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