: receptor activity (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR006025; Pept_M_Zn_BS.
IPR001930; Peptidase_M1.
IPR014782; Peptidase_M1_N.
Graphical view of domain structure.

PANTHER

PTHR11533; Peptidase_M1; 1.

Pfam

PF01433; Peptidase_M1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00756; ALADIPTASE.

PROSITE

PS00142; ZINC_PROTEASE; 1.

BLOCKS

P15144.

Genome annotation databases

Ensembl

ENSG00000166825; Homo sapiens. [Contig view]

GeneID

290; -.

KEGG

hsa:290; -.

Phylogenomic databases

HOVERGEN

P15144; -.

Other

DB00973; Ezetimibe.

ANPEP; Homo sapiens.

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

Keywords

Aminopeptidase; Angiogenesis; Cell membrane; Cytoplasm; Developmental protein; Differentiation; Direct protein sequencing; Glycoprotein; Host-virus interaction; Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism; Protease; Signal-anchor; Sulfation; Transmembrane; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 967`	`966`	`Aminopeptidase N.`	`PRO_0000095081`
`TOPO_DOM`	`2 8`	`7`	`Cytoplasmic.`
`TRANSMEM`	`9 32`	`24`	`Signal-anchor for type II membrane protein (Potential).`
`REGION`	`33 68`	`36`	`Cytosolic Ser/Thr-rich junction.`
`REGION`	`69 967`	`899`	`Metalloprotease.`
`REGION`	`260 353`	`94`	`Interaction with HCoV-229E.`
`ACT_SITE`	`389 389`		`By similarity.`
`ACT_SITE`	`477 477`		`Proton donor (Potential).`
`METAL`	`388 388`		`Zinc; catalytic (By similarity).`
`METAL`	`392 392`		`Zinc; catalytic (By similarity).`
`METAL`	`411 411`		`Zinc; catalytic (By similarity).`
`MOD_RES`	`176 176`		`Sulfotyrosine (Potential).`
`MOD_RES`	`419 419`		`Sulfotyrosine (Potential).`
`MOD_RES`	`424 424`		`Sulfotyrosine (Potential).`
`MOD_RES`	`913 913`		`Sulfotyrosine (Potential).`
`MOD_RES`	`928 928`		`Phosphothreonine.`
`CARBOHYD`	`128 128`		`N-linked (GlcNAc...).`
`CARBOHYD`	`234 234`		`N-linked (GlcNAc...).`
`CARBOHYD`	`265 265`		`N-linked (GlcNAc...).`
`CARBOHYD`	`319 319`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`527 527`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`573 573`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`625 625`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`681 681`		`N-linked (GlcNAc...).`
`CARBOHYD`	`735 735`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`818 818`		`N-linked (GlcNAc...).`
`VARIANT`	`20 20`	`1`	`V -> M (in dbSNP:rs10152474 [NCBI]).`	`VAR_031262`
`VARIANT`	`86 86`	`1`	`R -> Q (in dbSNP:rs25653 [NCBI]).`	`VAR_014736`
`VARIANT`	`242 242`	`1`	`D -> Y.`	`VAR_006727`
`VARIANT`	`243 243`	`1`	`L -> P.`	`VAR_006728`
`VARIANT`	`311 311`	`1`	`A -> V (in dbSNP:rs17240268 [NCBI]).`	`VAR_031263`
`VARIANT`	`321 321`	`1`	`T -> M (in dbSNP:rs8179199 [NCBI]).`	`VAR_031264`
`VARIANT`	`603 603`	`1`	`I -> K (in dbSNP:rs17240212 [NCBI]).`	`VAR_031265`
`VARIANT`	`603 603`	`1`	`I -> M (in dbSNP:rs8192297 [NCBI]).`	`VAR_031266`
`VARIANT`	`752 752`	`1`	`S -> N (in dbSNP:rs25651 [NCBI]).`	`VAR_014737`
`MUTAGEN`	`288 295`		`DYVEKQAS->QSVEETAQ: No change in receptor activity and HCoV-229E infection.`
`MUTAGEN`	`288 295`		`DYVEKQAS->QSVNEQAQ: No change in receptor activity and HCoV-229E infection.`
`MUTAGEN`	`288 295`		`DYVEKQAS->QSVNETAQ: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity.`
`MUTAGEN`	`291 293`		`EKQ->NKT: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity.`
`MUTAGEN`	`291 291`		`E->N: No change of receptor activity and HCoV-229E infection.`
`MUTAGEN`	`293 293`		`Q->T: No change of receptor activity and HCoV-229E infection.`
`MUTAGEN`	`818 818`		`N->E: Very low receptor activity and HCoV-229E infection.`
`CONFLICT`	`536 536`		`V -> E (in Ref. 1; CAA31640).`
`CONFLICT`	`887 887`		`L -> P (in Ref. 1; CAA31640).`

