SHPS1_BOVIN
ID SHPS1_BOVIN Reviewed; 506 AA.
AC O46631; O46632;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type substrate 1;
DE Short=SHP substrate 1;
DE Short=SHPS-1;
DE AltName: Full=CD172 antigen-like family member A;
DE AltName: Full=Inhibitory receptor SHPS-1;
DE AltName: Full=MyD-1 antigen;
DE AltName: Full=Signal-regulatory protein alpha-1;
DE Short=Sirp-alpha-1;
DE AltName: CD_antigen=CD172a;
DE Flags: Precursor;
GN Name=SIRPA; Synonyms=MYD1, PTPNS1, SHPS1, SIRP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-23; ALA-28; LEU-61; ARG-70;
RP HIS-120; 125-GLN; 127-GLY; 129-HIS; 132-VAL; ASN-145; VAL-153; ASP-203;
RP ARG-261; LEU-302; LEU-316; ARG-337; ASN-367; LEU-422; PHE-429 AND GLU-433.
RC STRAIN=Friesian; TISSUE=Peripheral blood;
RX PubMed=9485180;
RX DOI=10.1002/(sici)1521-4141(199801)28:01<1::aid-immu1>3.0.co;2-v;
RA Brooke G.P., Parsons K.R., Howard C.J.;
RT "Cloning of two members of the SIRP alpha family of protein tyrosine
RT phosphatase binding proteins in cattle that are expressed on monocytes and
RT a subpopulation of dendritic cells and which mediate binding to CD4 T
RT cells.";
RL Eur. J. Immunol. 28:1-11(1998).
CC -!- FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts as
CC docking protein and induces translocation of PTPN6, PTPN11 and other
CC binding partners from the cytosol to the plasma membrane. Supports
CC adhesion of cerebellar neurons, neurite outgrowth and glial cell
CC attachment. May play a key role in intracellular signaling during
CC synaptogenesis and in synaptic function. Involved in the negative
CC regulation of receptor tyrosine kinase-coupled cellular responses
CC induced by cell adhesion, growth factors or insulin. Mediates negative
CC regulation of phagocytosis, mast cell activation and dendritic cell
CC activation. CD47 binding prevents maturation of immature dendritic
CC cells and inhibits cytokine production by mature dendritic cells (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds PTPN11 when tyrosine-phosphorylated, except in
CC macrophages, where it primarily binds PTPN6. Binds GRB2 in vitro. Binds
CC JAK2 irrespective of its phosphorylation status and forms a stable
CC complex. Binds SCAP1 and/or SCAP2. The resulting complex recruits FYB1.
CC Binds FGR and PTK2B (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen macrophages. Detected in
CC skin dendritic cells.
CC -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y11045; CAA71942.1; -; mRNA.
DR EMBL; Y11046; CAA71943.1; -; mRNA.
DR RefSeq; NP_786982.1; NM_175788.1.
DR AlphaFoldDB; O46631; -.
DR SMR; O46631; -.
DR STRING; 9913.ENSBTAP00000009488; -.
DR PaxDb; O46631; -.
DR PRIDE; O46631; -.
DR GeneID; 327666; -.
DR KEGG; bta:327666; -.
DR CTD; 140885; -.
DR eggNOG; ENOG502S1XD; Eukaryota.
DR InParanoid; O46631; -.
DR OrthoDB; 904196at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07654; C1-set; 2.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00407; IGc1; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; SH3-binding; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..506
FT /note="Tyrosine-protein phosphatase non-receptor type
FT substrate 1"
FT /id="PRO_0000014940"
FT TOPO_DOM 30..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..145
FT /note="Ig-like V-type"
FT DOMAIN 148..248
FT /note="Ig-like C1-type 1"
FT DOMAIN 255..348
FT /note="Ig-like C1-type 2"
FT REGION 136..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 432..435
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 441..446
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 455..458
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 472..475
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 498..501
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 407..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 431
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000255"
FT MOD_RES 455
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000255"
FT MOD_RES 472
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P97710"
FT MOD_RES 498
FT /note="Phosphotyrosine; by Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P97710"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 170..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 273..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 23
FT /note="N -> S"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 28
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 61
FT /note="S -> L"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 70
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 120
FT /note="Y -> H"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 125
FT /note="R -> Q"
FT VARIANT 127
FT /note="E -> G"
FT VARIANT 129
FT /note="R -> H"
FT VARIANT 132
FT /note="M -> V"
FT VARIANT 145
FT /note="S -> N"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 153
FT /note="L -> V"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 203
FT /note="N -> D"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 261
FT /note="G -> R"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 302
FT /note="F -> L"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 316
FT /note="F -> L"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 337
FT /note="G -> R"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 367
FT /note="S -> N"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 422
FT /note="Q -> L"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 429
FT /note="I -> F"
FT /evidence="ECO:0000269|PubMed:9485180"
FT VARIANT 433
FT /note="D -> E"
FT /evidence="ECO:0000269|PubMed:9485180"
SQ SEQUENCE 506 AA; 55093 MW; 6B7E310677FCF9CB CRC64;
MEPARPAPGR LRPLLCLLLA ASNAWTGTAG DGELQVIQPE RSVSVAAGET ATLHCTVTSL
SPVGPIKWFK GTGPGREFIY SQKEAPFPRV TNVSDATKRN NMDFSIRISN ITPADAGVYY
CVKFRKEERG DMEFKSGPGT HLTVSAKPSP PVLSGPTVRA TPEQTVNFTC TSHGFSPRNI
SLKWFKNGNE LSASQTSVDP EDNNVSYSIN STTKVLLATG DVHSQVICEV AHVTLQGGPP
LRGTANLSET IRVPPTLEIT GSPSAGNQVN VTCQVNKFYP RHLQLTWLEN GNMSRTEAAS
VFVENKDGTF NQTSWFLVNS SAHREAVVLT CQVEHDGQPA VSKNHTLEVS APQKDQDTGQ
TPGPNDSNWT SIFIVVGVVC ALLVALLIAA LYLLRIRQNK AKGSTSSTRL HEPEKNTRET
TQIQDNNDIT YADLNLPKGK KSTPKANEPN NHTEYASIQA RPPPVSEDTL TYADLDMVHL
NRTPKQPAPK PEPSYSEYAS VQVQRK
