LTBP2_MOUSE
ID LTBP2_MOUSE Reviewed; 1813 AA.
AC O08999; Q8C6W9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Latent-transforming growth factor beta-binding protein 2;
DE Short=LTBP-2;
DE Flags: Precursor;
GN Name=Ltbp2;
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], AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-778.
RC STRAIN=C57BL/6J; TISSUE=Head;
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 PROTEIN SEQUENCE OF 205-211, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
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 [5]
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=19361779; DOI=10.1016/j.ajhg.2009.03.017;
RA Ali M., McKibbin M., Booth A., Parry D.A., Jain P., Riazuddin S.A.,
RA Hejtmancik J.F., Khan S.N., Firasat S., Shires M., Gilmour D.F., Towns K.,
RA Murphy A.L., Azmanov D., Tournev I., Cherninkova S., Jafri H., Raashid Y.,
RA Toomes C., Craig J., Mackey D.A., Kalaydjieva L., Riazuddin S.,
RA Inglehearn C.F.;
RT "Null mutations in LTBP2 cause primary congenital glaucoma.";
RL Am. J. Hum. Genet. 84:664-671(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: May play an integral structural role in elastic-fiber
CC architectural organization and/or assembly.
CC {ECO:0000250|UniProtKB:Q14767}.
CC -!- SUBUNIT: Forms part of the large latent transforming growth factor beta
CC precursor complex; removal is essential for activation of complex.
CC Interacts with SDC4. Interacts (via C-terminal domain) with FBN1 (via
CC N-terminal domain) in a Ca(+2)-dependent manner.
CC {ECO:0000250|UniProtKB:Q14767}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q14767}.
CC -!- TISSUE SPECIFICITY: Expressed in the anterior chamber of the eye.
CC {ECO:0000269|PubMed:19361779}.
CC -!- PTM: N-Glycosylated. {ECO:0000250|UniProtKB:Q14767}.
CC -!- PTM: Contains hydroxylated asparagine residues.
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC35229.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF004874; AAB61611.1; ALT_INIT; mRNA.
DR EMBL; AK052980; BAC35229.1; ALT_INIT; mRNA.
DR RefSeq; NP_038617.3; NM_013589.3.
DR AlphaFoldDB; O08999; -.
DR IntAct; O08999; 1.
DR MINT; O08999; -.
DR STRING; 10090.ENSMUSP00000002073; -.
DR GlyGen; O08999; 8 sites.
DR iPTMnet; O08999; -.
DR PhosphoSitePlus; O08999; -.
DR CPTAC; non-CPTAC-3989; -.
DR jPOST; O08999; -.
DR MaxQB; O08999; -.
DR PaxDb; O08999; -.
DR PRIDE; O08999; -.
DR ProteomicsDB; 290184; -.
DR DNASU; 16997; -.
DR GeneID; 16997; -.
DR KEGG; mmu:16997; -.
DR CTD; 4053; -.
DR MGI; MGI:99502; Ltbp2.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; O08999; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; O08999; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR BioGRID-ORCS; 16997; 1 hit in 56 CRISPR screens.
DR ChiTaRS; Ltbp2; mouse.
DR PRO; PR:O08999; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08999; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0050436; F:microfibril binding; IBA:GO_Central.
DR GO; GO:0097435; P:supramolecular fiber organization; IMP:MGI.
DR Gene3D; 3.90.290.10; -; 4.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
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; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 16.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 20.
DR SMART; SM00179; EGF_CA; 18.
DR SUPFAM; SSF57184; SSF57184; 6.
DR SUPFAM; SSF57581; SSF57581; 4.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 12.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 10.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 16.
DR PROSITE; PS51364; TB; 4.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Growth factor binding; Heparin-binding;
KW Hydroxylation; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000250|UniProtKB:O35806"
FT CHAIN 36..1813
FT /note="Latent-transforming growth factor beta-binding
FT protein 2"
FT /id="PRO_0000007644"
FT DOMAIN 181..213
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 381..413
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 536..588
FT /note="TB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 609..649
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 659..711
FT /note="TB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 835..877
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 878..920
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 921..960
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 961..1000
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1001..1041
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1042..1083
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1084..1125
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1126..1166
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1167..1208
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1209..1250
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1251..1294
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1295..1336
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1337..1379
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1403..1455
FT /note="TB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1477..1519
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1520..1559
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1576..1628
FT /note="TB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1725..1765
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1766..1810
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 94..115
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 103..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..243
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 492..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1631..1813
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:Q14767"
FT REGION 1671..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329..339
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 385..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 389..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 403..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 538..560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 547..573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 561..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 613..624
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 619..633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 635..648
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 661..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 670..696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 684..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 685..711
