LTBP1_RAT
ID LTBP1_RAT Reviewed; 1712 AA.
AC Q00918;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Latent-transforming growth factor beta-binding protein 1;
DE Short=LTBP-1;
DE AltName: Full=Transforming growth factor beta-1-binding protein 1;
DE Short=TGF-beta-1-BP-1;
DE AltName: Full=Transforming growth factor beta-1-masking protein large subunit;
DE Flags: Precursor;
GN Name=Ltbp1;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2247454; DOI=10.1073/pnas.87.22.8835;
RA Tsuji T., Okada F., Yamaguchi K., Nakamura T.;
RT "Molecular cloning of the large subunit of transforming growth factor type
RT beta masking protein and expression of the mRNA in various rat tissues.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8835-8839(1990).
RN [2]
RP FUNCTION.
RX PubMed=7593177; DOI=10.1083/jcb.131.2.539;
RA Dallas S.L., Miyazono K., Skerry T.M., Mundy G.R., Bonewald L.F.;
RT "Dual role for the latent transforming growth factor-beta binding protein
RT in storage of latent TGF-beta in the extracellular matrix and as a
RT structural matrix protein.";
RL J. Cell Biol. 131:539-549(1995).
RN [3]
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 [4]
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).
RN [5]
RP IDENTIFICATION BY MASS 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: 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 (PubMed:7593177).
CC Associates specifically via disulfide bonds with the Latency-associated
CC peptide (LAP), which is the regulatory chain of TGF-beta, and regulates
CC integrin-dependent activation of TGF-beta (By similarity). Outcompeted
CC by LRRC32/GARP for binding to LAP regulatory chain of TGF-beta (By
CC similarity). {ECO:0000250|UniProtKB:Q14766,
CC ECO:0000269|PubMed:7593177}.
CC -!- SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with the
CC Latency-associated peptide chain (LAP) regulatory chain of TGFB1,
CC leading to regulate activation of TGF-beta-1. LTBP1 does not bind
CC directly to TGF-beta-1, the active chain of TGFB1. Interacts (via C-
CC terminal domain) with FBN1 (via N-terminal domain). Interacts with
CC FBN2. Interacts with ADAMTSL2. Interacts with EFEMP2 (By similarity).
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q14766}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- DOMAIN: The 8-Cys3 region in the third TB domain mediates the
CC interchain disulfide bond interaction with the Latency-associated
CC peptide chain (LAP) regulatory chain of TGFB1.
CC {ECO:0000250|UniProtKB:Q14766}.
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 -!- PTM: O-glycosylated on serine residues by POGLUT2 and POGLUT3.
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
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DR EMBL; M55431; AAA42235.1; -; mRNA.
DR PIR; A38261; A38261.
DR RefSeq; NP_067598.1; NM_021587.1.
DR AlphaFoldDB; Q00918; -.
DR IntAct; Q00918; 1.
DR STRING; 10116.ENSRNOP00000040099; -.
DR CarbonylDB; Q00918; -.
DR GlyGen; Q00918; 7 sites.
DR iPTMnet; Q00918; -.
DR PhosphoSitePlus; Q00918; -.
DR PaxDb; Q00918; -.
DR GeneID; 59107; -.
DR KEGG; rno:59107; -.
DR UCSC; RGD:68379; rat.
DR CTD; 4052; -.
DR RGD; 68379; Ltbp1.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q00918; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q00918; -.
DR Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q00918; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0038045; C:large latent transforming growth factor-beta complex; IDA:RGD.
DR GO; GO:0001527; C:microfibril; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050436; F:microfibril binding; ISO:RGD.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:RGD.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR GO; GO:0060976; P:coronary vasculature development; ISO:RGD.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:RGD.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; ISS:UniProtKB.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
DR Gene3D; 3.90.290.10; -; 4.
DR InterPro; IPR026823; cEGF.
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; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 13.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 18.
DR SMART; SM00179; EGF_CA; 16.
DR SUPFAM; SSF57184; SSF57184; 4.
DR SUPFAM; SSF57581; SSF57581; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 13.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 10.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS01187; EGF_CA; 15.
