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Database: UniProt
Entry: Q9BWV1
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Original site: Q9BWV1 
ID   BOC_HUMAN               Reviewed;        1114 AA.
AC   Q9BWV1; A6NJ30; B2RMS8; D3DN70; Q6UXJ5; Q8N2P7; Q8NF26;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   29-OCT-2014, entry version 112.
DE   RecName: Full=Brother of CDO;
DE            Short=Protein BOC;
DE   Flags: Precursor;
GN   Name=BOC; ORFNames=UNQ604/PRO1190;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDON,
RP   GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=11782431; DOI=10.1093/emboj/21.1.114;
RA   Kang J.-S., Mulieri P.J., Hu Y., Taliana L., Krauss R.S.;
RT   "BOC, an Ig superfamily member, associates with CDO to positively
RT   regulate myogenic differentiation.";
RL   EMBO J. 21:114-124(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-1114 (ISOFORM 3).
RC   TISSUE=Embryo, and Spleen;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 31-45.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [8]
RP   IDENTIFICATION IN A COMPLEX WITH CDON; CDH2; CDH15 AND CTNNB1, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12634428; DOI=10.1073/pnas.0736565100;
RA   Kang J.-S., Feinleib J.L., Knox S., Ketteringham M.A., Krauss R.S.;
RT   "Promyogenic members of the Ig and cadherin families associate to
RT   positively regulate differentiation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:3989-3994(2003).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 710-817 IN COMPLEXES WITH
RP   DHH AND IHH, AND INTERACTION WITH SHH; DHH AND IHH.
RX   PubMed=20519495; DOI=10.1074/jbc.M110.131680;
RA   Kavran J.M., Ward M.D., Oladosu O.O., Mulepati S., Leahy D.J.;
RT   "All mammalian Hedgehog proteins interact with cell adhesion molecule,
RT   down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a
RT   conserved manner.";
RL   J. Biol. Chem. 285:24584-24590(2010).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] MET-713.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Component of a cell-surface receptor complex that
CC       mediates cell-cell interactions between muscle precursor cells.
CC       Promotes differentiation of myogenic cells.
CC   -!- SUBUNIT: Part of a complex that contains BOC, CDON, NEO1,
CC       cadherins and CTNNB1. Interacts with NTN3 (By similarity).
CC       Interacts with SHH, DHH and IHH. Interacts with CDH2 and CTNNB1.
CC       Interacts with CDH15 only during the early stages of myoblast
CC       differentiation. {ECO:0000250, ECO:0000269|PubMed:11782431,
CC       ECO:0000269|PubMed:12634428, ECO:0000269|PubMed:20519495}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12634428};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:12634428}.
CC       Note=Enriched at sites of cell-cell contact.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9BWV1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BWV1-2; Sequence=VSP_037603, VSP_037604;
CC         Note=No experimental confirmation available. Incomplete
CC         sequence.;
CC       Name=3;
CC         IsoId=Q9BWV1-3; Sequence=VSP_034684;
CC   -!- TISSUE SPECIFICITY: Detected in skeletal muscle, heart, thymus,
CC       kidney and small intestine. Detected at lower levels in brain,
CC       placenta, lung and colon mucosa. {ECO:0000269|PubMed:11782431}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11782431}.
CC   -!- MISCELLANEOUS: The C-terminal cytoplasmic domain is not required
CC       for the stimuation of myogenesis.
CC   -!- SIMILARITY: Contains 3 fibronectin type-III domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
CC   -!- SIMILARITY: Contains 4 Ig-like C2-type (immunoglobulin-like)
CC       domains. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC11057.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR   EMBL; AY027658; AAK14795.1; -; mRNA.
DR   EMBL; AY358328; AAQ88694.1; -; mRNA.
DR   EMBL; AK074556; BAC11057.1; ALT_INIT; mRNA.
DR   EMBL; AK090455; BAC03436.1; -; mRNA.
DR   EMBL; AC026329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW79643.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79644.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79646.1; -; Genomic_DNA.
DR   EMBL; BC136390; AAI36391.1; -; mRNA.