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 839..852
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 847..861
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 863..876
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 882..893
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 887..902
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 904..919
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 925..936
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 931..945
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 947..959
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 965..976
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 971..985
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 988..999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1005..1016
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1011..1025
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1027..1040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1046..1057
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1052..1066
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1069..1082
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1088..1099
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1094..1108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1111..1124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1130..1142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1137..1151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1153..1165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1171..1183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1177..1192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1194..1207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1213..1224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1219..1233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1235..1249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1255..1268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1263..1277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1281..1293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1299..1311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1305..1320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1322..1335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1341..1353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1348..1362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1364..1378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1405..1428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1415..1440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1429..1443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1430..1455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1481..1494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1489..1503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1505..1518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1524..1534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1529..1543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1545..1558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1578..1601
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1587..1613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1602..1616
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1603..1628
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1729..1740
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1735..1749
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1751..1764
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1770..1785
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1780..1794
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1796..1809
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 14
FT /note="Q -> R (in Ref. 2; BAC35229)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="E -> G (in Ref. 2; BAC35229)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="W -> R (in Ref. 2; BAC35229)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="H -> R (in Ref. 2; BAC35229)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="S -> E (in Ref. 2; BAC35229)"
FT /evidence="ECO:0000305"
FT CONFLICT 580..582
FT /note="Missing (in Ref. 2; BAC35229)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="D -> L (in Ref. 2; BAC35229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1813 AA; 195829 MW; D993DF6489AA27D5 CRC64;
MRAPTTARCS GCIQRVRWRG FLPLVLAVLM GTSHAQRDSI GRYEPASRDA NRLWHPVGSH
PAAAAAKVYS LFREPDAPVP GLSPSEWNQP AQGNPGWLAE AEARRPPRTQ QLRRVQPPVQ
TRRSHPRGQQ QIAARAAPSV ARLETPQRPA AARRGRLTGR NVCGGQCCPG WTTSNSTNHC
IKPVCQPPCQ NRGSCSRPQV CICRSGFRGA RCEEVIPEEE FDPQNARPVP RRSVERAPGP
HRSSEARGSL VTRIQPLVPP PSPPPSRRLS QPWPLQQHSG PSRTVRRYPA TGANGQLMSN
ALPSGLELRD SSPQAAHVNH LSPPWGLNLT EKIKKIKVVF TPTICKQTCA RGRCANSCEK
GDTTTLYSQG GHGHDPKSGF RIYFCQIPCL NGGRCIGRDE CWCPANSTGK FCHLPVPQPD
REPAGRGSRH RTLLEGPLKQ STFTLPLSNQ LASVNPSLVK VQIHHPPEAS VQIHQVARVR
GELDPVLEDN SVETRASHRP HGNLGHSPWA SNSIPARAGE APRPPPVLSR HYGLLGQCYL
STVNGQCANP LGSLTSQEDC CGSVGTFWGV TSCAPCPPRQ EGPAFPVIEN GQLECPQGYK
RLNLSHCQDI NECLTLGLCK DSECVNTRGS YLCTCRPGLM LDPSRSRCVS DKAVSMQQGL
CYRSLGSGTC TLPLVHRITK QICCCSRVGK AWGSTCEQCP LPGTEAFREI CPAGHGYTYS
SSDIRLSMRK AEEEELASPL REQTEQSTAP PPGQAERQPL RAATATWIEA ETLPDKGDSR
AVQITTSAPH LPARVPGDAT GRPAPSLPGQ GIPESPAEEQ VIPSSDVLVT HSPPDFDPCF
AGASNICGPG TCVSLPNGYR CVCSPGYQLH PSQDYCTDDN ECMRNPCEGR GRCVNSVGSY
SCLCYPGYTL VTLGDTQECQ DIDECEQPGV CSGGRCSNTE GSYHCECDRG YIMVRKGHCQ
DINECRHPGT CPDGRCVNSP GSYTCLACEE GYVGQSGSCV DVNECLTPGI CTHGRCINME
GSFRCSCEPG YEVTPDKKGC RDVDECASRA SCPTGLCLNT EGSFTCSACQ SGYWVNEDGT
ACEDLDECAF PGVCPTGVCT NTVGSFSCKD CDQGYRPNPL GNRCEDVDEC EGPQSSCRGG
ECKNTEGSYQ CLCHQGFQLV NGTMCEDVNE CVGEEHCAPH GECLNSLGSF FCLCAPGFAS
AEGGTRCQDV DECAATDPCP GGHCVNTEGS FSCLCETASF QPSPDSGECL DIDECEDRED
PVCGAWRCEN SPGSYRCILD CQPGFYVAPN GDCIDIDECA NDTVCGNHGF CDNTDGSFRC
LCDQGFETSP SGWECVDVNE CELMMAVCGD ALCENVEGSF LCLCASDLEE YDAEEGHCRP
RVAGAQRIPE VRTEDQAPSL IRMECYSEHN GGPPCSQILG QNSTQAECCC TQGARWGKAC
APCPSEDSVE FSQLCPSGQG YIPVEGAWTF GQTMYTDADE CVLFGPALCQ NGRCSNIVPG
YICLCNPGYH YDASSRKCQD HNECQDLACE NGECVNQEGS FHCLCNPPLT LDLSGQRCVN
TTSSTEDFPD HDIHMDICWK KVTNDVCSQP LRGHHTTYTE CCCQDGEAWS QQCALCPPRS
SEVYAQLCNV ARIEAERGAG IHFRPGYEYG PGLDDLPENL YGPDGAPFYN YLGPEDTAPE
PPFSNPASQP GDNTPVLEPP LQPSELQPHY LASHSEPPAS FEGLQAEECG ILNGCENGRC
VRVREGYTCD CFEGFQLDAP TLACVDVNEC EDLNGPARLC AHGHCENTEG SYRCHCSPGY
VAEPGPPHCA AKE
