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Tyrosine-protein phosphatase non-receptor type substrate 1 (SHP substrate 1) (SHPS-1) (Brain Ig-like molecule with tyrosine-based activation motifs) (Bit) (CD172 antigen-like family member A) (Inhibitory receptor SHPS-1) (Macrophage fusion receptor) (Macrophage membrane protein MFP150) (Signal-regulatory protein alpha-1) (Sirp-alpha-1) (CD antigen CD172a)

 SHPS1_RAT               Reviewed;         509 AA.
P97710; O08951; O70426; Q9QWI5;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
12-SEP-2018, entry version 145.
RecName: Full=Tyrosine-protein phosphatase non-receptor type substrate 1;
Short=SHP substrate 1;
Short=SHPS-1;
AltName: Full=Brain Ig-like molecule with tyrosine-based activation motifs;
Short=Bit;
AltName: Full=CD172 antigen-like family member A;
AltName: Full=Inhibitory receptor SHPS-1;
AltName: Full=Macrophage fusion receptor;
AltName: Full=Macrophage membrane protein MFP150;
AltName: Full=Signal-regulatory protein alpha-1;
Short=Sirp-alpha-1;
AltName: CD_antigen=CD172a;
Flags: Precursor;
Name=Sirpa; Synonyms=Bit, Mfr, Ptpns1, Shps1, Sirp;
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], PROTEIN SEQUENCE OF 42-60; 68-91; 128-137;
150-158; 174-189; 192-202; 204-212; 218-237; 259-270; 279-282; 405-415
AND 446-453, GLYCOSYLATION, PHOSPHORYLATION AT TYROSINE RESIDUES, AND
INTERACTION WITH PTPN6 AND PTPN11.
TISSUE=Fetal fibroblast;
PubMed=8943344; DOI=10.1128/MCB.16.12.6887;
Fujioka Y., Matozaki T., Noguchi T., Iwamatsu A., Yamao T.,
Takahashi N., Tsuda M., Takada T., Kasuga M.;
"A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-
containing protein tyrosine phosphatase SHP-2 in response to mitogens
and cell adhesion.";
Mol. Cell. Biol. 16:6887-6899(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-48 AND 446-453,
FUNCTION, AND PHOSPHORYLATION AT TYROSINE RESIDUES.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9271230; DOI=10.1016/S0014-5793(97)00724-2;
Sano S., Ohnishi H., Omori A., Hasegawa J., Kubota M.;
"BIT, an immune antigen receptor-like molecule in the brain.";
FEBS Lett. 411:327-334(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 99-107; 128-149;
192-217; 405-417; 419-429; 446-467 AND 496-506, GLYCOSYLATION, AND
TISSUE SPECIFICITY.
STRAIN=Fischer 344; TISSUE=Macrophage;
PubMed=9774638; DOI=10.1128/MCB.18.11.6213;
Saginario C., Sterling H., Beckers C., Kobayashi R., Solimena M.,
Ullu E., Vignery A.;
"MFR, a putative receptor mediating the fusion of macrophages.";
Mol. Cell. Biol. 18:6213-6223(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-419, AND TISSUE SPECIFICITY.
STRAIN=WAG/Rij; TISSUE=Alveolar macrophage;
PubMed=9712053;
Adams S., van der Laan L.J.W., Vernon-Wilson E.,
Renardel de Lavalette C., Doepp E.A., Dijkstra C.D., Simmons D.L.,
van den Berg T.K.;
"Signal-regulatory protein is selectively expressed by myeloid and
neuronal cells.";
J. Immunol. 161:1853-1859(1998).
[5]
PROTEIN SEQUENCE OF 192-203; 218-226 AND 297-307, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[6]
PHOSPHORYLATION IN RESPONSE TO EGF, AND INTERACTION WITH PTPN11.
PubMed=9344856; DOI=10.1006/bbrc.1997.7489;
Ochi F., Matozaki T., Noguchi T., Fujioka Y., Yamao T., Takada T.,
Tsuda M., Takeda H., Fukunaga K., Okabayashi Y., Kasuga M.;
"Epidermal growth factor stimulates the tyrosine phosphorylation of
SHPS-1 and association of SHPS-1 with SHP-2, a SH2 domain-containing
protein tyrosine phosphatase.";
Biochem. Biophys. Res. Commun. 239:483-487(1997).
[7]
PHOSPHORYLATION AT TYR-477 AND TYR-501, AND MUTAGENESIS OF TYR-436;
TYR-460; TYR-477 AND TYR-501.
