PTPRC_RAT
ID PTPRC_RAT Reviewed; 1273 AA.
AC P04157;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase C;
DE EC=3.1.3.48;
DE AltName: Full=Leukocyte common antigen;
DE Short=L-CA;
DE AltName: Full=T200;
DE AltName: CD_antigen=CD45;
DE Flags: Precursor;
GN Name=Ptprc;
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 [LARGE SCALE MRNA] OF 1-147 (ISOFORM 4).
RG Amgen EST program;
RT "Amgen rat EST program.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-218 (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=2440674; DOI=10.1002/j.1460-2075.1987.tb02362.x;
RA Barclay A.N., Jackson D.I., Willis A.C., Williams A.F.;
RT "Lymphocyte specific heterogeneity in the rat leucocyte common antigen
RT (T200) is due to differences in polypeptide sequences near the NH2-
RT terminus.";
RL EMBO J. 6:1259-1264(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-1273 (ISOFORMS 1; 3; 4 AND 5).
RA Barclay A.N., Jackson D.I., Willis A.C., Williams A.F.;
RL Submitted (MAY-1987) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 208-1255 (ISOFORM 1).
RX PubMed=3158393; DOI=10.1016/0092-8674(85)90063-7;
RA Thomas M.L., Barclay A.N., Gagnon J., Williams A.F.;
RT "Evidence from cDNA clones that the rat leukocyte-common antigen (T200)
RT spans the lipid bilayer and contains a cytoplasmic domain of 80,000 Mr.";
RL Cell 41:83-93(1985).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-652; SER-963; SER-966;
RP SER-970; SER-973; SER-974; SER-978 AND SER-1209, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Protein tyrosine-protein phosphatase required for T-cell
CC activation through the antigen receptor. Acts as a positive regulator
CC of T-cell coactivation upon binding to DPP4. The first PTPase domain
CC has enzymatic activity, while the second one seems to affect the
CC substrate specificity of the first one. Upon T-cell activation,
CC recruits and dephosphorylates SKAP1 and FYN (By similarity).
CC Dephosphorylates LYN, and thereby modulates LYN activity (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with SKAP1. Interacts with DPP4; the interaction is
CC enhanced in an interleukin-12-dependent manner in activated
CC lymphocytes. Binds GANAB and PRKCSH (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08575};
CC Single-pass type I membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000250|UniProtKB:P08575}. Note=Colocalized with DPP4 in membrane
CC rafts. {ECO:0000250|UniProtKB:P08575}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=L-CA variant 4;
CC IsoId=P04157-1; Sequence=Displayed;
CC Name=2; Synonyms=L-CA variant 1;
CC IsoId=P04157-2; Sequence=VSP_005167;
CC Name=3; Synonyms=L-CA variant 2;
CC IsoId=P04157-3; Sequence=VSP_005166;
CC Name=4; Synonyms=L-CA variant 3;
CC IsoId=P04157-4; Sequence=VSP_005165, VSP_005168;
CC Name=5;
CC IsoId=P04157-5; Sequence=VSP_026163;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are found in thymocyte and
CC lymph node. Isoform 4 and isoform 3 are found in the lymph nod.
CC -!- DOMAIN: The first PTPase domain interacts with SKAP1. {ECO:0000250}.
CC -!- PTM: Heavily N- and O-glycosylated.
CC -!- PTM: The cytoplasmic domain contains potential phosphorylation sites.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 1/6 subfamily. {ECO:0000305}.
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DR EMBL; CB793707; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Y00065; CAA68272.1; -; mRNA.
DR EMBL; Y00065; CAA68273.1; -; mRNA.
DR EMBL; Y00065; CAA68274.1; -; mRNA.
DR EMBL; Y00065; CAA68275.1; -; mRNA.
DR EMBL; M25820; AAA41518.1; -; mRNA.
DR EMBL; M25821; AAA41519.1; -; mRNA.
DR EMBL; M25822; AAA41520.1; -; mRNA.
DR EMBL; M25823; AAA41521.1; -; mRNA.
DR PIR; A45854; A45854.
