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Brother of CDO (Protein BOC)

 BOC_MOUSE               Reviewed;        1110 AA.
Q6AZB0; Q6KAM5; Q6P5H3; Q7TMJ3; Q8CE73; Q8CE91; Q8R377; Q923W7;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
02-MAY-2006, sequence version 2.
30-AUG-2017, entry version 129.
RecName: Full=Brother of CDO;
Short=Protein BOC;
Flags: Precursor;
Name=Boc;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
GLN-1051.
STRAIN=C57BL/6J; TISSUE=Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
VARIANT GLN-1051.
STRAIN=C57BL/6J, and FVB/N-3;
TISSUE=Fetal brain, Mammary gland, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-1109 (ISOFORMS 1; 3 AND 4), INDUCTION,
AND TISSUE SPECIFICITY.
PubMed=11782431; DOI=10.1093/emboj/21.1.114;
Kang J.-S., Mulieri P.J., Hu Y., Taliana L., Krauss R.S.;
"BOC, an Ig superfamily member, associates with CDO to positively
regulate myogenic differentiation.";
EMBO J. 21:114-124(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-1109 (ISOFORMS 1; 3 AND
4).
TISSUE=Brain;
PubMed=15449545; DOI=10.1093/dnares/11.2.127;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of FLJ genes:
the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
DNA Res. 11:127-135(2004).
[5]
IDENTIFICATION IN A COMPLEX WITH CDON; CDH2; CDH15 AND CTNNB1.
PubMed=12634428; DOI=10.1073/pnas.0736565100;
Kang J.-S., Feinleib J.L., Knox S., Ketteringham M.A., Krauss R.S.;
"Promyogenic members of the Ig and cadherin families associate to
positively regulate differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 100:3989-3994(2003).
[6]
STRUCTURE BY NMR OF 589-807.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the 2nd and 3rd fibronectin type III domain
from mouse biregional cell adhesion molecule-related/down-regulated
oncogenes (CDON) binding protein.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: Component of a cell-surface receptor complex that
mediates cell-cell interactions between muscle precursor cells.
Promotes differentiation of myogenic cells.
-!- SUBUNIT: Part of a complex that contains BOC, CDON, NEO1,
cadherins and CTNNB1. Interacts with SHH, DHH and IHH. Interacts
with NTN3 (By similarity). Interacts with CDH2 and CTNNB1.
Interacts with CDH15 only during the early stages of myoblast
differentiation. {ECO:0000250, ECO:0000269|PubMed:12634428}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q6AZB0-1; Sequence=Displayed;
Name=2;
IsoId=Q6AZB0-2; Sequence=VSP_018197, VSP_018200;
Name=3;
IsoId=Q6AZB0-3; Sequence=VSP_018198;
Name=4;
IsoId=Q6AZB0-4; Sequence=VSP_018199;
-!- TISSUE SPECIFICITY: Highly expressed in embryonic somites, limb
buds, dermomyotomes and in the neural tube.
{ECO:0000269|PubMed:11782431}.
-!- INDUCTION: Up-regulated during early stages of myoblast
differentiation. {ECO:0000269|PubMed:11782431}.
-!- SEQUENCE CAUTION:
Sequence=AAK71999.1; Type=Frameshift; Positions=19, 35, 46; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK028770; BAC26110.1; -; mRNA.
EMBL; AK028889; BAC26176.1; -; mRNA.
EMBL; BC026443; AAH26443.1; -; mRNA.
EMBL; BC056138; AAH56138.1; -; mRNA.
EMBL; BC062892; AAH62892.1; -; mRNA.
EMBL; BC078631; AAH78631.1; -; mRNA.
EMBL; AF388037; AAK71999.1; ALT_FRAME; mRNA.
EMBL; AK131182; BAD21432.1; -; Transcribed_RNA.
CCDS; CCDS28186.1; -. [Q6AZB0-1]
RefSeq; NP_766094.1; NM_172506.2.
UniGene; Mm.41561; -.
PDB; 1X4Y; NMR; -; A=707-807.
PDB; 1X4Z; NMR; -; A=591-698.
PDBsum; 1X4Y; -.
PDBsum; 1X4Z; -.
ProteinModelPortal; Q6AZB0; -.
SMR; Q6AZB0; -.
BioGrid; 228240; 1.
DIP; DIP-60410N; -.
STRING; 10090.ENSMUSP00000023370; -.
iPTMnet; Q6AZB0; -.
PhosphoSitePlus; Q6AZB0; -.
PaxDb; Q6AZB0; -.
PeptideAtlas; Q6AZB0; -.
PRIDE; Q6AZB0; -.
GeneID; 117606; -.
KEGG; mmu:117606; -.
UCSC; uc007zhl.1; mouse. [Q6AZB0-1]
UCSC; uc007zhm.1; mouse. [Q6AZB0-4]
CTD; 91653; -.
