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SHPS1_RAT
ID   SHPS1_RAT               Reviewed;         509 AA.
AC   P97710; O08951; O70426; Q9QWI5;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type substrate 1;
DE            Short=SHP substrate 1;
DE            Short=SHPS-1;
DE   AltName: Full=Brain Ig-like molecule with tyrosine-based activation motifs;
DE            Short=Bit;
DE   AltName: Full=CD172 antigen-like family member A;
DE   AltName: Full=Inhibitory receptor SHPS-1;
DE   AltName: Full=Macrophage fusion receptor;
DE   AltName: Full=Macrophage membrane protein MFP150;
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=Bit, Mfr, Ptpns1, Shps1, Sirp;
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], PROTEIN SEQUENCE OF 42-60; 68-91; 128-137;
RP   150-158; 174-189; 192-202; 204-212; 218-237; 259-270; 279-282; 405-415 AND
RP   446-453, GLYCOSYLATION, PHOSPHORYLATION AT TYROSINE RESIDUES, AND
RP   INTERACTION WITH PTPN6 AND PTPN11.
RC   TISSUE=Fetal fibroblast;
RX   PubMed=8943344; DOI=10.1128/mcb.16.12.6887;
RA   Fujioka Y., Matozaki T., Noguchi T., Iwamatsu A., Yamao T., Takahashi N.,
RA   Tsuda M., Takada T., Kasuga M.;
RT   "A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-
RT   containing protein tyrosine phosphatase SHP-2 in response to mitogens and
RT   cell adhesion.";
RL   Mol. Cell. Biol. 16:6887-6899(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-48 AND 446-453,
RP   FUNCTION, AND PHOSPHORYLATION AT TYROSINE RESIDUES.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=9271230; DOI=10.1016/s0014-5793(97)00724-2;
RA   Sano S., Ohnishi H., Omori A., Hasegawa J., Kubota M.;
RT   "BIT, an immune antigen receptor-like molecule in the brain.";
RL   FEBS Lett. 411:327-334(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 99-107; 128-149; 192-217;
RP   405-417; 419-429; 446-467 AND 496-506, GLYCOSYLATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Fischer 344; TISSUE=Macrophage;
RX   PubMed=9774638; DOI=10.1128/mcb.18.11.6213;
RA   Saginario C., Sterling H., Beckers C., Kobayashi R., Solimena M., Ullu E.,
RA   Vignery A.;
RT   "MFR, a putative receptor mediating the fusion of macrophages.";
RL   Mol. Cell. Biol. 18:6213-6223(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-419, AND TISSUE SPECIFICITY.
RC   STRAIN=WAG/Rij; TISSUE=Alveolar macrophage;
RX   PubMed=9712053;
RA   Adams S., van der Laan L.J.W., Vernon-Wilson E., Renardel de Lavalette C.,
RA   Doepp E.A., Dijkstra C.D., Simmons D.L., van den Berg T.K.;
RT   "Signal-regulatory protein is selectively expressed by myeloid and neuronal
RT   cells.";
RL   J. Immunol. 161:1853-1859(1998).
RN   [5]
RP   PROTEIN SEQUENCE OF 192-203; 218-226 AND 297-307, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION IN RESPONSE TO EGF, AND INTERACTION WITH PTPN11.
RX   PubMed=9344856; DOI=10.1006/bbrc.1997.7489;
RA   Ochi F., Matozaki T., Noguchi T., Fujioka Y., Yamao T., Takada T.,
RA   Tsuda M., Takeda H., Fukunaga K., Okabayashi Y., Kasuga M.;
RT   "Epidermal growth factor stimulates the tyrosine phosphorylation of SHPS-1
RT   and association of SHPS-1 with SHP-2, a SH2 domain-containing protein
RT   tyrosine phosphatase.";
RL   Biochem. Biophys. Res. Commun. 239:483-487(1997).
RN   [7]
RP   PHOSPHORYLATION AT TYR-477 AND TYR-501, AND MUTAGENESIS OF TYR-436;
RP   TYR-460; TYR-477 AND TYR-501.
