[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CD3Z, TISSUE SPECIFICITY, AND PHOSPHORYLATION. DOI=10.1016/0092-8674(92)90598-7; PubMed=1423621 [NCBI, ExPASy, EBI, Israel, Japan] Chan A.C., Iwashima M., Turck C.W., Weiss A.; "ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain."; Cell 71:649-662(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). TISSUE=Leukocyte; DOI=10.1016/j.bbrc.2004.01.127; PubMed=14985102 [NCBI, ExPASy, EBI, Israel, Japan] Kuroyama H., Ikeda T., Kasai M., Yamasaki S., Tatsumi M., Utsuyama M., Saito T., Hirokawa K.; "Identification of a novel isoform of ZAP-70, truncated ZAP kinase."; Biochem. Biophys. Res. Commun. 315:935-941(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan] Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.; "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."; Nature 434:724-731(2005).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). TISSUE=Blood, and 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 521-547, VARIANT STD LEU-GLU-GLN-541 INS, AND FUNCTION. TISSUE=Lymphoid; DOI=10.1016/0092-8674(94)90368-9; PubMed=8124727 [NCBI, ExPASy, EBI, Israel, Japan] Arpaia E., Shahar M., Dadi H., Cohen A., Roifman C.M.; "Defective T cell receptor signaling and CD8+ thymic selection in humans lacking zap-70 kinase."; Cell 76:947-958(1994).
[6]	CHARACTERIZATION OF TAM-BINDING. DOI=10.1084/jem.181.1.375; PubMed=7528772 [NCBI, ExPASy, EBI, Israel, Japan] Isakov N., Wange R.L., Burgess W.H., Watts J.D., Aebersold R., Samelson L.E.; "ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity."; J. Exp. Med. 181:375-380(1995).
[7]	PHOSPHORYLATION AT TYR-315 AND TYR-319, AND MUTAGENESIS OF TYR-315 AND TYR-319. DOI=10.1074/jbc.274.10.6285; PubMed=10037717 [NCBI, ExPASy, EBI, Israel, Japan] Di Bartolo V., Mege D., Germain V., Pelosi M., Dufour E., Michel F., Magistrelli G., Isacchi A., Acuto O.; "Tyrosine 319, a newly identified phosphorylation site of ZAP-70, plays a critical role in T cell antigen receptor signaling."; J. Biol. Chem. 274:6285-6294(1999).
[8]	INTERACTION WITH CBL AND SLA. DOI=10.1073/pnas.96.17.9775; PubMed=10449770 [NCBI, ExPASy, EBI, Israel, Japan] Tang J., Sawasdikosol S., Chang J.-H., Burakoff S.J.; "SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling."; Proc. Natl. Acad. Sci. U.S.A. 96:9775-9780(1999).
[9]	INTERACTION WITH FCRL3. DOI=10.1006/bbrc.2000.4213; PubMed=11162587 [NCBI, ExPASy, EBI, Israel, Japan] Xu M.-J., Zhao R., Zhao Z.J.; "Molecular cloning and characterization of SPAP1, an inhibitory receptor."; Biochem. Biophys. Res. Commun. 280:768-775(2001).
[10]	INTERACTION WITH SHB. DOI=10.1046/j.1432-1033.2002.03008.x; PubMed=12084069 [NCBI, ExPASy, EBI, Israel, Japan] Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.; "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."; Eur. J. Biochem. 269:3279-3288(2002).
[11]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292; TYR-315; TYR-319; TYR-492 AND TYR-493, AND MASS SPECTROMETRY. DOI=10.1073/pnas.2436191100; PubMed=12522270 [NCBI, ExPASy, EBI, Israel, Japan] Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASS SPECTROMETRY. TISSUE=T-cell; DOI=10.1021/ac035352d; PubMed=15144186 [NCBI, ExPASy, EBI, Israel, Japan] Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.; "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."; Anal. Chem. 76:2763-2772(2004).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248; TYR-292; TYR-315; TYR-319; TYR-492 AND TYR-493, AND MASS SPECTROMETRY. DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan] Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.; "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; Nat. Biotechnol. 23:94-101(2005).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292; TYR-315; TYR-319; TYR-492 AND TYR-493, AND MASS SPECTROMETRY. TISSUE=T-cell; DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan] Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.; "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry."; Nat. Methods 2:591-598(2005).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248; TYR-292 AND TYR-492, AND MASS SPECTROMETRY. DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan] Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.; "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."; Mol. Cell. Proteomics 6:537-547(2007).
[16]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-256. DOI=10.1021/bi026465e; PubMed=12450381 [NCBI, ExPASy, EBI, Israel, Japan] Folmer R.H., Geschwindner S., Xue Y.; "Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem."; Biochemistry 41:14176-14184(2002).
[17]	VARIANT STD ARG-518. DOI=10.1126/science.8202713; PubMed=8202713 [NCBI, ExPASy, EBI, Israel, Japan] Chan A.C., Kadlecek T.A., Elder M.E., Filipovich A.H., Kuo W.-L., Iwashima M., Parslow T.G., Weiss A.; "ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency."; Science 264:1599-1601(1994).
[18]	VARIANT STD HIS-465. DOI=10.1046/j.1365-2567.2001.01246.x; PubMed=11412303 [NCBI, ExPASy, EBI, Israel, Japan] Toyabe S., Watanabe A., Harada W., Karasawa T., Uchiyama M.; "Specific immunoglobulin E responses in ZAP-70-deficient patients are mediated by Syk-dependent T-cell receptor signalling."; Immunology 103:164-171(2001).
[19]	VARIANTS [LARGE SCALE ANALYSIS] LEU-175; LEU-191; GLU-448 AND LEU-523. DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan] Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; "Patterns of somatic mutation in human cancer genomes."; Nature 446:153-158(2007).