PubMed=9535915; DOI=10.1074/jbc.273.15.9234;
Takada T., Matozaki T., Takeda H., Fukunaga K., Noguchi T.,
Fujioka Y., Okazaki I., Tsuda M., Yamao T., Ochi F., Kasuga M.;
"Roles of the complex formation of SHPS-1 with SHP-2 in insulin-
stimulated mitogen-activated protein kinase activation.";
J. Biol. Chem. 273:9234-9242(1998).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93; ASN-169 AND ASN-312,
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: Immunoglobulin-like cell surface receptor for CD47. Acts
as docking protein and induces translocation of PTPN6, PTPN11 and
other binding partners from the cytosol to the plasma membrane.
Supports adhesion of cerebellar neurons, neurite outgrowth and
glial cell attachment. May play a key role in intracellular
signaling during synaptogenesis and in synaptic function. Involved
in the negative regulation of receptor tyrosine kinase-coupled
cellular responses induced by cell adhesion, growth factors or
insulin. Mediates negative regulation of phagocytosis, mast cell
activation and dendritic cell activation. CD47 binding prevents
maturation of immature dendritic cells and inhibits cytokine
production by mature dendritic cells. May play a role in the
release of nitric oxide by macrophages (By similarity).
{ECO:0000250, ECO:0000269|PubMed:9271230}.
-!- SUBUNIT: Binds PTPN11 when tyrosine-phosphorylated, except in
macrophages, where it primarily binds PTPN6. Binds GRB2 in vitro.
Binds FGR. Binds JAK2 irrespective of its phosphorylation status
and forms a stable complex. Binds SCAP1 and/or SCAP2. The
resulting complex recruits FYB1. Binds PTK2B (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q9R044:Nphs1; NbExp=2; IntAct=EBI-7945080, EBI-7945021;
Q06124:PTPN11 (xeno); NbExp=3; IntAct=EBI-7945080, EBI-297779;
P41499:Ptpn11; NbExp=3; IntAct=EBI-7945080, EBI-7180604;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Highly expressed in brain, spleen, lung, liver
and kidney. Detected at lower levels in heart. Highly expressed in
alveolar and peritoneal macrophages, and at lower levels in
dendritic cells. {ECO:0000269|PubMed:9712053,
ECO:0000269|PubMed:9774638}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:8943344,
ECO:0000269|PubMed:9774638}.
-!- PTM: Phosphorylated on tyrosine residues in response to insulin,
cell adhesion or epidermal growth factors. Dephosphorylated by
PTPN11. {ECO:0000269|PubMed:8943344, ECO:0000269|PubMed:9271230,
ECO:0000269|PubMed:9344856, ECO:0000269|PubMed:9535915}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; D85183; BAA12734.1; -; mRNA.
EMBL; D38468; BAA20368.1; -; mRNA.
EMBL; U62328; AAC68478.1; -; mRNA.
EMBL; AF055065; AAC18089.1; -; mRNA.
RefSeq; NP_037148.2; NM_013016.2.
RefSeq; XP_017446986.1; XM_017591497.1.
UniGene; Rn.53971; -.
ProteinModelPortal; P97710; -.
SMR; P97710; -.
BioGrid; 247560; 1.
IntAct; P97710; 4.
MINT; P97710; -.
STRING; 10116.ENSRNOP00000006408; -.
CarbonylDB; P97710; -.
iPTMnet; P97710; -.
PhosphoSitePlus; P97710; -.
UniCarbKB; P97710; -.
PaxDb; P97710; -.
PeptideAtlas; P97710; -.
PRIDE; P97710; -.
Ensembl; ENSRNOT00000006408; ENSRNOP00000006408; ENSRNOG00000004763.
GeneID; 25528; -.
KEGG; rno:25528; -.
UCSC; RGD:3449; rat.
CTD; 140885; -.
RGD; 3449; Sirpa.
eggNOG; ENOG410IKYM; Eukaryota.
eggNOG; ENOG410YKK2; LUCA.
GeneTree; ENSGT00440000033339; -.
HOVERGEN; HBG056632; -.
InParanoid; P97710; -.
KO; K06551; -.
Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
Reactome; R-RNO-2172127; DAP12 interactions.
Reactome; R-RNO-391160; Signal regulatory protein family interactions.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:P97710; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000004763; Expressed in 10 organ(s), highest expression level in brain.
ExpressionAtlas; P97710; baseline and differential.
Genevisible; P97710; RN.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IDA:RGD.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07654; C1-set; 2.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 2.
SMART; SM00407; IGc1; 2.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
Reference proteome; Repeat; SH3-binding; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 31 {ECO:0000269|PubMed:9271230}.
