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Entry version 90 (07 Apr 2021)
Sequence version 1 (11 Oct 2005)
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Protein

Platelet endothelial cell adhesion molecule

Gene

Pecam1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-660 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions. Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils. Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal. Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes. Modulates bradykinin receptor BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells. Induces susceptibility to atherosclerosis.By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Platelet endothelial cell adhesion molecule
Short name:
PECAM-1
Alternative name(s):
CD_antigen: CD31
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Pecam1
Synonyms:Pecam
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
61927, Pecam1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini18 – 589ExtracellularSequence analysisAdd BLAST572
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei590 – 610HelicalSequence analysisAdd BLAST21
Topological domaini611 – 678CytoplasmicSequence analysisAdd BLAST68

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000004517618 – 678Platelet endothelial cell adhesion moleculeAdd BLAST661

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi47 ↔ 99PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi74N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi141N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi142 ↔ 195PROSITE-ProRule annotation
Disulfide bondi245 ↔ 293PROSITE-ProRule annotation
Glycosylationi309N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi336 ↔ 375PROSITE-ProRule annotation
Glycosylationi345N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi360N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi420 ↔ 465PROSITE-ProRule annotation
Glycosylationi424N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi512 ↔ 561PROSITE-ProRule annotation
Glycosylationi540N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei660Phosphotyrosine; by FERBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on Ser and Tyr residues after cellular activation. In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation. Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation.By similarity
Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q3SWT0

PRoteomics IDEntifications database

More...
PRIDEi
Q3SWT0

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q3SWT0, 7 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q3SWT0

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q3SWT0

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Trans-homodimer (via Ig-like C2-type 1 and Ig-like C2-type 2 domains); trans-homodimerization is required for cell-cell interaction.

Forms a complex with BDKRB2 and GNAQ.

Interacts with BDKRB2 and GNAQ.

Interacts with PTPN11.

Interacts with FER.

Interacts with CD177; the interaction is Ca2+-dependent; the interaction is direct.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000044403

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q3SWT0

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini40 – 126Ig-like C2-type 1Add BLAST87
Domaini135 – 213Ig-like C2-type 2Add BLAST79
Domaini225 – 309Ig-like C2-type 3Add BLAST85
Domaini315 – 391Ig-like C2-type 4Add BLAST77
Domaini413 – 472Ig-like C2-type 5Add BLAST60
Domaini488 – 577Ig-like C2-type 6Add BLAST90

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi658 – 663ITIM motifBy similarity6

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Ig-like C2-type domains 2 and 3 contribute to formation of the complex with BDKRB2 and in regulation of its activity.By similarity

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QW63, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q3SWT0

Database of Orthologous Groups

More...
OrthoDBi
419506at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q3SWT0

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007110, Ig-like_dom
IPR036179, Ig-like_dom_sf
IPR013783, Ig-like_fold
IPR003599, Ig_sub
IPR003598, Ig_sub2
IPR013151, Immunoglobulin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00047, ig, 1 hit
PF13895, Ig_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409, IG, 4 hits
SM00408, IGc2, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726, SSF48726, 4 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50835, IG_LIKE, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q3SWT0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLLALLLTML LYASLQAQEN SFTINSIHME SRPSWEVSNG QKLTLQCLVD
60 70 80 90 100
ISTTSKSRPQ HQVLFYKDDA LVYNVSSSEH TESFVIPQSR VFHAGKYKCT
110 120 130 140 150
VILNSKEKTT IEYQLTVNGV PMPEVTVDKK EVTEGGIVTV NCSMQEEKPP
160 170 180 190 200
IYFKIEKVEL GTKNVKLSRE KTSNMNFVLI EFPIEEQDHL LVFRCQAGVL
210 220 230 240 250
SGIKMQTSEF IRSEYVTVQE FFSTPKFQIQ PPEMIIEGNQ LHIKCSVQVA
260 270 280 290 300
HLAQEFPEII IQKDKAIVAT SKQSKEAVYS VMALVEHSGH YTCKVESNRI
310 320 330 340 350
SKASSILVNI TELFPRPKLE LSSSRLDQGE MLDLSCSVSG APVANFTIQK
360 370 380 390 400
EETVLSQYQN FSKIAEERDS GLYSCTAGIG KVVKRSNLVP VQVCEMLSKP
410 420 430 440 450
RIFHDAKFEI IKGQIIGISC QSVNGTAPIT YRLLRAKSNF QTVQKNSNDP
460 470 480 490 500
VTFTDKPTRD MEYQCIVDNC HSHPEVRSEI LRVKVIAPVD EVTISILSGN
510 520 530 540 550
DVQSGDEMVL RCSVKEGTGP VTFQFYKEKE GRPFHEETVN DTQVFWHHEQ
560 570 580 590 600
TSKEQEGQYY CTAFNRASIV TSLRSGPLTV RVFLAPWKKG LIAVVVIGVV
610 620 630 640 650
IAALIVAAKY YFLRKAKAKQ KPVEMSRPAV PLLNSNSEKV SEPSVETNSH
660 670
YDSQNMDVEY TEVEVSSLEP HQENGRLP
Length:678
Mass (Da):76,189
Last modified:October 11, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i58062E6CC3FD16E5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
BC104711 mRNA Translation: AAI04712.1
U77697 mRNA Translation: AAB36541.1

NCBI Reference Sequences

More...
RefSeqi
NP_113779.1, NM_031591.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29583

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:29583

UCSC genome browser

More...
UCSCi
RGD:61927, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC104711 mRNA Translation: AAI04712.1
U77697 mRNA Translation: AAB36541.1
RefSeqiNP_113779.1, NM_031591.1

3D structure databases

SMRiQ3SWT0
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000044403

PTM databases

GlyGeniQ3SWT0, 7 sites
iPTMnetiQ3SWT0
PhosphoSitePlusiQ3SWT0

Proteomic databases

PaxDbiQ3SWT0
PRIDEiQ3SWT0

Genome annotation databases

GeneIDi29583
KEGGirno:29583
UCSCiRGD:61927, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5175
RGDi61927, Pecam1

Phylogenomic databases

eggNOGiENOG502QW63, Eukaryota
InParanoidiQ3SWT0
OrthoDBi419506at2759
PhylomeDBiQ3SWT0

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q3SWT0

Family and domain databases

Gene3Di2.60.40.10, 4 hits
InterProiView protein in InterPro
IPR007110, Ig-like_dom
IPR036179, Ig-like_dom_sf
IPR013783, Ig-like_fold
IPR003599, Ig_sub
IPR003598, Ig_sub2
IPR013151, Immunoglobulin
PfamiView protein in Pfam
PF00047, ig, 1 hit
PF13895, Ig_2, 1 hit
SMARTiView protein in SMART
SM00409, IG, 4 hits
SM00408, IGc2, 2 hits
SUPFAMiSSF48726, SSF48726, 4 hits
PROSITEiView protein in PROSITE
PS50835, IG_LIKE, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPECA1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q3SWT0
Secondary accession number(s): P97635
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 11, 2005
Last modified: April 7, 2021
This is version 90 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome
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