DR RefSeq; NP_001103357.1; NM_001109887.2. [P04157-4]
DR RefSeq; NP_001103358.1; NM_001109888.2. [P04157-5]
DR RefSeq; NP_001103359.1; NM_001109889.2. [P04157-3]
DR RefSeq; NP_001103360.1; NM_001109890.2. [P04157-2]
DR RefSeq; NP_612516.2; NM_138507.3. [P04157-1]
DR RefSeq; XP_006249972.1; XM_006249910.2. [P04157-1]
DR PDB; 5FN8; X-ray; 2.45 A; A/B=357-546.
DR PDBsum; 5FN8; -.
DR AlphaFoldDB; P04157; -.
DR SMR; P04157; -.
DR BioGRID; 246829; 1.
DR IntAct; P04157; 2.
DR MINT; P04157; -.
DR STRING; 10116.ENSRNOP00000063859; -.
DR GlyGen; P04157; 16 sites.
DR iPTMnet; P04157; -.
DR PhosphoSitePlus; P04157; -.
DR PaxDb; P04157; -.
DR PRIDE; P04157; -.
DR Ensembl; ENSRNOT00000060292; ENSRNOP00000057042; ENSRNOG00000000655. [P04157-3]
DR Ensembl; ENSRNOT00000064785; ENSRNOP00000063859; ENSRNOG00000000655. [P04157-1]
DR GeneID; 24699; -.
DR KEGG; rno:24699; -.
DR UCSC; RGD:3451; rat. [P04157-1]
DR CTD; 5788; -.
DR RGD; 3451; Ptprc.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000159457; -.
DR HOGENOM; CLU_001645_2_1_1; -.
DR InParanoid; P04157; -.
DR OMA; IFRKCFH; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P04157; -.
DR TreeFam; TF351829; -.
DR Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains.
DR Reactome; R-RNO-416700; Other semaphorin interactions.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P04157; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000000655; Expressed in spleen and 19 other tissues.
DR Genevisible; P04157; RN.
DR GO; GO:0032059; C:bleb; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; TAS:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0098857; C:membrane microdomain; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0030506; F:ankyrin binding; ISO:RGD.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0019887; F:protein kinase regulator activity; TAS:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IGI:ARUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0030507; F:spectrin binding; ISO:RGD.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:RGD.
DR GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048539; P:bone marrow development; ISO:RGD.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:RGD.
DR GO; GO:0044770; P:cell cycle phase transition; ISO:RGD.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0001779; P:natural killer cell differentiation; ISO:RGD.
DR GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; ISO:RGD.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0045060; P:negative thymic T cell selection; ISO:RGD.
DR GO; GO:0044855; P:plasma membrane raft distribution; ISO:RGD.
DR GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; ISO:RGD.
DR GO; GO:0050857; P:positive regulation of antigen receptor-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1905451; P:positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; ISO:RGD.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISO:RGD.
DR GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; ISO:RGD.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; ISO:RGD.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:RGD.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:1903615; P:positive regulation of protein tyrosine phosphatase activity; ISO:RGD.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:RGD.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; ISO:RGD.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0002711; P:positive regulation of T cell mediated immunity; ISO:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0045059; P:positive thymic T cell selection; ISO:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:2001236; P:regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:0002923; P:regulation of humoral immune response mediated by circulating immunoglobulin; ISO:RGD.
DR GO; GO:0032677; P:regulation of interleukin-8 production; ISO:RGD.
DR GO; GO:0050764; P:regulation of phagocytosis; ISO:RGD.
DR GO; GO:0061097; P:regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0010332; P:response to gamma radiation; IDA:RGD.
DR GO; GO:0048864; P:stem cell development; ISO:RGD.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IGI:ARUK-UCL.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR024739; PTP_recept_N.
