TSP1_MOUSE
ID TSP1_MOUSE Reviewed; 1170 AA.
AC P35441;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 180.
DE RecName: Full=Thrombospondin-1;
DE AltName: Full=Glycoprotein G {ECO:0000250|UniProtKB:P07996};
DE Flags: Precursor;
GN Name=Thbs1; Synonyms=Tsp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1774063; DOI=10.1016/0888-7543(91)90066-n;
RA Lawler J., Duquette M., Ferro P., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A.;
RT "Characterization of the murine thrombospondin gene.";
RL Genomics 11:587-600(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1371115; DOI=10.1016/s0021-9258(19)50727-x;
RA Laherty C.D., O'Rourke K., Wolf F.W., Katz R., Seldin M.F., Dixit V.M.;
RT "Characterization of mouse thrombospondin 2 sequence and expression during
RT cell growth and development.";
RL J. Biol. Chem. 267:3274-3281(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-490.
RX PubMed=2398070; DOI=10.1016/s0021-9258(17)46276-4;
RA Bornstein P., Alfi D., Devarayalu S., Framson P., Li P.;
RT "Characterization of the mouse thrombospondin gene and evaluation of the
RT role of the first intron in human gene expression.";
RL J. Biol. Chem. 265:16691-16698(1990).
RN [4]
RP PROTEIN SEQUENCE OF 19-37.
RX PubMed=8654563; DOI=10.1016/0014-5793(96)00460-7;
RA Chen H., Aeschlimann D., Nowlen J., Mosher D.F.;
RT "Expression and initial characterization of recombinant mouse
RT thrombospondin 1 and thrombospondin 3.";
RL FEBS Lett. 387:36-41(1996).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1067.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATF6.
RX PubMed=22682248; DOI=10.1016/j.cell.2012.03.050;
RA Lynch J.M., Maillet M., Vanhoutte D., Schloemer A., Sargent M.A.,
RA Blair N.S., Lynch K.A., Okada T., Aronow B.J., Osinska H., Prywes R.,
RA Lorenz J.N., Mori K., Lawler J., Robbins J., Molkentin J.D.;
RT "A thrombospondin-dependent pathway for a protective ER stress response.";
RL Cell 149:1257-1268(2012).
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions. Binds heparin. May play a role in dentinogenesis
CC and/or maintenance of dentin and dental pulp. Ligand for CD36 mediating
CC antiangiogenic properties (By similarity). Plays a role in ER stress
CC response, via its interaction with the activating transcription factor
CC 6 alpha (ATF6) which produces adaptive ER stress response factors.
CC {ECO:0000250, ECO:0000269|PubMed:22682248}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked (By similarity). Can bind to
CC fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-
CC V/beta-1, alpha-V/beta-3 and alpha-IIb/beta-3. Binds heparin. Interacts
CC (via the TSP type I repeats) with CD36; the interaction conveys an
CC antiangiogenic effect. Interacts (via the TSP type I repeats) with HRG;
CC the interaction blocks the antiangiogenic effect of THBS1 with CD36 (By
CC similarity). Interacts with ATF6 (via lumenal domain). Interacts with
CC FN1; this interaction is enhanced by TNFAIP6, which may act as a
CC bridging molecule between FN1 and THBS1. {ECO:0000250,
CC ECO:0000250|UniProtKB:P07996, ECO:0000269|PubMed:22682248}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07996}. Cell
CC surface {ECO:0000250|UniProtKB:P07996}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:P07996}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:22682248}. Sarcoplasmic reticulum
CC {ECO:0000269|PubMed:22682248}. Note=Secreted by thrombin-activated
CC platelets and binds to the cell surface in the presence of
CC extracellular Ca(2+) (By similarity). Incorporated into the
CC extracellular matrix of fibroblasts (By similarity). Also detected in
CC the endoplasmic reticulum and sarcoplasmic reticulum where it plays a
CC role in the ER stress response (PubMed:22682248).
CC {ECO:0000250|UniProtKB:P07996, ECO:0000269|PubMed:22682248}.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR EMBL; M62470; AAA50611.1; -; Genomic_DNA.
DR EMBL; M62450; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62451; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62452; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62453; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62454; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62455; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62456; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62457; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62458; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62459; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62460; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62461; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62462; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62463; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62464; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62465; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62466; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62467; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62468; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M62469; AAA50611.1; JOINED; Genomic_DNA.
DR EMBL; M87276; AAA53063.1; -; mRNA.
DR EMBL; J05606; AAA40431.1; -; Genomic_DNA.
DR EMBL; J05605; AAA40431.1; JOINED; Genomic_DNA.
DR PIR; A40558; A40558.
