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Leukocyte surface antigen CD47 (Integrin-associated protein) (IAP) (CD antigen CD47)

 CD47_RAT                Reviewed;         303 AA.
P97829; O35294;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
07-NOV-2018, entry version 118.
RecName: Full=Leukocyte surface antigen CD47;
AltName: Full=Integrin-associated protein;
Short=IAP;
AltName: CD_antigen=CD47;
Flags: Precursor;
Name=Cd47;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
STRAIN=Wistar; TISSUE=Kidney;
PubMed=9119739; DOI=10.1111/j.1349-7006.1997.tb00356.x;
Nishiyama Y., Tanaka T., Naitoh H., Mori C., Fukumoto M., Hiai H.,
Toyokuni S.;
"Overexpression of integrin-associated protein (CD47) in rat kidney
treated with a renal carcinogen, ferric nitrilotriacetate.";
Jpn. J. Cancer Res. 88:120-128(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
AND INDUCTION.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9592107;
Huang A.-M., Wang H.L., Tang Y.P., Lee E.H.Y.;
"Expression of integrin-associated protein gene associated with memory
formation in rats.";
J. Neurosci. 18:4305-4313(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Brown Norway; TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[4]
PROTEIN SEQUENCE OF 43-57; 63-93; 123-128 AND 158-164, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-89,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-109, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24090084; DOI=10.1021/pr400783j;
Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
Graham M.E., Packer N.H., Cordwell S.J.;
"Site-specific glycan-peptide analysis for determination of N-
glycoproteome heterogeneity.";
J. Proteome Res. 12:5791-5800(2013).
-!- FUNCTION: Has a role in both cell adhesion by acting as an
adhesion receptor for THBS1 on platelets, and in the modulation of
integrins. Receptor for SIRPA, binding to which prevents
maturation of immature dendritic cells and inhibits cytokine
production by mature dendritic cells. Interaction with SIRPG
mediates cell-cell adhesion, enhances superantigen-dependent T-
cell-mediated proliferation and costimulates T-cell activation.
May play a role in membrane transport and/or integrin dependent
signal transduction. May prevent premature elimination of red
blood cells. May be involved in membrane permeability changes
induced following virus infection (By similarity). Plays an
important role in memory formation and synaptic plasticity in the
hippocampus. {ECO:0000250, ECO:0000269|PubMed:9592107}.
-!- SUBUNIT: Monomer. Interacts with fibrinogen, PTPNS1, SIRPG, THBS1,
UBQLN1 and UBQLN2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P97829-1; Sequence=Displayed;
Name=2;
IsoId=P97829-2; Sequence=VSP_015794, VSP_015795;
Note=Contains a phosphoserine at position 311.
{ECO:0000244|PubMed:22673903};
-!- TISSUE SPECIFICITY: Expressed in hippocampus.
{ECO:0000269|PubMed:9592107}.
-!- INDUCTION: By ferric nitrilotriacetate, NMDA and amphetamine.
{ECO:0000269|PubMed:9119739, ECO:0000269|PubMed:9592107}.
-----------------------------------------------------------------------
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EMBL; D87659; BAA13420.1; -; mRNA.
EMBL; AF017437; AAB70273.1; -; mRNA.
EMBL; BC085740; AAH85740.1; -; mRNA.
RefSeq; NP_062068.1; NM_019195.2. [P97829-1]
UniGene; Rn.7409; -.
ProteinModelPortal; P97829; -.
SMR; P97829; -.
BioGrid; 248018; 1.
STRING; 10116.ENSRNOP00000050938; -.
iPTMnet; P97829; -.
PhosphoSitePlus; P97829; -.
SwissPalm; P97829; -.
UniCarbKB; P97829; -.
PaxDb; P97829; -.
PRIDE; P97829; -.
Ensembl; ENSRNOT00000050142; ENSRNOP00000050938; ENSRNOG00000001964. [P97829-1]
Ensembl; ENSRNOT00000078434; ENSRNOP00000071430; ENSRNOG00000001964. [P97829-1]
GeneID; 29364; -.
