LTBP3_MOUSE
ID LTBP3_MOUSE Reviewed; 1253 AA.
AC Q61810; F8VQ06; Q8BNQ6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 4.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Latent-transforming growth factor beta-binding protein 3;
DE Short=LTBP-3;
DE Flags: Precursor;
GN Name=Ltbp3;
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 [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RX PubMed=7730318; DOI=10.1074/jbc.270.17.10147;
RA Yin W., Smiley E., Germiller J., Mecham R.P., Florer J.B., Wenstrup R.J.,
RA Bonadio J.;
RT "Isolation of a novel latent transforming growth factor-beta binding
RT protein gene (LTBP-3).";
RL J. Biol. Chem. 270:10147-10160(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP INTERACTION WITH TGFB1.
RX PubMed=9602168; DOI=10.1016/s0167-4838(98)00003-x;
RA Yin W., Fang J., Smiley E., Bonadio J.;
RT "8-cysteine TGF-BP structural motifs are the site of covalent binding
RT between mouse LTBP-3, LTBP-2, and latent TGF-beta 1.";
RL Biochim. Biophys. Acta 1383:340-350(1998).
RN [5]
RP INTERACTION WITH TGFB1.
RX PubMed=12062452; DOI=10.1016/s0014-5793(02)02648-0;
RA Chen Y., Dabovic B., Annes J.P., Rifkin D.B.;
RT "Latent TGF-beta binding protein-3 (LTBP-3) requires binding to TGF-beta
RT for secretion.";
RL FEBS Lett. 517:277-280(2002).
RN [6]
RP REVIEW.
RX PubMed=10743502; DOI=10.1016/s1359-6101(99)00010-6;
RA Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.;
RT "Latent transforming growth factor-beta binding proteins (LTBPs)
RT -- structural extracellular matrix proteins for targeting TGF-beta
RT action.";
RL Cytokine Growth Factor Rev. 10:99-117(1999).
RN [7]
RP REVIEW.
RX PubMed=11104663; DOI=10.1042/bj3520601;
RA Oklu R., Hesketh R.;
RT "The latent transforming growth factor beta binding protein (LTBP)
RT family.";
RL Biochem. J. 352:601-610(2000).
CC -!- FUNCTION: Key regulator of transforming growth factor beta (TGFB1,
CC TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in
CC a latent state during storage in extracellular space. Associates
CC specifically via disulfide bonds with the Latency-associated peptide
CC (LAP), which is the regulatory chain of TGF-beta, and regulates
CC integrin-dependent activation of TGF-beta.
CC {ECO:0000303|PubMed:10743502, ECO:0000303|PubMed:11104663}.
CC -!- SUBUNIT: Forms part of the large latent transforming growth factor beta
CC (TGFB1) precursor complex; removal is essential for activation of
CC complex. Interacts with EFEMP2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NS15, ECO:0000269|PubMed:12062452,
CC ECO:0000269|PubMed:9602168}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NS15}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:Q9NS15}. Note=Secretion occurs after
CC coexpression with TGFB1 and requires complexing with 'Cys-33' of the
CC TGFB1 propeptide. {ECO:0000250|UniProtKB:Q9NS15}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61810-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61810-2; Sequence=VSP_009242, VSP_009243;
CC -!- DEVELOPMENTAL STAGE: At 8.5-9.0 dpc highly expressed in liver.
CC Significant expression was also seen in the developing central nervous,
CC somites and cardiovascular tissue. At 13.5-16.5 dpc expression was seen
CC in osteoblasts, respiratory epithelial cells, and nephrons and dermal
CC connective tissue. {ECO:0000269|PubMed:7730318}.
CC -!- PTM: Contains hydroxylated asparagine residues.
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- PTM: Two intrachain disulfide bonds from the TB3 domain are rearranged
CC upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide,
CC anchoring it to the extracellular matrix.
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB53015.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB53015.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L40459; AAB53015.1; ALT_SEQ; mRNA.