DR   CCDS; CCDS2971.1; -. [Q9BWV1-1]
DR   RefSeq; NP_150279.1; NM_033254.2. [Q9BWV1-1]
DR   RefSeq; XP_005247948.1; XM_005247891.1. [Q9BWV1-3]
DR   RefSeq; XP_005247949.1; XM_005247892.1. [Q9BWV1-3]
DR   RefSeq; XP_005247950.1; XM_005247893.1. [Q9BWV1-3]
DR   RefSeq; XP_005247951.1; XM_005247894.1. [Q9BWV1-3]
DR   RefSeq; XP_005247953.1; XM_005247896.1. [Q9BWV1-1]
DR   UniGene; Hs.591318; -.
DR   PDB; 3N1G; X-ray; 1.90 A; C/D=710-817.
DR   PDB; 3N1M; X-ray; 1.69 A; C=710-817.
DR   PDB; 3N1P; X-ray; 2.70 A; C=710-817.
DR   PDBsum; 3N1G; -.
DR   PDBsum; 3N1M; -.
DR   PDBsum; 3N1P; -.
DR   ProteinModelPortal; Q9BWV1; -.
DR   SMR; Q9BWV1; 34-571, 597-813.
DR   BioGrid; 124859; 5.
DR   IntAct; Q9BWV1; 3.
DR   STRING; 9606.ENSP00000347546; -.
DR   PhosphoSite; Q9BWV1; -.
DR   DMDM; 74761309; -.
DR   PaxDb; Q9BWV1; -.
DR   PRIDE; Q9BWV1; -.
DR   Ensembl; ENST00000273395; ENSP00000273395; ENSG00000144857. [Q9BWV1-3]
DR   Ensembl; ENST00000355385; ENSP00000347546; ENSG00000144857. [Q9BWV1-1]
DR   Ensembl; ENST00000495514; ENSP00000418663; ENSG00000144857. [Q9BWV1-1]
DR   GeneID; 91653; -.
DR   KEGG; hsa:91653; -.
DR   UCSC; uc003dzx.3; human. [Q9BWV1-1]
DR   UCSC; uc003dzz.3; human. [Q9BWV1-3]
DR   CTD; 91653; -.
DR   GeneCards; GC03P112929; -.
DR   HGNC; HGNC:17173; BOC.
DR   HPA; CAB025806; -.
DR   MIM; 608708; gene.
DR   neXtProt; NX_Q9BWV1; -.
DR   PharmGKB; PA143485316; -.
DR   eggNOG; NOG150637; -.
DR   GeneTree; ENSGT00760000118886; -.
DR   HOVERGEN; HBG061102; -.
DR   InParanoid; Q9BWV1; -.
DR   OMA; QPDHGRL; -.
DR   OrthoDB; EOG7MD4PB; -.
DR   PhylomeDB; Q9BWV1; -.
DR   TreeFam; TF332268; -.
DR   Reactome; REACT_21402; CDO in myogenesis.
DR   SignaLink; Q9BWV1; -.
DR   EvolutionaryTrace; Q9BWV1; -.
DR   GeneWiki; BOC_(gene); -.
DR   GenomeRNAi; 91653; -.
DR   NextBio; 77360; -.
DR   PRO; PR:Q9BWV1; -.
DR   Bgee; Q9BWV1; -.
DR   CleanEx; HS_BOC; -.
DR   ExpressionAtlas; Q9BWV1; baseline and differential.
DR   Genevestigator; Q9BWV1; -.
DR   GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0042692; P:muscle cell differentiation; TAS:Reactome.
DR   GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:HGNC.
DR   GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; -; 7.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     30       {ECO:0000269|PubMed:15340161}.
FT   CHAIN        31   1114       Brother of CDO.
FT                                /FTId=PRO_0000234052.
FT   TOPO_DOM     31    855       Extracellular. {ECO:0000255}.
FT   TRANSMEM    856    876       Helical. {ECO:0000255}.
FT   TOPO_DOM    877   1114       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       36    123       Ig-like C2-type 1.
FT   DOMAIN      129    213       Ig-like C2-type 2.
FT   DOMAIN      235    315       Ig-like C2-type 3.
FT   DOMAIN      323    409       Ig-like C2-type 4.