RX   PubMed=9535915; DOI=10.1074/jbc.273.15.9234;
RA   Takada T., Matozaki T., Takeda H., Fukunaga K., Noguchi T., Fujioka Y.,
RA   Okazaki I., Tsuda M., Yamao T., Ochi F., Kasuga M.;
RT   "Roles of the complex formation of SHPS-1 with SHP-2 in insulin-stimulated
RT   mitogen-activated protein kinase activation.";
RL   J. Biol. Chem. 273:9234-9242(1998).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93; ASN-169 AND ASN-312, 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: 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. May
CC       play a role in the release of nitric oxide by macrophages (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:9271230}.
CC   -!- SUBUNIT: Binds PTPN11 when tyrosine-phosphorylated, except in
CC       macrophages, where it primarily binds PTPN6. Binds GRB2 in vitro. Binds
CC       FGR. Binds JAK2 irrespective of its phosphorylation status and forms a
CC       stable complex. Binds SCAP1 and/or SCAP2. The resulting complex
CC       recruits FYB1. Binds PTK2B (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P97710; Q9R044: Nphs1; NbExp=2; IntAct=EBI-7945080, EBI-7945021;
CC       P97710; P41499: Ptpn11; NbExp=3; IntAct=EBI-7945080, EBI-7180604;
CC       P97710; Q06124: PTPN11; Xeno; NbExp=3; IntAct=EBI-7945080, EBI-297779;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, spleen, lung, liver and
CC       kidney. Detected at lower levels in heart. Highly expressed in alveolar
CC       and peritoneal macrophages, and at lower levels in dendritic cells.
CC       {ECO:0000269|PubMed:9712053, ECO:0000269|PubMed:9774638}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8943344,
CC       ECO:0000269|PubMed:9774638}.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to insulin, cell
CC       adhesion or epidermal growth factors. Dephosphorylated by PTPN11.
CC       {ECO:0000269|PubMed:8943344, ECO:0000269|PubMed:9271230,
CC       ECO:0000269|PubMed:9344856, ECO:0000269|PubMed:9535915}.
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DR   EMBL; D85183; BAA12734.1; -; mRNA.
DR   EMBL; D38468; BAA20368.1; -; mRNA.
DR   EMBL; U62328; AAC68478.1; -; mRNA.
DR   EMBL; AF055065; AAC18089.1; -; mRNA.
DR   RefSeq; NP_037148.2; NM_013016.2.
DR   RefSeq; XP_017446986.1; XM_017591497.1.
DR   AlphaFoldDB; P97710; -.
DR   SMR; P97710; -.
DR   BioGRID; 247560; 4.
DR   IntAct; P97710; 4.
DR   MINT; P97710; -.
DR   STRING; 10116.ENSRNOP00000006408; -.
DR   CarbonylDB; P97710; -.
DR   GlyGen; P97710; 13 sites, 24 N-linked glycans (3 sites).
DR   iPTMnet; P97710; -.
DR   PhosphoSitePlus; P97710; -.
DR   jPOST; P97710; -.
DR   PaxDb; P97710; -.
DR   PeptideAtlas; P97710; -.
DR   PRIDE; P97710; -.
DR   Ensembl; ENSRNOT00000006408; ENSRNOP00000006408; ENSRNOG00000004763.
DR   GeneID; 25528; -.
DR   KEGG; rno:25528; -.
DR   UCSC; RGD:3449; rat.
DR   CTD; 140885; -.
DR   RGD; 3449; Sirpa.
DR   eggNOG; ENOG502S1XD; Eukaryota.
DR   GeneTree; ENSGT00960000186656; -.
DR   InParanoid; P97710; -.
DR   Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-RNO-2172127; DAP12 interactions.
DR   Reactome; R-RNO-391160; Signal regulatory protein family interactions.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:P97710; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000004763; Expressed in frontal cortex and 20 other tissues.
DR   ExpressionAtlas; P97710; baseline and differential.
DR   Genevisible; P97710; RN.
DR   GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:RGD.
DR   GO; GO:0030695; F:GTPase regulator activity; IMP:ARUK-UCL.
DR   GO; GO:1990405; F:protein antigen binding; ISO:RGD.
DR   GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IPI:ARUK-UCL.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL.
DR   GO; GO:0045309; F:protein phosphorylated amino acid binding; ISO:RGD.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR   GO; GO:0016477; P:cell migration; IDA:RGD.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:ARUK-UCL.