Comments

FUNCTION: Plays a role in T-cell development and lymphocyte activation. Essential for TCR-mediated IL-2 production. Isoform 1 induces TCR-mediated signal transduction, isoform 2 does not.
CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
SUBUNIT: Interacts with SLA2 when it is phosphorylated. Interacts with CD3Z and with phosphorylated NFAM1. Interacts with CBLB (By similarity). Interacts with CBL and SLA when it is phosphorylated. The association with SLA (or SLA2) and CBL probably leads to its destruction. Interacts with SHB. Interacts with DEF6 (By similarity). Interacts with FCRL3.
INTERACTION:
P06239:LCK; NbExp=1; IntAct=EBI-1211276, EBI-1348;
Q9Y2R2:PTPN22; NbExp=2; IntAct=EBI-1211276, EBI-1211241;
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=After antigen stimulation, isoform 1 concentrates at the immunological synapse and isoform 2 remains cytoplasmic (By similarity).

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P43403-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	TZK
Isoform ID	P43403-2
Features which should be applied to build the isoform sequence: VSP_031156.

Name	3
Isoform ID	P43403-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_031157, VSP_031158.

TISSUE SPECIFICITY: Expressed in T- and natural killer cells.
DOMAIN: The SH2 domain binds to the phosphorylated tyrosine-based activation motif (TAM) of CD3Z.
PTM: Phosphorylated on tyrosine residues upon T-cell antigen receptor (TCR) stimulation. Tyr-319 phosphorylation is essential for full activity.
DISEASE: Defects in ZAP70 are the cause of selective T-cell defect (STD) [MIM:176947]. STD is an autosomal recessive form of severe combined immunodeficiency characterized by a selective absence of CD8-type T-cells.
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily.
SIMILARITY: Contains 1 protein kinase domain.
SIMILARITY: Contains 2 SH2 domains.
WEB RESOURCE: Name=ZAP70base; Note=ZAP70 mutation db; URL="http://bioinf.uta.fi/ZAP70base/";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ZAP70";.

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

L05148; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]
AB083211; BAC43747.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC016699; AAX93187.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039039; AAH39039.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053878; AAH53878.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00329789; -.
IPI00410185; -.
IPI00885038; -.

PIR

A44266; A44266.
A49955; A49955.

RefSeq

NP_001070.2; -.
NP_997402.1; -.

UniGene

Hs.234569

3D structure databases

PDB

1M61; X-ray; 2.50 A; A=1-256.	[ExPASy / RCSB / EBI]
1U59; X-ray; 2.30 A; A=327-606.	[ExPASy / RCSB / EBI]
2OQ1; X-ray; 1.90 A; A=3-256.	[ExPASy / RCSB / EBI]
2OZO; X-ray; 2.60 A; A=1-606.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1M61; -.
1U59; -.
2OQ1; -.
2OZO; -.

ModBase

P43403.

Protein-protein interaction databases

IntAct

P43403; 2.