Sequence information

Length: 967 AA [This is the length of the unprocessed precursor]

Molecular weight: 109540 Da [This is the MW of the unprocessed precursor]

CRC64: 37B6BC1BF0D6B1F2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKGFYISKS LGILGILLGV AAVCTIIALS VVYSQEKNKN ANSSPVASTT PSASATTNPA 

        70         80         90        100        110        120 
SATTLDQSKA WNRYRLPNTL KPDSYRVTLR PYLTPNDRGL YVFKGSSTVR FTCKEATDVI 

       130        140        150        160        170        180 
IIHSKKLNYT LSQGHRVVLR GVGGSQPPDI DKTELVEPTE YLVVHLKGSL VKDSQYEMDS 

       190        200        210        220        230        240 
EFEGELADDL AGFYRSEYME GNVRKVVATT QMQAADARKS FPCFDEPAMK AEFNITLIHP 

       250        260        270        280        290        300 
KDLTALSNML PKGPSTPLPE DPNWNVTEFH TTPKMSTYLL AFIVSEFDYV EKQASNGVLI 

       310        320        330        340        350        360 
RIWARPSAIA AGHGDYALNV TGPILNFFAG HYDTPYPLPK SDQIGLPDFN AGAMENWGLV 

       370        380        390        400        410        420 
TYRENSLLFD PLSSSSSNKE RVVTVIAHEL AHQWFGNLVT IEWWNDLWLN EGFASYVEYL 

       430        440        450        460        470        480 
GADYAEPTWN LKDLMVLNDV YRVMAVDALA SSHPLSTPAS EINTPAQISE LFDAISYSKG 

       490        500        510        520        530        540 
ASVLRMLSSF LSEDVFKQGL ASYLHTFAYQ NTIYLNLWDH LQEAVNNRSI QLPTTVRDIM 

       550        560        570        580        590        600 
NRWTLQMGFP VITVDTSTGT LSQEHFLLDP DSNVTRPSEF NYVWIVPITS IRDGRQQQDY 

       610        620        630        640        650        660 
WLIDVRAQND LFSTSGNEWV LLNLNVTGYY RVNYDEENWR KIQTQLQRDH SAIPVINRAQ 

       670        680        690        700        710        720 
IINDAFNLAS AHKVPVTLAL NNTLFLIEER QYMPWEAALS SLSYFKLMFD RSEVYGPMKN 

       730        740        750        760        770        780 
YLKKQVTPLF IHFRNNTNNW REIPENLMDQ YSEVNAISTA CSNGVPECEE MVSGLFKQWM 

       790        800        810        820        830        840 
ENPNNNPIHP NLRSTVYCNA IAQGGEEEWD FAWEQFRNAT LVNEADKLRA ALACSKELWI 

       850        860        870        880        890        900 
LNRYLSYTLN PDLIRKQDAT STIISITNNV IGQGLVWDFV QSNWKKLFND YGGGSFSFSN 

       910        920        930        940        950        960 
LIQAVTRRFS TEYELQQLEQ FKKDNEETGF GSGTRALEQA LEKTKANIKW VKENKEVVLQ 


WFTENSK

P15144 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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

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