TSP2_HUMAN
ID TSP2_HUMAN Reviewed; 1172 AA.
AC P35442; A6H8N1; A7E232; Q5RI52;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Thrombospondin-2;
DE Flags: Precursor;
GN Name=THBS2; Synonyms=TSP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8406456; DOI=10.1006/geno.1993.1308;
RA Labell T.L., Byers P.H.;
RT "Sequence and characterization of the complete human thrombospondin 2 cDNA:
RT potential regulatory role for the 3' untranslated region.";
RL Genomics 17:225-229(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 560-1172.
RC TISSUE=Fibroblast;
RX PubMed=1559694; DOI=10.1016/0888-7543(92)90430-z;
RA Labell T.L., McGookey Milewicz D.J., Disteche C.M., Byers P.H.;
RT "Thrombospondin II: partial cDNA sequence, chromosome location, and
RT expression of a second member of the thrombospondin gene family in
RT humans.";
RL Genomics 12:421-429(1992).
RN [7]
RP INTERACTION WITH THBS1 AND THBS2.
RX PubMed=1371676; DOI=10.1016/0006-291x(92)91860-s;
RA Asch A.S., Silbiger S., Heimer E., Nachman R.L.;
RT "Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding.";
RL Biochem. Biophys. Res. Commun. 182:1208-1217(1992).
RN [8]
RP DISULFIDE BONDS IN THROMBOSPONDIN DOMAIN.
RX PubMed=11590138; DOI=10.1074/jbc.m104218200;
RA Misenheimer T.M., Hahr A.J., Harms A.C., Annis D.S., Mosher D.F.;
RT "Disulfide connectivity of recombinant C-terminal region of human
RT thrombospondin 2.";
RL J. Biol. Chem. 276:45882-45887(2001).
RN [9]
RP INVOLVEMENT IN SUSCEPTIBILITY TO IDD, AND TISSUE SPECIFICITY.
RX PubMed=18455130; DOI=10.1016/j.ajhg.2008.03.013;
RA Hirose Y., Chiba K., Karasugi T., Nakajima M., Kawaguchi Y., Mikami Y.,
RA Furuichi T., Mio F., Miyake A., Miyamoto T., Ozaki K., Takahashi A.,
RA Mizuta H., Kubo T., Kimura T., Tanaka T., Toyama Y., Ikegawa S.;
RT "A functional polymorphism in THBS2 that affects alternative splicing and
RT MMP binding is associated with lumbar-disc herniation.";
RL Am. J. Hum. Genet. 82:1122-1129(2008).
RN [10]
RP FUNCTION.
RX PubMed=20714802; DOI=10.1007/s10549-010-1085-7;
RA Koch M., Hussein F., Woeste A., Grundker C., Frontzek K., Emons G.,
RA Hawighorst T.;
RT "CD36-mediated activation of endothelial cell apoptosis by an N-terminal
RT recombinant fragment of thrombospondin-2 inhibits breast cancer growth and
RT metastasis in vivo.";
RL Breast Cancer Res. Treat. 128:337-346(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 551-1172 IN COMPLEX WITH CALCIUM
RP IONS, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-584; ASN-710 AND ASN-1069.
RX PubMed=16186819; DOI=10.1038/nsmb997;
RA Carlson C.B., Bernstein D.A., Annis D.S., Misenheimer T.M., Hannah B.L.,
RA Mosher D.F., Keck J.L.;
RT "Structure of the calcium-rich signature domain of human thrombospondin-
RT 2.";
RL Nat. Struct. Mol. Biol. 12:910-914(2005).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 551-1172, AND MUTAGENESIS OF
RP ASN-702.
RX PubMed=18499674; DOI=10.1074/jbc.m800223200;
RA Carlson C.B., Liu Y., Keck J.L., Mosher D.F.;
RT "Influences of the N700S thrombospondin-1 polymorphism on protein structure
RT and stability.";
RL J. Biol. Chem. 283:20069-20076(2008).
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions. Ligand for CD36 mediating antiangiogenic
CC properties. {ECO:0000269|PubMed:20714802}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Interacts (via the TSP type I
CC repeats) with CD36; the interaction conveys an antiangiogenic effect.