PTM databases

PhosphoSite

P43403; -.

Enzyme and pathway databases

BRENDA

2.7.10.2; 247.

Pathway_Interaction_DB

pi3kcipathway; Class I PI3K signaling events.
tcrpathway; TCR signaling in naive CD4+ T cells.
cd8tcrpathway; TCR signaling in naive CD8+ T cells.

Reactome

REACT_6900; Signaling in Immune system.

Organism-specific databases

GC02P097788; -.

HIX0002292; -.

HGNC:12858; ZAP70.

CAB002625; -.
HPA003134; -.

MIM

176947; gene+phenotype. [NCBI / EBI]

Orphanet

911; Severe combined immunodeficiency due to ZAP70 deficiency.

PharmGKB

PA37447; -.

Gene expression databases

P43403; -.

P43403; -.

HS_ZAP70; -.

ENSG00000115085; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from HPA).
GO:0042101;	Cellular component: T cell receptor complex (inferred from direct assay from MGI).
GO:0005524;	Molecular function: ATP binding (non-traceable author statement from UniProtKB).
GO:0004715;	Molecular function: non-membrane spanning protein tyrosine kinase activity (inferred from electronic annotation from EC).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006955;	Biological process: immune response (inferred from direct assay from UniProtKB).
GO:0045582;	Biological process: positive regulation of T cell differentiation (inferred from direct assay from MGI).
GO:0045059;	Biological process: positive thymic T cell selection (inferred from direct assay from MGI).
GO:0006468;	Biological process: protein amino acid phosphorylation (non-traceable author statement from UniProtKB).
GO:0007243;	Biological process: protein kinase cascade (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR000980; SH2.
IPR012234; Tyr_kinase_SYK.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.505.10; SH2; 2.

Pfam

PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 2.
Pfam graphical view of domain structure.

PIRSF

PIRSF000604; TyrPK_SYK; 1.

PRINTS

PR00401; SH2DOMAIN.
PR00109; TYRKINASE.

ProDom

PD000001; Prot_kinase; 1.
PD000093; SH2; 2.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00252; SH2; 2.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 2.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P43403; -.

Genome annotation databases

Ensembl

ENSG00000115085; Homo sapiens. [Contig view]

GeneID

7535; -.

KEGG

hsa:7535; -.

Phylogenomic databases

HOVERGEN

P43403; -.

OMA

P43403; PRPMPMD.

Other

29481; -.

P43403; -.

ZAP70; Homo sapiens.