DR InterPro; IPR016335; Ptprc.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF12567; CD45; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF12453; PTP_N; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PIRSF; PIRSF002004; Leukocyte_common_antigen; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Glycoprotein; Hydrolase;
KW Membrane; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT CHAIN 24..1273
FT /note="Receptor-type tyrosine-protein phosphatase C"
FT /id="PRO_0000025472"
FT TOPO_DOM 24..546
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..1273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 361..452
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 453..545
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 622..881
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 913..1196
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 45..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1219..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 822
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1137
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 790
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 822..828
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 866
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 652
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08575"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08575"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
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 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 30..161
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2440674"
FT /id="VSP_005167"
FT VAR_SEQ 30..120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2440674, ECO:0000303|Ref.3"
FT /id="VSP_005166"
FT VAR_SEQ 30..71
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:2440674, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.3"
FT /id="VSP_005165"
FT VAR_SEQ 72..161
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_026163"
FT VAR_SEQ 121..161
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:2440674, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.3"
FT /id="VSP_005168"
FT CONFLICT 56
FT /note="S -> R (in Ref. 3; AAA41518/AAA41521)"
FT /evidence="ECO:0000305"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:5FN8"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:5FN8"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:5FN8"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:5FN8"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:5FN8"
FT STRAND 470..475
FT /evidence="ECO:0007829|PDB:5FN8"
FT STRAND 486..493
FT /evidence="ECO:0007829|PDB:5FN8"
FT STRAND 496..510
FT /evidence="ECO:0007829|PDB:5FN8"
FT STRAND 518..526
FT /evidence="ECO:0007829|PDB:5FN8"
FT STRAND 535..540
FT /evidence="ECO:0007829|PDB:5FN8"
SQ SEQUENCE 1273 AA; 143269 MW; EDFA48100ACF2CB2 CRC64;
MYLWLKLLAF SLALLGPEVF VTGQGTTDDG LDTTEIVLLP QTDPLPARTT EFTPPSISER
GNGSSETTYL PGFSSTLMPH LTPQPDSQTP SARGADTQTL SSQADLTTLT AAPSGETDPP
GVPEESTVPE TFPGGTPILA RNSTAPSPTH TSNVSTTDIS SGANLTTPAP STLGFASNTT
TSTEIATPQT KPSCDEKFGN VTVRYIYDDS SKNFNANLEG DKKPKCEYTD CEKELKNLPE
CSQKNVTLSN GSCTPDKIIN LDVPPGTHNF NLTNCTPDIE ANTSICLEWK IKNKFTCDIQ
KISYNFRCTP EMKTFALDKH GTLWLHNLTV RTNYTCAAEV LYNNVILLKQ DRRVQTDFGT
PEMLPHVQCK NSTNSTTLVS WAEPASKHHG YILCYKKTPS EKCENLANDV NSFEVKNLRP
YTEYTVSLFA YVIGRVQRNG PAKDCNFRTK AARPGKVNGM KTSRASDNSI NVTCNSPYEI
NGPEARYILE VKSGGSLVKT FNQSTCKFVV DNLYYSTDYE FLVYFYNGEY LGDPEIKPQS
TSYNSKALII FLVFLIIVTS IALLVVLYKI YDLRKKRSSN LDEQQELVER DEEKQLINVD
PIHSDLLLET YKRKIADEGR LFLAEFQSIP RVFSKFPIKD ARKSQNQNKN RYVDILPYDY
NRVELSEING DAGSTYINAS YIDGFKEPRK YIAAQGPRDE TVDDFWKMIW EQKATVIVMV
TRCEEGNRNK CAEYWPCMEE GTRTFRDVVV TINDHKRCPD YIIQKLSIAH KKEKATGREV
THIQFTSWPD HGVPEDPHLL LKLRRRVNAF SNFFSGPIVV HCSAGVGRTG TYIGIDAMLE
SLEAEGKVDV YGYVVNLRRQ RCLMVQVEAQ YILIHQALVE YNQFGETEVN LSELHSCLQN
LKKRDPPSDP SPLEAEYQRL PSYRSWRTQH IGNQEENKKK NRSSNVVPYD FNRVPLKHEL
EMSKESEAES DESSDEDSDS EETSKYINAS FVMSYWKPEM MIAAQGPLKE TIGDFWQMIF
QRKVKVIVML TELMSGDQEV CAQYWGEGKQ TYGDMEVMLK DTNKSSAYIL RAFELRHSKR
KEPRTVYQYQ CTTWKGEELP AEPKDLVTLI QNIKQKLPKS GSEGMKYHKH ASILVHCRDG
SQQTGLFCAL FNLLESAETE DVVDVFQVVK SLRKARPGMV GSFEQYQFLY DIMASIYPTQ
NGQVKKANSQ DKIEFHNEVD GAKQDANCVQ PADPLNKAQE DSKEVGASEP ASGSEEPEHS
ANGPMSPALT PSS