CC Interacts (via the TSP type I repeats) with HRG; the interaction blocks
CC the antiangiogenic effect of THBS2 with CD36 (By similarity). Can bind
CC to fibrinogen, fibronectin, laminin and type V collagen. {ECO:0000250,
CC ECO:0000269|PubMed:11590138, ECO:0000269|PubMed:1371676,
CC ECO:0000269|PubMed:16186819}.
CC -!- INTERACTION:
CC P35442; P54290: Cacna2d1; Xeno; NbExp=2; IntAct=EBI-2466249, EBI-2466294;
CC -!- TISSUE SPECIFICITY: High expression in invertebral disk tissue.
CC {ECO:0000269|PubMed:18455130}.
CC -!- DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common
CC musculo-skeletal disorder caused by degeneration of intervertebral
CC disks of the lumbar spine. It results in low-back pain and unilateral
CC leg pain. {ECO:0000269|PubMed:18455130}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/THBS2ID42549ch6q27.html";
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DR EMBL; L12350; AAA03703.1; -; mRNA.
DR EMBL; M81339; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK292429; BAF85118.1; -; mRNA.
DR EMBL; BX322234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47455.1; -; Genomic_DNA.
DR EMBL; BC146676; AAI46677.1; -; mRNA.
DR EMBL; BC150175; AAI50176.1; -; mRNA.
DR CCDS; CCDS34574.1; -.
DR PIR; A47379; TSHUP2.
DR RefSeq; NP_003238.2; NM_003247.3.
DR PDB; 1YO8; X-ray; 2.60 A; A=551-1172.
DR PDB; 2RHP; X-ray; 2.90 A; A=551-1172.
DR PDBsum; 1YO8; -.
DR PDBsum; 2RHP; -.
DR AlphaFoldDB; P35442; -.
DR SMR; P35442; -.
DR BioGRID; 112916; 22.
DR ComplexPortal; CPX-1788; Thrombospondin 2 complex.
DR CORUM; P35442; -.
DR IntAct; P35442; 12.
DR STRING; 9606.ENSP00000355751; -.
DR GlyConnect; 1805; 24 N-Linked glycans (4 sites).
DR GlyGen; P35442; 7 sites, 23 N-linked glycans (4 sites).
DR iPTMnet; P35442; -.
DR PhosphoSitePlus; P35442; -.
DR BioMuta; THBS2; -.
DR DMDM; 215273908; -.
DR CPTAC; CPTAC-1186; -.
DR EPD; P35442; -.
DR jPOST; P35442; -.
DR MassIVE; P35442; -.
DR MaxQB; P35442; -.
DR PaxDb; P35442; -.
DR PeptideAtlas; P35442; -.
DR PRIDE; P35442; -.
DR ProteomicsDB; 55062; -.
DR Antibodypedia; 33564; 254 antibodies from 26 providers.
DR DNASU; 7058; -.
DR Ensembl; ENST00000366787.7; ENSP00000355751.3; ENSG00000186340.17.
DR Ensembl; ENST00000617924.6; ENSP00000482784.1; ENSG00000186340.17.
DR Ensembl; ENST00000676498.1; ENSP00000504820.1; ENSG00000186340.17.
DR Ensembl; ENST00000676760.1; ENSP00000503020.1; ENSG00000186340.17.
DR GeneID; 7058; -.
DR KEGG; hsa:7058; -.
DR MANE-Select; ENST00000617924.6; ENSP00000482784.1; NM_003247.5; NP_003238.2.
DR UCSC; uc003qwt.5; human.
DR CTD; 7058; -.
DR DisGeNET; 7058; -.
DR GeneCards; THBS2; -.
DR HGNC; HGNC:11786; THBS2.
DR HPA; ENSG00000186340; Low tissue specificity.
DR MalaCards; THBS2; -.
DR MIM; 188061; gene.
DR MIM; 603932; phenotype.
DR neXtProt; NX_P35442; -.
DR OpenTargets; ENSG00000186340; -.
DR PharmGKB; PA36498; -.
DR VEuPathDB; HostDB:ENSG00000186340; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000157846; -.
DR HOGENOM; CLU_009257_0_0_1; -.
DR InParanoid; P35442; -.
DR OMA; PPVTCAN; -.