DR AlphaFoldDB; P35441; -.
DR SMR; P35441; -.
DR ComplexPortal; CPX-3022; Thrombospondin 1 complex.
DR CORUM; P35441; -.
DR IntAct; P35441; 6.
DR MINT; P35441; -.
DR STRING; 10090.ENSMUSP00000044903; -.
DR GlyConnect; 667; 1 N-Linked glycan (1 site).
DR GlyGen; P35441; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P35441; -.
DR PhosphoSitePlus; P35441; -.
DR SwissPalm; P35441; -.
DR CPTAC; non-CPTAC-3360; -.
DR jPOST; P35441; -.
DR MaxQB; P35441; -.
DR PaxDb; P35441; -.
DR PeptideAtlas; P35441; -.
DR PRIDE; P35441; -.
DR ProteomicsDB; 297728; -.
DR MGI; MGI:98737; Thbs1.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR InParanoid; P35441; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR ChiTaRS; Thbs1; mouse.
DR PRO; PR:P35441; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P35441; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005577; C:fibrinogen complex; ISO:MGI.
DR GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0070052; F:collagen V binding; ISO:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0070051; F:fibrinogen binding; ISO:MGI.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:MGI.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:UniProtKB.
DR GO; GO:0048514; P:blood vessel morphogenesis; IGI:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0071732; P:cellular response to nitric oxide; IMP:MGI.
DR GO; GO:0003197; P:endocardial cushion development; IGI:MGI.
DR GO; GO:0043652; P:engulfment of apoptotic cell; ISO:MGI.
DR GO; GO:0003417; P:growth plate cartilage development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0070487; P:monocyte aggregation; IMP:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:MGI.
DR GO; GO:0002581; P:negative regulation of antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0002605; P:negative regulation of dendritic cell antigen processing and presentation; ISO:MGI.
DR GO; GO:2001027; P:negative regulation of endothelial cell chemotaxis; ISO:MGI.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:MGI.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; ISO:MGI.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; ISO:MGI.
DR GO; GO:0010748; P:negative regulation of long-chain fatty acid import across plasma membrane; ISO:MGI.
DR GO; GO:0010751; P:negative regulation of nitric oxide mediated signal transduction; ISO:MGI.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; ISO:MGI.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IGI:MGI.
DR GO; GO:0018149; P:peptide cross-linking; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISO:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISO:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:MGI.
DR GO; GO:0043032; P:positive regulation of macrophage activation; ISO:MGI.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0009749; P:response to glucose; ISO:MGI.
DR GO; GO:0032026; P:response to magnesium ion; ISO:MGI.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0002040; P:sprouting angiogenesis; ISO:MGI.
DR Gene3D; 2.20.100.10; -; 3.
DR Gene3D; 4.10.1080.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR028499; Thrombospondin-1.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR10199:SF78; PTHR10199:SF78; 1.
DR Pfam; PF00090; TSP_1; 3.
DR Pfam; PF02412; TSP_3; 7.
DR Pfam; PF05735; TSP_C; 1.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00209; TSP1; 3.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF82895; SSF82895; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS51234; TSP3; 8.
DR PROSITE; PS51236; TSP_CTER; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Endoplasmic reticulum; Extracellular matrix; Glycoprotein;
KW Heparin-binding; Reference proteome; Repeat; Sarcoplasmic reticulum;
KW Secreted; Signal; Unfolded protein response.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:8654563"
FT CHAIN 19..1170
FT /note="Thrombospondin-1"
FT /id="PRO_0000035843"
FT DOMAIN 56..270
FT /note="Laminin G-like"
FT DOMAIN 316..373