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:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR   GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
DR   GO; GO:0097530; P:granulocyte migration; ISO:RGD.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR   GO; GO:0035696; P:monocyte extravasation; IMP:ARUK-UCL.
DR   GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; ISO:RGD.
DR   GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISO:RGD.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR   GO; GO:1903720; P:negative regulation of I-kappaB phosphorylation; ISO:RGD.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:RGD.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; ISO:RGD.
DR   GO; GO:0071641; P:negative regulation of macrophage inflammatory protein 1 alpha production; ISO:RGD.
DR   GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:RGD.
DR   GO; GO:0050765; P:negative regulation of phagocytosis; IMP:ARUK-UCL.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
DR   GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR   GO; GO:0006910; P:phagocytosis, recognition; ISO:RGD.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR   GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0032649; P:regulation of interferon-gamma production; ISO:RGD.
DR   GO; GO:0032651; P:regulation of interleukin-1 beta production; IMP:ARUK-UCL.
DR   GO; GO:0032675; P:regulation of interleukin-6 production; IMP:ARUK-UCL.
DR   GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IMP:ARUK-UCL.
DR   GO; GO:0032680; P:regulation of tumor necrosis factor production; IMP:ARUK-UCL.
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; IPR003006; Ig/MHC_CS.
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   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; SH3-binding; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000269|PubMed:9271230"
FT   CHAIN           32..509
FT                   /note="Tyrosine-protein phosphatase non-receptor type
FT                   substrate 1"
FT                   /id="PRO_0000014943"
FT   TOPO_DOM        32..373
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..509
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..138
FT                   /note="Ig-like V-type"
FT   DOMAIN          150..248
FT                   /note="Ig-like C1-type 1"
FT   DOMAIN          255..349
FT                   /note="Ig-like C1-type 2"
FT   REGION          441..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           436..439
FT                   /note="SH2-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           446..451
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           460..463
FT                   /note="SH2-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           477..480
FT                   /note="SH2-binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           501..504
FT                   /note="SH2-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        492..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         436
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         460
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         477
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000269|PubMed:9535915"
FT   MOD_RES         501
FT                   /note="Phosphotyrosine; by Tyr-kinases"
FT                   /evidence="ECO:0000269|PubMed:9535915"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
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        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        345
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        55..122
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        172..229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        274..332
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   MUTAGEN         436
FT                   /note="Y->F: Abolishes tyrosine phosphorylation and PTPN11
FT                   binding; when associated with F-460; F-477 and F-501."
FT                   /evidence="ECO:0000269|PubMed:9535915"
FT   MUTAGEN         460
FT                   /note="Y->F: Abolishes tyrosine phosphorylation and PTPN11
FT                   binding; when associated with F-436; F-477 and F-501."
FT                   /evidence="ECO:0000269|PubMed:9535915"
FT   MUTAGEN         477
FT                   /note="Y->F: Strongly reduces insulin-induced tyrosine
FT                   phosphorylation and PTPN11 binding. Abolishes tyrosine
FT                   phosphorylation and PTPN11 binding; when associated with F-
FT                   436; F-460 and F-501."
FT                   /evidence="ECO:0000269|PubMed:9535915"
FT   MUTAGEN         501
FT                   /note="Y->F: Strongly reduces insulin-induced tyrosine
FT                   phosphorylation and PTPN11 binding. Abolishes tyrosine
FT                   phosphorylation and PTPN11 binding; when associated with F-
FT                   436; F-460 and F-477."
FT                   /evidence="ECO:0000269|PubMed:9535915"
FT   CONFLICT        8
FT                   /note="P -> L (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        10
FT                   /note="Missing (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="F -> I (in Ref. 3; AAC68478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58
FT                   /note="S -> C (in Ref. 4; AAC18089)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99..100
FT                   /note="KR -> MP (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="G -> A (in Ref. 2; BAA20368)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="D -> N (in Ref. 3; AAC68478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="N -> L (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="N -> G (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        405
FT                   /note="G -> F (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="E -> P (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        418..421
FT                   /note="NARE -> EGQN (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        450
FT                   /note="R -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        499
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   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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