DR OrthoDB; 120983at2759; -.
DR PhylomeDB; P35442; -.
DR TreeFam; TF324917; -.
DR PathwayCommons; P35442; -.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; P35442; -.
DR SIGNOR; P35442; -.
DR BioGRID-ORCS; 7058; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; THBS2; human.
DR EvolutionaryTrace; P35442; -.
DR GeneWiki; THBS2; -.
DR GenomeRNAi; 7058; -.
DR Pharos; P35442; Tbio.
DR PRO; PR:P35442; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P35442; protein.
DR Bgee; ENSG00000186340; Expressed in pericardium and 188 other tissues.
DR ExpressionAtlas; P35442; baseline and differential.
DR Genevisible; P35442; HS.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
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; IPR024731; EGF_dom.
DR InterPro; IPR001791; Laminin_G.
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; IPR015455; TSP2.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR10199:SF10; PTHR10199:SF10; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00090; TSP_1; 3.
DR Pfam; PF02412; TSP_3; 6.
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 3D-structure; Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
KW Glycoprotein; Heparin-binding; Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1172
FT /note="Thrombospondin-2"
FT /id="PRO_0000035846"
FT DOMAIN 19..215
FT /note="Laminin G-like"
FT DOMAIN 318..375
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 381..431
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 437..492
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 494..549
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 549..589
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 648..692
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 693..728
FT /note="TSP type-3 1"
FT REPEAT 729..764
FT /note="TSP type-3 2"
FT REPEAT 765..787
FT /note="TSP type-3 3"
FT REPEAT 788..823
FT /note="TSP type-3 4"
FT REPEAT 824..846
FT /note="TSP type-3 5"
FT REPEAT 847..884
FT /note="TSP type-3 6"
FT REPEAT 885..920
FT /note="TSP type-3 7"
FT REPEAT 921..956
FT /note="TSP type-3 8"
FT DOMAIN 960..1172
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 19..232
FT /note="Heparin-binding"
FT /evidence="ECO:0000255"
FT REGION 843..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 928..930
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 871..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16186819"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16186819"
FT CARBOHYD 1069
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16186819"
FT DISULFID 266
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 270
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 393..425
FT /evidence="ECO:0000250"
FT DISULFID 397..430
FT /evidence="ECO:0000250"
FT DISULFID 408..415
FT /evidence="ECO:0000250"
FT DISULFID 449..486
FT /evidence="ECO:0000250"
FT DISULFID 453..491
FT /evidence="ECO:0000250"
FT DISULFID 464..476
FT /evidence="ECO:0000250"
FT DISULFID 506..543
FT /evidence="ECO:0000250"
FT DISULFID 510..548
FT /evidence="ECO:0000250"
FT DISULFID 521..533
FT /evidence="ECO:0000250"
FT DISULFID 553..564
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 558..574
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 577..588
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 594..610
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 601..619
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 622..646
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 652..665
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 659..678
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 680..691
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 707..715
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 720..740
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 756..776
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 779..799
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 815..835
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 838..858
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 876..896
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 912..932
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT DISULFID 948..1169
FT /evidence="ECO:0000269|PubMed:16186819,
FT ECO:0000269|PubMed:18499674, ECO:0007744|PDB:1YO8,
FT ECO:0007744|PDB:2RHP"
FT VARIANT 133
FT /note="T -> S (in dbSNP:rs36088849)"
FT /id="VAR_045842"
FT VARIANT 375
FT /note="L -> F (in dbSNP:rs35404985)"
FT /id="VAR_045843"
FT MUTAGEN 702
FT /note="N->S: Alters protein stability."
