GenomeNet

Database: UniProt
Entry: O08999
LinkDB: O08999
Original site: O08999 
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   10-APR-2019, entry version 155.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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.,
RA   Towns K., Murphy A.L., Azmanov D., Tournev I., Cherninkova S.,
RA   Jafri H., Raashid Y., Toomes C., Craig J., Mackey D.A.,
RA   Kalaydjieva L., Riazuddin S., 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
RP   BY 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
RT   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
CC       beta precursor complex; removal is essential for activation of
CC       complex. Interacts with SDC4. Interacts (via C-terminal domain)
CC       with FBN1 (via 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};
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   UniGene; Mm.3900; -.
DR   ProteinModelPortal; O08999; -.
DR   SMR; O08999; -.
DR   IntAct; O08999; 2.
DR   MINT; O08999; -.
DR   STRING; 10090.ENSMUSP00000002073; -.
DR   iPTMnet; O08999; -.
DR   PhosphoSitePlus; O08999; -.
DR   jPOST; O08999; -.
DR   MaxQB; O08999; -.
DR   PaxDb; O08999; -.
DR   PRIDE; O08999; -.
DR   GeneID; 16997; -.
DR   KEGG; mmu:16997; -.
DR   CTD; 4053; -.
DR   MGI; MGI:99502; Ltbp2.
DR   eggNOG; ENOG410KD9U; Eukaryota.
DR   eggNOG; ENOG410XSTY; LUCA.
DR   HOGENOM; HOG000293153; -.
DR   HOVERGEN; HBG052370; -.
DR   InParanoid; O08999; -.
DR   KO; K08023; -.
DR   OrthoDB; 1174178at2759; -.
DR   PhylomeDB; O08999; -.
DR   ChiTaRS; Ltbp2; mouse.
DR   PRO; PR:O08999; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Growth factor binding; Heparin-binding; Hydroxylation; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     35       {ECO:0000250|UniProtKB:O35806}.
FT   CHAIN        36   1813       Latent-transforming growth factor beta-
FT                                binding protein 2.
FT                                /FTId=PRO_0000007644.
FT   DOMAIN      181    213       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      381    413       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      536    588       TB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN      609    649       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      659    711       TB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN      835    877       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      878    920       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      921    960       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      961   1000       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1001   1041       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1042   1083       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1084   1125       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1126   1166       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1167   1208       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1209   1250       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1251   1294       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1295   1336       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1337   1379       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1403   1455       TB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN     1477   1519       EGF-like 17; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1520   1559       EGF-like 18; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1576   1628       TB 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN     1725   1765       EGF-like 19; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1766   1810       EGF-like 20; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REGION       94    115       Heparin-binding. {ECO:0000250}.
FT   REGION      226    243       Heparin-binding. {ECO:0000250}.
FT   REGION      329    339       Heparin-binding. {ECO:0000250}.
FT   REGION     1631   1813       C-terminal domain.
FT                                {ECO:0000250|UniProtKB:Q14767}.
FT   COMPBIAS    847   1364       Cys-rich.
FT   MOD_RES     491    491       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    175    175       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    328    328       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    603    603       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1161   1161       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1301   1301       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1422   1422       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1560   1560       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    185    195       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    189    201       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    203    212       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    385    395       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    389    401       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    403    412       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    538    560       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    547    573       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    561    576       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    613    624       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    619    633       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    635    648       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    661    683       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    670    696       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    684    699       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    685    711       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    839    852       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    847    861       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    863    876       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    882    893       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    887    902       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    904    919       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    925    936       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    931    945       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    947    959       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    965    976       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    971    985       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    988    999       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1005   1016       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1011   1025       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1027   1040       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1046   1057       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1052   1066       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1069   1082       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1088   1099       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1094   1108       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1111   1124       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1130   1142       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1137   1151       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1153   1165       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1171   1183       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1177   1192       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1194   1207       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1213   1224       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1219   1233       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1235   1249       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1255   1268       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1263   1277       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1281   1293       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1299   1311       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1305   1320       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1322   1335       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1341   1353       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1348   1362       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1364   1378       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1405   1428       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1415   1440       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1429   1443       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1430   1455       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1481   1494       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1489   1503       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1505   1518       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1524   1534       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1529   1543       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1545   1558       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1578   1601       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1587   1613       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1602   1616       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1603   1628       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1729   1740       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1735   1749       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1751   1764       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1770   1785       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1780   1794       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1796   1809       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CONFLICT     14     14       Q -> R (in Ref. 2; BAC35229).
FT                                {ECO:0000305}.
FT   CONFLICT     74     74       E -> G (in Ref. 2; BAC35229).
FT                                {ECO:0000305}.
FT   CONFLICT     97     97       W -> R (in Ref. 2; BAC35229).
FT                                {ECO:0000305}.
FT   CONFLICT    498    498       H -> R (in Ref. 2; BAC35229).
FT                                {ECO:0000305}.
FT   CONFLICT    553    553       S -> E (in Ref. 2; BAC35229).
FT                                {ECO:0000305}.
FT   CONFLICT    580    582       Missing (in Ref. 2; BAC35229).
FT                                {ECO:0000305}.
FT   CONFLICT    778    778       D -> L (in Ref. 2; BAC35229).
FT                                {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
//
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