FT   DOMAIN      474    571       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      608    703       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      712    812       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   CARBOHYD     65     65       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     76     76       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     98     98       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    189    189       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    275    275       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    517    517       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    725    725       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    759    759       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     57    106       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    150    200       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    252    299       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    344    391       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   VAR_SEQ       1    183       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_037603.
FT   VAR_SEQ     184    223       NLQIVNASQEDEGMYKCAAYNPVTQEVKTSGSSDRLRVRR
FT                                -> KTRNGCLIPSPCSLGLPPGHALQDILVHTPSVLALLAP
FT                                PG (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_037604.
FT   VAR_SEQ     514    514       K -> KQ (in isoform 3).
FT                                {ECO:0000303|PubMed:12975309,
FT                                ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_034684.
FT   VARIANT     713    713       V -> M (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035503.
FT   VARIANT     883    883       K -> N (in dbSNP:rs35536878).
FT                                /FTId=VAR_033600.
FT   VARIANT     915    915       Q -> H (in dbSNP:rs3814405).
FT                                /FTId=VAR_033601.
FT   CONFLICT    461    461       Q -> K (in Ref. 2; AAQ88694).
FT                                {ECO:0000305}.
FT   STRAND      717    725
FT   STRAND      728    734
FT   HELIX       737    740
FT   STRAND      746    754
FT   HELIX       760    762
FT   STRAND      764    769
FT   STRAND      774    777
FT   STRAND      785    794
FT   STRAND      805    808
SQ   SEQUENCE   1114 AA;  121059 MW;  BDA9021D39CFE3BC CRC64;
     MLRGTMTAWR GMRPEVTLAC LLLATAGCFA DLNEVPQVTV QPASTVQKPG GTVILGCVVE
     PPRMNVTWRL NGKELNGSDD ALGVLITHGT LVITALNNHT VGRYQCVARM PAGAVASVPA
     TVTLANLQDF KLDVQHVIEV DEGNTAVIAC HLPESHPKAQ VRYSVKQEWL EASRGNYLIM
     PSGNLQIVNA SQEDEGMYKC AAYNPVTQEV KTSGSSDRLR VRRSTAEAAR IIYPPEAQTI
     IVTKGQSLIL ECVASGIPPP RVTWAKDGSS VTGYNKTRFL LSNLLIDTTS EEDSGTYRCM
     ADNGVGQPGA AVILYNVQVF EPPEVTMELS QLVIPWGQSA KLTCEVRGNP PPSVLWLRNA
     VPLISSQRLR LSRRALRVLS MGPEDEGVYQ CMAENEVGSA HAVVQLRTSR PSITPRLWQD
     AELATGTPPV SPSKLGNPEQ MLRGQPALPR PPTSVGPASP QCPGEKGQGA PAEAPIILSS
     PRTSKTDSYE LVWRPRHEGS GRAPILYYVV KHRKVTNSSD DWTISGIPAN QHRLTLTRLD
     PGSLYEVEMA AYNCAGEGQT AMVTFRTGRR PKPEIMASKE QQIQRDDPGA SPQSSSQPDH
     GRLSPPEAPD RPTISTASET SVYVTWIPRG NGGFPIQSFR VEYKKLKKVG DWILATSAIP
     PSRLSVEITG LEKGTSYKFR VRALNMLGES EPSAPSRPYV VSGYSGRVYE RPVAGPYITF
     TDAVNETTIM LKWMYIPASN NNTPIHGFYI YYRPTDSDND SDYKKDMVEG DKYWHSISHL
     QPETSYDIKM QCFNEGGESE FSNVMICETK ARKSSGQPGR LPPPTLAPPQ PPLPETIERP
     VGTGAMVARS SDLPYLIVGV VLGSIVLIIV TFIPFCLWRA WSKQKHTTDL GFPRSALPPS
     CPYTMVPLGG LPGHQASGQP YLSGISGRAC ANGIHMNRGC PSAAVGYPGM KPQQHCPGEL
     QQQSDTSSLL RQTHLGNGYD PQSHQITRGP KSSPDEGSFL YTLPDDSTHQ LLQPHHDCCQ
     RQEQPAAVGQ SGVRRAPDSP VLEAVWDPPF HSGPPCCLGL VPVEEVDSPD SCQVSGGDWC
     PQHPVGAYVG QEPGMQLSPG PLVRVSFETP PLTI
//
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