FT /evidence="ECO:0000269|PubMed:18499674"
FT CONFLICT 2
FT /note="V -> A (in Ref. 5; AAI50176)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..173
FT /note="DSF -> GPV (in Ref. 1; AAA03703)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="S -> F (in Ref. 1; AAA03703)"
FT /evidence="ECO:0000305"
FT CONFLICT 1111
FT /note="R -> G (in Ref. 5; AAI46677)"
FT /evidence="ECO:0000305"
FT HELIX 552..555
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 593..596
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 614..619
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 637..640
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 651..655
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 663..667
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 673..680
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 684..693
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 697..700
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 706..710
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 734..736
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 738..740
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 746..749
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 755..758
FT /evidence="ECO:0007829|PDB:2RHP"
FT STRAND 767..772
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 774..776
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 793..795
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 797..799
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 805..808
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 810..812
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 829..831
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 833..835
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 851..854
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 856..858
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 866..869
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 871..873
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 894..896
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 903..905
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 907..909
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 911..914
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 926..928
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 930..932
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 939..941
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 943..945
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 960..968
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 971..973
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 979..982
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 983..985
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 987..990
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 995..1016
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1024..1033
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1036..1045
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1053..1055
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1061..1069
FT /evidence="ECO:0007829|PDB:1YO8"
FT HELIX 1076..1083
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1084..1086
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 1089..1091
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1092..1097
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1110..1116
FT /evidence="ECO:0007829|PDB:1YO8"
FT TURN 1118..1120
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1122..1129
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1132..1136
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1139..1141
FT /evidence="ECO:0007829|PDB:2RHP"
FT STRAND 1148..1156
FT /evidence="ECO:0007829|PDB:1YO8"
FT STRAND 1159..1169
FT /evidence="ECO:0007829|PDB:1YO8"
SQ SEQUENCE 1172 AA; 129991 MW; 415BF376F4669F6A CRC64;
MVWRLVLLAL WVWPSTQAGH QDKDTTFDLF SISNINRKTI GAKQFRGPDP GVPAYRFVRF
DYIPPVNADD LSKITKIMRQ KEGFFLTAQL KQDGKSRGTL LALEGPGLSQ RQFEIVSNGP
ADTLDLTYWI DGTRHVVSLE DVGLADSQWK NVTVQVAGET YSLHVGCDLI DSFALDEPFY
EHLQAEKSRM YVAKGSARES HFRGLLQNVH LVFENSVEDI LSKKGCQQGQ GAEINAISEN
TETLRLGPHV TTEYVGPSSE RRPEVCERSC EELGNMVQEL SGLHVLVNQL SENLKRVSND
NQFLWELIGG PPKTRNMSAC WQDGRFFAEN ETWVVDSCTT CTCKKFKTIC HQITCPPATC
ASPSFVEGEC CPSCLHSVDG EEGWSPWAEW TQCSVTCGSG TQQRGRSCDV TSNTCLGPSI
QTRACSLSKC DTRIRQDGGW SHWSPWSSCS VTCGVGNITR IRLCNSPVPQ MGGKNCKGSG
RETKACQGAP CPIDGRWSPW SPWSACTVTC AGGIRERTRV CNSPEPQYGG KACVGDVQER
QMCNKRSCPV DGCLSNPCFP GAQCSSFPDG SWSCGSCPVG FLGNGTHCED LDECALVPDI
CFSTSKVPRC VNTQPGFHCL PCPPRYRGNQ PVGVGLEAAK TEKQVCEPEN PCKDKTHNCH
KHAECIYLGH FSDPMYKCEC QTGYAGDGLI CGEDSDLDGW PNLNLVCATN ATYHCIKDNC
PHLPNSGQED FDKDGIGDAC DDDDDNDGVT DEKDNCQLLF NPRQADYDKD EVGDRCDNCP
YVHNPAQIDT DNNGEGDACS VDIDGDDVFN ERDNCPYVYN TDQRDTDGDG VGDHCDNCPL
VHNPDQTDVD NDLVGDQCDN NEDIDDDGHQ NNQDNCPYIS NANQADHDRD GQGDACDPDD
DNDGVPDDRD NCRLVFNPDQ EDLDGDGRGD ICKDDFDNDN IPDIDDVCPE NNAISETDFR
NFQMVPLDPK GTTQIDPNWV IRHQGKELVQ TANSDPGIAV GFDEFGSVDF SGTFYVNTDR
DDDYAGFVFG YQSSSRFYVV MWKQVTQTYW EDQPTRAYGY SGVSLKVVNS TTGTGEHLRN
ALWHTGNTPG QVRTLWHDPR NIGWKDYTAY RWHLTHRPKT GYIRVLVHEG KQVMADSGPI
YDQTYAGGRL GLFVFSQEMV YFSDLKYECR DI
