CD47_RAT
ID CD47_RAT Reviewed; 303 AA.
AC P97829; O35294;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Leukocyte surface antigen CD47;
DE AltName: Full=Integrin-associated protein;
DE Short=IAP;
DE AltName: CD_antigen=CD47;
DE Flags: Precursor;
GN Name=Cd47;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=9119739; DOI=10.1111/j.1349-7006.1997.tb00356.x;
RA Nishiyama Y., Tanaka T., Naitoh H., Mori C., Fukumoto M., Hiai H.,
RA Toyokuni S.;
RT "Overexpression of integrin-associated protein (CD47) in rat kidney treated
RT with a renal carcinogen, ferric nitrilotriacetate.";
RL Jpn. J. Cancer Res. 88:120-128(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9592107; DOI=10.1523/jneurosci.18-11-04305.1998;
RA Huang A.-M., Wang H.L., Tang Y.P., Lee E.H.Y.;
RT "Expression of integrin-associated protein gene associated with memory
RT formation in rats.";
RL J. Neurosci. 18:4305-4313(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Brown Norway; TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 43-57; 63-93; 123-128 AND 158-164, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-89,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Has a role in both cell adhesion by acting as an adhesion
CC receptor for THBS1 on platelets, and in the modulation of integrins.
CC Receptor for SIRPA, binding to which prevents maturation of immature
CC dendritic cells and inhibits cytokine production by mature dendritic
CC cells. Interaction with SIRPG mediates cell-cell adhesion, enhances
CC superantigen-dependent T-cell-mediated proliferation and costimulates
CC T-cell activation. May play a role in membrane transport and/or
CC integrin dependent signal transduction. May prevent premature
CC elimination of red blood cells. May be involved in membrane
CC permeability changes induced following virus infection (By similarity).
CC Plays an important role in memory formation and synaptic plasticity in
CC the hippocampus. {ECO:0000250, ECO:0000269|PubMed:9592107}.
CC -!- SUBUNIT: Monomer. Interacts with fibrinogen, PTPNS1, SIRPG, THBS1,
CC UBQLN1 and UBQLN2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97829-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97829-2; Sequence=VSP_015794, VSP_015795;
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus.
CC {ECO:0000269|PubMed:9592107}.
CC -!- INDUCTION: By ferric nitrilotriacetate, NMDA and amphetamine.
CC {ECO:0000269|PubMed:9119739, ECO:0000269|PubMed:9592107}.
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DR EMBL; D87659; BAA13420.1; -; mRNA.
DR EMBL; AF017437; AAB70273.1; -; mRNA.
DR EMBL; BC085740; AAH85740.1; -; mRNA.
DR RefSeq; NP_062068.1; NM_019195.2. [P97829-1]
DR AlphaFoldDB; P97829; -.
DR SMR; P97829; -.
DR BioGRID; 248018; 2.
DR IntAct; P97829; 1.
DR MINT; P97829; -.
DR STRING; 10116.ENSRNOP00000050938; -.
DR GuidetoPHARMACOLOGY; 2943; -.
DR GlyGen; P97829; 6 sites, 23 N-linked glycans (3 sites).
DR iPTMnet; P97829; -.
DR PhosphoSitePlus; P97829; -.
DR SwissPalm; P97829; -.
DR PaxDb; P97829; -.
DR PRIDE; P97829; -.
DR GeneID; 29364; -.
DR KEGG; rno:29364; -.
DR UCSC; RGD:2308; rat. [P97829-1]
DR CTD; 961; -.
DR RGD; 2308; Cd47.
DR VEuPathDB; HostDB:ENSRNOG00000001964; -.
DR eggNOG; ENOG502RYTQ; Eukaryota.
DR InParanoid; P97829; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-391160; Signal regulatory protein family interactions.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P97829; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001964; Expressed in pancreas and 19 other tissues.
DR ExpressionAtlas; P97829; baseline and differential.
DR Genevisible; P97829; RN.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:RGD.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IPI:ARUK-UCL.
DR GO; GO:0070053; F:thrombospondin receptor activity; ISO:RGD.
DR GO; GO:1904669; P:ATP export; ISO:RGD.
DR GO; GO:0016477; P:cell migration; IDA:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IMP:ARUK-UCL.
DR GO; GO:0071347; P:cellular response to interleukin-1; IMP:ARUK-UCL.
DR GO; GO:0071349; P:cellular response to interleukin-12; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0070487; P:monocyte aggregation; ISO:RGD.
DR GO; GO:1905450; P:negative regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; IMP:ARUK-UCL.
DR GO; GO:0008228; P:opsonization; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:2000439; P:positive regulation of monocyte extravasation; IMP:ARUK-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:ARUK-UCL.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISO:RGD.
DR GO; GO:0032649; P:regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0032653; P:regulation of interleukin-10 production; ISO:RGD.
DR GO; GO:0032655; P:regulation of interleukin-12 production; ISO:RGD.
DR GO; GO:0032675; P:regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISO:RGD.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR CDD; cd16090; IgV_CD47; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR006704; CD47.
DR InterPro; IPR013147; CD47-like_TM.
DR InterPro; IPR013270; CD47_Vset.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR037805; IgV_CD47.
DR PANTHER; PTHR10613; PTHR10613; 1.
DR Pfam; PF04549; CD47; 1.
DR Pfam; PF08204; V-set_CD47; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Integrin; Membrane; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..303
FT /note="Leukocyte surface antigen CD47"
FT /id="PRO_0000042209"
FT TOPO_DOM 19..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..125
FT /note="Ig-like V-type"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q08722, ECO:0000305"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 8..11
FT /note="LLLG -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9592107"
FT /id="VSP_015794"
FT VAR_SEQ 302..303
FT /note="NN -> KAVEEPLNAFKESKGMMNDE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9592107"
FT /id="VSP_015795"
FT MOD_RES P97829-2:311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ 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