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

Keywords

3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Disease mutation; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Repeat; SCID; SH2 domain; Transferase; Tyrosine-protein kinase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 619`	`619`	`Tyrosine-protein kinase ZAP-70.`	`PRO_0000088168`
`DOMAIN`	`10 102`	`93`	`SH2 1.`
`DOMAIN`	`163 254`	`92`	`SH2 2.`
`DOMAIN`	`338 600`	`263`	`Protein kinase.`
`NP_BIND`	`344 352`	`9`	`ATP (By similarity).`
`ACT_SITE`	`461 461`		`Proton acceptor (By similarity).`
`BINDING`	`369 369`		`ATP (By similarity).`
`MOD_RES`	`248 248`		`Phosphotyrosine.`
`MOD_RES`	`289 289`		`Phosphoserine.`
`MOD_RES`	`292 292`		`Phosphotyrosine.`
`MOD_RES`	`315 315`		`Phosphotyrosine.`
`MOD_RES`	`319 319`		`Phosphotyrosine.`
`MOD_RES`	`492 492`		`Phosphotyrosine; by autocatalysis.`
`MOD_RES`	`493 493`		`Phosphotyrosine.`
`VAR_SEQ`	`1 307`		`Missing (in isoform 2).`	`VSP_031156`
`VAR_SEQ`	`1 126`		`Missing (in isoform 3).`	`VSP_031157`
`VAR_SEQ`	`127 134`		`VRQTWKLE -> MRLGPRWK (in isoform 3).`	`VSP_031158`
`VARIANT`	`175 175`	`1`	`R -> L.`	`VAR_041846 [3D]`
`VARIANT`	`191 191`	`1`	`P -> L.`	`VAR_041847 [3D]`
`VARIANT`	`448 448`	`1`	`G -> E (in a head and neck squamous cell carcinoma sample; somatic mutation).`	`VAR_041848`
`VARIANT`	`465 465`	`1`	`R -> H (in STD).`	`VAR_015538`
`VARIANT`	`518 518`	`1`	`S -> R (in STD).`	`VAR_006351`
`VARIANT`	`523 523`	`1`	`W -> L.`	`VAR_041849`
`VARIANT`	`541 541`	`1`	`K -> KLEQ (in STD).`	`VAR_038688`
`MUTAGEN`	`315 315`		`Y->F: No inhibition of activation.`
`MUTAGEN`	`319 319`		`Y->F: Inhibition of activation.`
`TURN`	`4 7`	`4`
`HELIX`	`17 26`	`10`
`STRAND`	`34 38`	`5`
`STRAND`	`40 42`	`3`
`STRAND`	`46 52`	`7`
`STRAND`	`55 63`	`9`
`STRAND`	`69 71`	`3`
`STRAND`	`77 79`	`3`
`HELIX`	`80 89`	`10`
`STRAND`	`94 96`	`3`
`HELIX`	`114 131`	`18`
`HELIX`	`135 156`	`22`
`HELIX`	`157 160`	`4`
`HELIX`	`170 178`	`9`
`STRAND`	`186 191`	`6`
`STRAND`	`197 204`	`8`
`STRAND`	`207 215`	`9`
`STRAND`	`221 223`	`3`
`STRAND`	`229 231`	`3`
`HELIX`	`232 241`	`10`
`STRAND`	`246 248`	`3`
`STRAND`	`316 320`	`5`
`HELIX`	`334 336`	`3`
`STRAND`	`337 345`	`9`
`STRAND`	`350 357`	`8`
`STRAND`	`364 371`	`8`
`HELIX`	`377 392`	`16`
`STRAND`	`401 415`	`15`
`HELIX`	`422 426`	`5`
`TURN`	`430 432`	`3`
`HELIX`	`435 454`	`20`
`HELIX`	`464 466`	`3`
`STRAND`	`467 471`	`5`
`STRAND`	`474 477`	`4`
`HELIX`	`503 505`	`3`
`HELIX`	`508 513`	`6`
`HELIX`	`518 533`	`16`
`TURN`	`539 542`	`4`
`HELIX`	`546 553`	`8`
`HELIX`	`566 574`	`9`
`HELIX`	`580 582`	`3`
`HELIX`	`586 601`	`16`

Sequence information

Length: 619 AA [This is the length of the unprocessed precursor]

Molecular weight: 69872 Da [This is the MW of the unprocessed precursor]

CRC64: D1E1A8EC66FA116F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPDPAAHLPF FYGSISRAEA EEHLKLAGMA DGLFLLRQCL RSLGGYVLSL VHDVRFHHFP 

        70         80         90        100        110        120 
IERQLNGTYA IAGGKAHCGP AELCEFYSRD PDGLPCNLRK PCNRPSGLEP QPGVFDCLRD 

       130        140        150        160        170        180 
AMVRDYVRQT WKLEGEALEQ AIISQAPQVE KLIATTAHER MPWYHSSLTR EEAERKLYSG 

       190        200        210        220        230        240 
AQTDGKFLLR PRKEQGTYAL SLIYGKTVYH YLISQDKAGK YCIPEGTKFD TLWQLVEYLK 

       250        260        270        280        290        300 
LKADGLIYCL KEACPNSSAS NASGAAAPTL PAHPSTLTHP QRRIDTLNSD GYTPEPARIT 

       310        320        330        340        350        360 
SPDKPRPMPM DTSVYESPYS DPEELKDKKL FLKRDNLLIA DIELGCGNFG SVRQGVYRMR 

       370        380        390        400        410        420 
KKQIDVAIKV LKQGTEKADT EEMMREAQIM HQLDNPYIVR LIGVCQAEAL MLVMEMAGGG 

       430        440        450        460        470        480 
PLHKFLVGKR EEIPVSNVAE LLHQVSMGMK YLEEKNFVHR DLAARNVLLV NRHYAKISDF 

       490        500        510        520        530        540 
GLSKALGADD SYYTARSAGK WPLKWYAPEC INFRKFSSRS DVWSYGVTMW EALSYGQKPY 

       550        560        570        580        590        600 
KKMKGPEVMA FIEQGKRMEC PPECPPELYA LMSDCWIYKW EDRPDFLTVE QRMRACYYSL 

       610 
ASKVEGPPGS TQKAEAACA

P43403 in FASTA 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