KEGG; rno:29364; -.
UCSC; RGD:2308; rat. [P97829-1]
CTD; 961; -.
RGD; 2308; Cd47.
eggNOG; ENOG410IJTS; Eukaryota.
eggNOG; ENOG41113GI; LUCA.
GeneTree; ENSGT00390000007697; -.
HOGENOM; HOG000013020; -.
HOVERGEN; HBG003808; -.
InParanoid; P97829; -.
KO; K06266; -.
Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
Reactome; R-RNO-216083; Integrin cell surface interactions.
Reactome; R-RNO-391160; Signal regulatory protein family interactions.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:P97829; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001964; Expressed in 10 organ(s), highest expression level in lung.
ExpressionAtlas; P97829; baseline and differential.
Genevisible; P97829; RN.
GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
GO; GO:0070062; C:extracellular exosome; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IPI:ARUK-UCL.
GO; GO:0070053; F:thrombospondin receptor activity; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IDA:RGD.
GO; GO:0071346; P:cellular response to interferon-gamma; IMP:ARUK-UCL.
GO; GO:0071347; P:cellular response to interleukin-1; IMP:ARUK-UCL.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0035696; P:monocyte extravasation; IMP:ARUK-UCL.
GO; GO:1905450; P:negative regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; IMP:ARUK-UCL.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IBA:GO_Central.
GO; GO:0050729; P:positive regulation of inflammatory response; IBA:GO_Central.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:ARUK-UCL.
CDD; cd16090; IgV_CD47; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR006704; CD47.
InterPro; IPR013147; CD47_TM.
InterPro; IPR013270; CD47_Vset.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR037805; IgV_CD47.
PANTHER; PTHR10613; PTHR10613; 1.
Pfam; PF04549; CD47; 1.
Pfam; PF08204; V-set_CD47; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Integrin; Membrane; Phosphoprotein;
Pyrrolidone carboxylic acid; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 303 Leukocyte surface antigen CD47.
/FTId=PRO_0000042209.
TOPO_DOM 19 140 Extracellular. {ECO:0000255}.
TRANSMEM 141 161 Helical. {ECO:0000255}.
TOPO_DOM 162 173 Cytoplasmic. {ECO:0000255}.
TRANSMEM 174 194 Helical. {ECO:0000255}.
TOPO_DOM 195 206 Extracellular. {ECO:0000255}.
TRANSMEM 207 227 Helical. {ECO:0000255}.
TOPO_DOM 228 238 Cytoplasmic. {ECO:0000255}.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TOPO_DOM 260 266 Extracellular. {ECO:0000255}.
TRANSMEM 267 287 Helical. {ECO:0000255}.
TOPO_DOM 288 303 Cytoplasmic. {ECO:0000255}.
DOMAIN 19 125 Ig-like V-type.
MOD_RES 19 19 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:Q08722,
ECO:0000305}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 261 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 41 112 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 8 11 LLLG -> R (in isoform 2).
{ECO:0000303|PubMed:9592107}.
/FTId=VSP_015794.
VAR_SEQ 302 303 NN -> KAVEEPLNAFKESKGMMNDE (in isoform
2). {ECO:0000303|PubMed:9592107}.
/FTId=VSP_015795.
SEQUENCE 303 AA; 32995 MW; E849397AB0DA8D65 CRC64;
MWPLAAALLL GSCCCGSAQL LLSKVKSVEF TSCNDTVVIP CKVLNVEAQS TDEMFVKWKL
NKSYIFIYDG NKNSTTREQN FTSAKISVSD LLKGIASLTM DTHEAVVGNY TCEVTELSRE
GKTVIELKNR PVSWFSTNEK ILIVIFPILA ILLFWGKFGI LTLKYKSSHT NKRIILLLVA
GLALTLIVVV GAILFIPGEK PVKNASGLGL IVISTGILIL LQYNVFMTAF GMTSFTIAIL
ITQVLGYVLA VVGMCLCIMA CEPVHGPLLI SGLGIIALAE LLGLVYMKFV ASNQRTIQPP
RNN


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