CHAIN 32 509 Tyrosine-protein phosphatase non-receptor
type substrate 1.
/FTId=PRO_0000014943.
TOPO_DOM 32 373 Extracellular. {ECO:0000255}.
TRANSMEM 374 394 Helical. {ECO:0000255}.
TOPO_DOM 395 509 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 138 Ig-like V-type.
DOMAIN 150 248 Ig-like C1-type 1.
DOMAIN 255 349 Ig-like C1-type 2.
MOTIF 436 439 SH2-binding. {ECO:0000255}.
MOTIF 446 451 SH3-binding. {ECO:0000255}.
MOTIF 460 463 SH2-binding. {ECO:0000255}.
MOTIF 477 480 SH2-binding. {ECO:0000255}.
MOTIF 501 504 SH2-binding. {ECO:0000255}.
MOD_RES 436 436 Phosphotyrosine; by Tyr-kinases.
{ECO:0000255}.
MOD_RES 460 460 Phosphotyrosine; by Tyr-kinases.
{ECO:0000255}.
MOD_RES 477 477 Phosphotyrosine; by Tyr-kinases.
{ECO:0000269|PubMed:9535915}.
MOD_RES 501 501 Phosphotyrosine; by Tyr-kinases.
{ECO:0000269|PubMed:9535915}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PubMed:24090084}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 122 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 172 229 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 274 332 {ECO:0000255|PROSITE-ProRule:PRU00114}.
MUTAGEN 436 436 Y->F: Abolishes tyrosine phosphorylation
and PTPN11 binding; when associated with
F-460; F-477 and F-501.
{ECO:0000269|PubMed:9535915}.
MUTAGEN 460 460 Y->F: Abolishes tyrosine phosphorylation
and PTPN11 binding; when associated with
F-436; F-477 and F-501.
{ECO:0000269|PubMed:9535915}.
MUTAGEN 477 477 Y->F: Strongly reduces insulin-induced
tyrosine phosphorylation and PTPN11
binding. Abolishes tyrosine
phosphorylation and PTPN11 binding; when
associated with F-436; F-460 and F-501.
{ECO:0000269|PubMed:9535915}.
MUTAGEN 501 501 Y->F: Strongly reduces insulin-induced
tyrosine phosphorylation and PTPN11
binding. Abolishes tyrosine
phosphorylation and PTPN11 binding; when
associated with F-436; F-460 and F-477.
{ECO:0000269|PubMed:9535915}.
CONFLICT 8 8 P -> L (in Ref. 4). {ECO:0000305}.
CONFLICT 10 10 Missing (in Ref. 4). {ECO:0000305}.
CONFLICT 25 25 F -> I (in Ref. 3; AAC68478).
{ECO:0000305}.
CONFLICT 58 58 S -> C (in Ref. 4; AAC18089).
{ECO:0000305}.
CONFLICT 99 100 KR -> MP (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 162 162 G -> A (in Ref. 2; BAA20368).
{ECO:0000305}.
CONFLICT 189 189 D -> N (in Ref. 3; AAC68478).
{ECO:0000305}.
CONFLICT 205 205 N -> L (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 209 209 N -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 405 405 G -> F (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 416 416 E -> P (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 418 421 NARE -> EGQN (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 450 450 R -> E (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 499 499 Missing (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 509 AA; 55691 MW; 5BE1FE0A4DD429F4 CRC64;
MEPAGPAPGR LGPLLFCLLL SASCFCAGAS GKELKVTQAD KSVSVAAGDS ATLNCTVSSL
TPVGPIKWFK GEGQNRSPIY SFIGGEHFPR ITNVSDATKR NNMDFSICIS NVTPEDAGTY
YCVKFQKGIV EPDTEIKSGG GTTLYVLAKP SSPEVSGPDS RGSPGQTVNF TCKSYGFSPR
NITLKWLKDG KELSHLETTI SSKSNVSYNI SSTVSVKLSP EDIHSRVICE VAHVTLEGRP
LNGTANFSNI IRVSPTLKIT QQPLTPASQV NLTCQVQKFY PKALQLNWLE NGNLSRTDKP
EHFTDNRDGT YNYTSLFLVN SSAHREDVVF TCQVEHDSQP AITENHTVRA FAHSSSGGSM
ETIPDNNAYY NWNVFIGVGV ACALLVVLLM AALYLLRIKQ KKAKGSTSST RLHEPEKNAR
EITQIQDTND INDITYADLN LPKEKKPAPR VPEPNNHTEY ASIETGKLPR PEDTLTYADL
DMVHLNRAQP TPKPEPSFSE YASVQVQRK


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