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 379..429
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 435..490
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 492..547
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 547..587
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 646..690
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 691..726
FT /note="TSP type-3 1"
FT REPEAT 727..762
FT /note="TSP type-3 2"
FT REPEAT 763..785
FT /note="TSP type-3 3"
FT REPEAT 786..821
FT /note="TSP type-3 4"
FT REPEAT 822..844
FT /note="TSP type-3 5"
FT REPEAT 845..882
FT /note="TSP type-3 6"
FT REPEAT 883..918
FT /note="TSP type-3 7"
FT REPEAT 919..954
FT /note="TSP type-3 8"
FT DOMAIN 958..1170
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 47..95
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 840..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 926..928
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 883..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1067
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT DISULFID 171..232
FT /evidence="ECO:0000250"
FT DISULFID 270
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 274
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 391..423
FT /evidence="ECO:0000250"
FT DISULFID 395..428
FT /evidence="ECO:0000250"
FT DISULFID 406..413
FT /evidence="ECO:0000250"
FT DISULFID 447..484
FT /evidence="ECO:0000250"
FT DISULFID 451..489
FT /evidence="ECO:0000250"
FT DISULFID 462..474
FT /evidence="ECO:0000250"
FT DISULFID 504..541
FT /evidence="ECO:0000250"
FT DISULFID 508..546
FT /evidence="ECO:0000250"
FT DISULFID 519..531
FT /evidence="ECO:0000250"
FT DISULFID 551..562
FT /evidence="ECO:0000250"
FT DISULFID 556..572
FT /evidence="ECO:0000250"
FT DISULFID 575..586
FT /evidence="ECO:0000250"
FT DISULFID 592..608
FT /evidence="ECO:0000250"
FT DISULFID 599..617
FT /evidence="ECO:0000250"
FT DISULFID 620..644
FT /evidence="ECO:0000250"
FT DISULFID 650..663
FT /evidence="ECO:0000250"
FT DISULFID 657..676
FT /evidence="ECO:0000250"
FT DISULFID 678..689
FT /evidence="ECO:0000250"
FT DISULFID 705..713
FT /evidence="ECO:0000250"
FT DISULFID 718..738
FT /evidence="ECO:0000250"
FT DISULFID 754..774
FT /evidence="ECO:0000250"
FT DISULFID 777..797
FT /evidence="ECO:0000250"
FT DISULFID 813..833
FT /evidence="ECO:0000250"
FT DISULFID 836..856
FT /evidence="ECO:0000250"
FT DISULFID 874..894
FT /evidence="ECO:0000250"
FT DISULFID 910..930
FT /evidence="ECO:0000250"
FT DISULFID 946..1167
FT /evidence="ECO:0000250"
FT CONFLICT 1025
FT /note="F -> L (in Ref. 2; AAA53063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1170 AA; 129647 MW; 0443E493615E7F06 CRC64;
MELLRGLGVL FLLHMCGSNR IPESGGDNGV FDIFELIGGA RRGPGRRLVK GQDLSSPAFR
IENANLIPAV PDDKFQDLLD AVWADKGFIF LASLRQMKKT RGTLLAVERK DNTGQIFSVV
SNGKAGTLDL SLSLPGKQQV VSVEEALLAT GQWKSITLFV QEDRAQLYID CDKMESAELD
VPIQSIFTRD LASVARLRVA KGDVNDNFQG VLQNVRFVFG TTPEDILRNK GCSSSTNVLL
TLDNNVVNGS SPAIRTNYIG HKTKDLQAIC GLSCDELSSM VLELKGLRTI VTTLQDSIRK
VTEENRELVS ELKRPPLCFH NGVQYKNNEE WTVDSCTECH CQNSVTICKK VSCPIMPCSN
ATVPDGECCP RCWPSDSADD GWSPWSEWTS CSATCGNGIQ QRGRSCDSLN NRCEGSSVQT
RTCHIQECDK RFKQDGGWSH WSPWSSCSVT CGDGVITRIR LCNSPSPQMN GKPCEGEARE
TKACKKDACP INGGWGPWSP WDICSVTCGG GVQRRSRLCN NPTPQFGGKD CVGDVTENQV
CNKQDCPIDG CLSNPCFAGA KCTSYPDGSW KCGACPPGYS GNGIQCKDVD ECKEVPDACF
NHNGEHRCKN TDPGYNCLPC PPRFTGSQPF GRGVEHAMAN KQVCKPRNPC TDGTHDCNKN
AKCNYLGHYS DPMYRCECKP GYAGNGIICG EDTDLDGWPN ENLVCVANAT YHCKKDNCPN
LPNSGQEDYD KDGIGDACDD DDDNDKIPDD RDNCPFHYNP AQYDYDRDDV GDRCDNCPYN
HNPDQADTDK NGEGDACAVD IDGDGILNER DNCQYVYNVD QRDTDMDGVG DQCDNCPLEH
NPDQLDSDSD LIGDTCDNNQ DIDEDGHQNN LDNCPYVPNA NQADHDKDGK GDACDHDDDN
DGIPDDRDNC RLVPNPDQKD SDGDGRGDAC KDDFDHDNVP DIDDICPENF DISETDFRRF
QMIPLDPKGT SQNDPNWVVR HQGKELVQTV NCDPGLAVGY DEFNAVDFSG TFFINTERDD
DYAGFVFGYQ SSSRFYVVMW KQVTQSYWDT NPTRAQGYSG LSVKVVNSTT GPGEHLRNAL
WHTGNTPGQV RTLWHDPRHI GWKDFTAYRW RLSHRPKTGY IRVVMYEGKK IMADSGPIYD
KTYAGGRLGL FVFSQEMVFF SDMKYECRDS