DR EMBL; AK080869; BAC38053.1; -; mRNA.
DR EMBL; AC134563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37891.1; -. [Q61810-1]
DR PIR; A57293; A57293.
DR RefSeq; NP_032546.2; NM_008520.2. [Q61810-1]
DR AlphaFoldDB; Q61810; -.
DR BioGRID; 201221; 7.
DR DIP; DIP-48641N; -.
DR IntAct; Q61810; 2.
DR STRING; 10090.ENSMUSP00000080214; -.
DR CarbonylDB; Q61810; -.
DR GlyGen; Q61810; 5 sites.
DR iPTMnet; Q61810; -.
DR PhosphoSitePlus; Q61810; -.
DR MaxQB; Q61810; -.
DR PaxDb; Q61810; -.
DR PeptideAtlas; Q61810; -.
DR PRIDE; Q61810; -.
DR ProteomicsDB; 290185; -. [Q61810-1]
DR ProteomicsDB; 290186; -. [Q61810-2]
DR ProteomicsDB; 346857; -.
DR Antibodypedia; 70903; 9 antibodies from 9 providers.
DR DNASU; 16998; -.
DR Ensembl; ENSMUST00000081496; ENSMUSP00000080214; ENSMUSG00000024940. [Q61810-1]
DR GeneID; 16998; -.
DR KEGG; mmu:16998; -.
DR CTD; 4054; -.
DR MGI; MGI:1101355; Ltbp3.
DR VEuPathDB; HostDB:ENSMUSG00000024940; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160285; -.
DR HOGENOM; CLU_001884_1_0_1; -.
DR InParanoid; Q61810; -.
DR OMA; PCGPGKG; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q61810; -.
DR TreeFam; TF317514; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR BioGRID-ORCS; 16998; 1 hit in 58 CRISPR screens.
DR ChiTaRS; Ltbp3; mouse.
DR PRO; PR:Q61810; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q61810; protein.
DR Bgee; ENSMUSG00000024940; Expressed in ciliary body and 291 other tissues.
DR ExpressionAtlas; Q61810; baseline and differential.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; ISA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0046849; P:bone remodeling; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0048251; P:elastic fiber assembly; IBA:GO_Central.
DR GO; GO:0060430; P:lung saccule development; IMP:MGI.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IMP:MGI.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:MGI.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:MGI.
DR GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; ISO:MGI.
DR GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0036363; P:transforming growth factor beta activation; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR Gene3D; 3.90.290.10; -; 4.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR Pfam; PF07645; EGF_CA; 11.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00179; EGF_CA; 13.
DR SUPFAM; SSF57184; SSF57184; 3.
DR SUPFAM; SSF57581; SSF57581; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 10.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 12.
DR PROSITE; PS01187; EGF_CA; 11.