DR PROSITE; PS51364; TB; 4.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Growth factor binding; Hydroxylation; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1712
FT /note="Latent-transforming growth factor beta-binding
FT protein 1"
FT /id="PRO_0000445555"
FT DOMAIN 181..213
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 391..423
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 549..601
FT /note="TB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 618..658
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 669..721
FT /note="TB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 865..906
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 907..948
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 949..989
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 990..1029
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1030..1070
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1071..1111
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1112..1152
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1153..1193
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1194..1235
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1236..1277
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1278..1320
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1338..1392
FT /note="TB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1415..1457
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1458..1498
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1515..1568
FT /note="TB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1612..1652
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1653..1697
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 63..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1402
FT /note="8-Cys3 region"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT REGION 1498..1712
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT SITE 736..737
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 1577..1578
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT MOD_RES 966
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT MOD_RES 1129
FT /note="(3R)-3-hydroxyasparagine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT MOD_RES 1405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT MOD_RES 1588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT MOD_RES 1607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CG19"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT CARBOHYD 929
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT CARBOHYD 1011
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT CARBOHYD 1042
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1051
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT CARBOHYD 1133
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT CARBOHYD 1216
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT CARBOHYD 1242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1479
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT CARBOHYD 1678
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT DISULFID 185..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 189..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 203..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 395..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 399..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 413..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 551..573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 560..586
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 574..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 622..633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 628..642
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 644..657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 671..694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 681..706
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 695..709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 696..721
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 869..881
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 876..890
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 892..905
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 911..923
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 918..932
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 934..947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 953..964
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 959..973
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 976..988
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 994..1005
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1000..1014
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1017..1028
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1034..1045
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1040..1054
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1056..1069
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1075..1086
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1081..1095
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1097..1110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1116..1127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1122..1136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1138..1151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1157..1169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1164..1178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1180..1192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1198..1210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1204..1219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1221..1234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1240..1252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1246..1261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1263..1276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1282..1294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1289..1303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1305..1319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1340..1363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1350..1375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1350
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT DISULFID 1364..1380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1365..1392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1375
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q14766"
FT DISULFID 1419..1432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1427..1441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1443..1456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1462..1473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1468..1482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1484..1497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1517..1541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1527..1553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1542..1556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1543..1568
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1616..1627
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1622..1636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1638..1651
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1657..1672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1667..1681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1683..1696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1712 AA; 186599 MW; 650BCEAA691FD134 CRC64;
MAGAWLRWGL LLWAGLLAWS AHGRVRRITY VVRPGPGLPA GTLPLAGPPR TFNVALDARY
SRSSTATSSR SLAGPPAERT RRTSQPGGAA LPGLRSPLPP EPARPGAPSR QLHSKAGAQT
AVTRFAKHGR QVVRSKVQQD TQSSGGSRLQ VQQKQQLQGI NVCGGQCCHG WSKAPGSQRC
TKPSCVPPCQ NGGMCLRPQF CVCKPGTKGK ACEITAAQDT MSPVFGGQNP GSSWVPPEPA
AKRTSTKKAD TLPRVSPVAQ MTLTLKPKPS MGLSQQIHSQ VAPLSSQNVM IRHGQTQEYV
LKPKYFPAPK VVSGEQSTEG SFSLRYGQEQ GTAPFQVSNH TGRIKVVFTP SICKVTCTKG
NCHNSCQKGN TTTLISENGH AADTLTATNF RVVICHLPCM NGGQCSSRDK CQCPPNFTGK
LCQIPVLGAS MPKLYQHAQQ PGKALGSHVI HSTHTLPLTM TNQQGVKVKF PPNIVNIHVK
HPPEASVQIH QVSRIDGPVG QRVKEVQPGQ SQVSYQGLPV QKTQTVHSTY SHQQVIPHVY
PVAAKTQLGR CFQETIGSQC GKALPGLSKQ EDCCGTVGTS WGFNKCQKCP KKQSYHGYTQ
MMECLQGYKR VNNTFCQDIN ECQLQGVCPN GECLNTMGSY RCSCKMGFGP DPTFSSCVPD
PPMISEEKGP CYRLVSPGRQ CMHPLSVHLT KQICCCSVGK AWGPQCEKCP LPGTAAFKEI
CPGGMGYTVS GIHRRRPIHQ HIGKEAVFVK PKNTQPVAKS THPPPLPAKE EPVEALTSSR
EHGPGVAEPE VVTAPPEKEI PSLDQEKTRL EPGQPQLSPG VSTIHLHPQF PVVVEKTSPP
VPVEVAPEGS TSSASQVIAP TQVTEINECT VNPDICGAGH CINLPVRYTC ICYEGYKFSE
QQRKCIDIDE CAQAQHLCSQ GRCENTEGSF LCICPAGFIA SEEGSNCIDV DECLRPDVCR
DGRCINTAGA FRCEYCDSGY RMSRRGHCED IDECLTPSTC PEEQCVNSPG SYQCVPCTEG
FRGWNGQCLD VDECLQPKVC TNGSCTNLEG SYMCSCHKGY SPTPDHRHCQ DIDECQQGNL
CMNGQCKNTD GSFRCTCGQG YQLSAAKDQC EDIDECEHRH LCSHGQCRNT EGSFQCLCNQ
GYRASVLGDH CEDINECLED SSVCQGGDCI NTAGSYDCTC PDGLQLNDNK GCQDINECAQ
PGLCAPHGEC LNTQGSFHCV CEQGFSISAD GRTCEDIDEC VNNTVCDSHG FCDNTAGSFR
CLCYQGFQAP QDGQGCVDVN ECELLSGVCG EAFCENVEGS FLCVCADENQ EYSPMTGQCR
SRATEDSGVD RQPKEEKKEC YYNLNDASLC DNVLAPNVTK QECCCTSGAG WGDNCEIFPC
PVQGTAEFSE MCPRGKGFVP AGESSYETGG ENYKDADECL LFGEEICKNG YCLNTQPGYE
CYCKEGTYYD PVKLQCFDMD ECQDPNSCID GQCVNTEGSY NCFCTHPMVL DASEKRCVQP
TESNEQIEET DVYQDLCWEH LSEEYVCSRP LVGKQTTYTE CCCLYGEAWG MQCALCPMKD
SDDYAQLCNI PVTGRRRPYG RDALVDFSEQ YGPETDPYFI QDRFLNSFEE LQAEECGILN
GCENGRCVRV QEGYTCDCFD GYHLDMAKMT CVDVNECSEL NNRMSLCKNA KCINTEGSYK
CVCLPGYVPS DKPNYCTPLN TALNLDKDSD LE