DR PROSITE; PS51364; TB; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Growth factor binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..1253
FT /note="Latent-transforming growth factor beta-binding
FT protein 3"
FT /id="PRO_0000007647"
FT DOMAIN 106..138
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 274..328
FT /note="TB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 352..392
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 400..452
FT /note="TB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 571..612
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 613..656
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 657..699
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 741..781
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 782..822
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 823..861
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 863..905
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 914..968
FT /note="TB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 990..1032
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1033..1072
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1086..1136
FT /note="TB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1204..1231
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 244..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 114..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 128..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 276..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 286..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 301..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 356..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 362..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 378..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 402..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 412..437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 426..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 427..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 575..587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 582..596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 598..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 617..629
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 622..638
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 661..673
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 667..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 684..698
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 745..756
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 751..765
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 767..780
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 786..797
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 792..806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 808..821
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 827..838
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 833..847
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 849..861
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 867..880
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 874..889
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 891..904
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 916..939
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 926..951
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 926
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT DISULFID 940..956
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 941..968
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 951
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT DISULFID 994..1007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1002..1016
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1018..1031
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1037..1048
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1043..1057
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1059..1072
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1113..1127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1114..1136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1208..1223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1218..1232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 863..884
FT /note="DIDECSQDPGLCLPHGACENLQ -> GMRSWPGILKGEAGQCDLFDTL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009242"
FT VAR_SEQ 885..1253
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009243"
FT CONFLICT 16
FT /note="R -> H (in Ref. 2; BAC38053)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="A -> G (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="Missing (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="E -> Q (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="G -> A (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="E -> Q (in Ref. 2; BAC38053)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="Q -> P (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="G -> V (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 361..363
FT /note="MCR -> NVC (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..389
FT /note="SRT -> LAA (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="Missing (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="T -> A (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="Q -> L (in Ref. 1; AAB53015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1253 AA; 134363 MW; C773F38FD65F186E CRC64;
MPGPRGAAHG LAPAMRQAGA LGLLALLLLA LLGPGGGAEG GPAGERGTGG GGALARERFK
VVFAPVICKR TCLKGQCRDS CQQGSNMTLI GENGHSTDTL TGSGFRVVVC PLPCMNGGQC
SSRNQCLCPP DFTGRFCQVP AAGTGAGTGS SGPGLARTGA MSTGPLPPLA PEGESVASKH
AIYAVQVIAD PPGPGEGPPA QHAAFLVPLG PGQISAEVQA PPPVVNVRVH HPPEASVQVH
RIEGPNAEGP ASSQHLLPHP KPQHPRPPTQ KPLGRCFQDT LPKQPCGSNP LPGLTKQEDC
CGSIGTAWGQ SKCHKCPQLQ YTGVQKPGPV RGEVGADCPQ GYKRLNSTHC QDINECAMPG
MCRHGDCLNN PGSYRCVCPP GHSLGPSRTQ CIADKPEEKS LCFRLVSTEH QCQHPLTTRL
TRQLCCCSVG KAWGARCQRC PADGTAAFKE ICPAGKGYHI LTSHQTLTIQ GESDFSLFLH
PDGPPKPQQL PESPSRAPPL EDTEEERGVT MDPPVSEERS VQQSHPTTTT SPPRPYPELI
SRPSPPTFHR FLPDLPPSRS AVEIAPTQVT ETDECRLNQN ICGHGQCVPG PSDYSCHCNA
GYRSHPQHRY CVDVNECEAE PCGPGKGICM NTGGSYNCHC NRGYRLHVGA GGRSCVDLNE
CTKPHLCGDG GFCINFPGHY KCNCYPGYRL KASRPPICED IDECRDPSTC PDGKCENKPG
SFKCIACQPG YRSQGGGACR DVNECSEGTP CSPGWCENLP GSYRCTCAQG YEPAQDGLSC
IDVDECEAGK VCQDGICTNT PGSFQCQCLS GYHLSRDRSR CEDIDECDFP AACIGGDCIN
TNGSYRCLCP QGHRLVGGRK CQDIDECSQD PGLCLPHGAC ENLQGSYVCV CDEGFTLTQD
QHGCEEVEQP HHKKECYLNF DDTVFCDSVL ATNVTQQECC CSLGAGWGDH CEIYPCPVYS
SAEFHSLCPD GKGYTQDNNI VNYGIPAHRD IDECILFGAE ICKEGKCVNT QPGYECYCKQ
GFYYDGNLLE CVDVDECLDE SNCRNGVCEN TRGGYRCACT PPAEYSPAQR QCLSPEEMEH
APERREVCWG QRGEDGMCMG PLAGPALTFD DCCCRQGRGW GTQCRPCPPR GTGSQCPTSQ
SESNSFWDTS PLLLGKSPRD EDSSEEDSDE CRCVSGRCVP RPGGAVCECP GGFQLDASRA
RCVDIDECRE LNQRGLLCKS ERCVNTSGSF RCVCKAGFTR SRPHGACVPQ RRR