MGI; MGI:2151153; Boc.
eggNOG; ENOG410IHIH; Eukaryota.
eggNOG; ENOG410XSVT; LUCA.
HOVERGEN; HBG061102; -.
InParanoid; Q6AZB0; -.
KO; K20020; -.
PhylomeDB; Q6AZB0; -.
TreeFam; TF332268; -.
Reactome; R-MMU-375170; CDO in myogenesis.
Reactome; R-MMU-5632681; Ligand-receptor interactions.
EvolutionaryTrace; Q6AZB0; -.
PRO; PR:Q6AZB0; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0009986; C:cell surface; TAS:HGNC.
GO; GO:0030426; C:growth cone; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0030030; P:cell projection organization; IMP:MGI.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:HGNC.
GO; GO:0016202; P:regulation of striated muscle tissue development; ISO:MGI.
GO; GO:0016337; P:single organismal cell-cell adhesion; TAS:HGNC.
GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 8.
InterPro; IPR032982; BOC.
InterPro; IPR003961; FN3_dom.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
PANTHER; PTHR10489:SF799; PTHR10489:SF799; 1.
Pfam; PF00041; fn3; 3.
Pfam; PF07679; I-set; 1.
Pfam; PF00047; ig; 1.
SMART; SM00060; FN3; 3.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 4.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 3.
PROSITE; PS50835; IG_LIKE; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Polymorphism; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1110 Brother of CDO.
/FTId=PRO_0000234053.
TOPO_DOM 26 850 Extracellular. {ECO:0000255}.
TRANSMEM 851 871 Helical. {ECO:0000255}.
TOPO_DOM 872 1110 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 118 Ig-like C2-type 1.
DOMAIN 124 208 Ig-like C2-type 2.
DOMAIN 229 310 Ig-like C2-type 3.
DOMAIN 318 402 Ig-like C2-type 4.
DOMAIN 469 566 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 603 698 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 707 807 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 512 512 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 720 720 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 754 754 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 52 101 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 145 195 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 247 294 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 339 386 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 680 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_018197.
VAR_SEQ 449 449 Missing (in isoform 3).
{ECO:0000303|PubMed:11782431,
ECO:0000303|PubMed:15449545,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_018198.
VAR_SEQ 958 958 Missing (in isoform 4).
{ECO:0000303|PubMed:11782431,
ECO:0000303|PubMed:15449545,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_018199.
VAR_SEQ 985 1109 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_018200.
VARIANT 1051 1051 R -> Q (in strain: C57BL/6).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
CONFLICT 9 9 P -> A (in Ref. 3). {ECO:0000305}.
CONFLICT 24 24 L -> P (in Ref. 2; AAH78631).
{ECO:0000305}.
CONFLICT 64 64 R -> G (in Ref. 3; AAK71999).
{ECO:0000305}.
CONFLICT 74 74 D -> E (in Ref. 3; AAK71999).
{ECO:0000305}.
CONFLICT 85 85 T -> N (in Ref. 3; AAK71999).
{ECO:0000305}.
CONFLICT 105 105 M -> L (in Ref. 3; AAK71999).
{ECO:0000305}.
CONFLICT 304 304 G -> V (in Ref. 2; AAH62892).
{ECO:0000305}.
CONFLICT 453 453 P -> S (in Ref. 4; BAD21432).
{ECO:0000305}.
CONFLICT 878 878 K -> E (in Ref. 1; BAC26110).
{ECO:0000305}.
STRAND 595 597 {ECO:0000244|PDB:1X4Z}.
STRAND 608 611 {ECO:0000244|PDB:1X4Z}.
STRAND 614 620 {ECO:0000244|PDB:1X4Z}.
STRAND 633 643 {ECO:0000244|PDB:1X4Z}.
STRAND 648 654 {ECO:0000244|PDB:1X4Z}.
STRAND 660 665 {ECO:0000244|PDB:1X4Z}.
STRAND 671 680 {ECO:0000244|PDB:1X4Z}.
STRAND 712 717 {ECO:0000244|PDB:1X4Y}.
STRAND 719 722 {ECO:0000244|PDB:1X4Y}.
STRAND 724 729 {ECO:0000244|PDB:1X4Y}.
STRAND 742 747 {ECO:0000244|PDB:1X4Y}.
HELIX 755 757 {ECO:0000244|PDB:1X4Y}.
STRAND 761 764 {ECO:0000244|PDB:1X4Y}.
STRAND 769 772 {ECO:0000244|PDB:1X4Y}.
STRAND 780 788 {ECO:0000244|PDB:1X4Y}.
STRAND 800 803 {ECO:0000244|PDB:1X4Y}.
SEQUENCE 1110 AA; 121331 MW; ADC1B859CC126F2B CRC64;
MTTCRRERPI LTLLWILMAT AGCLADLNEV PQVTVQPMST VQKLGGTVIL GCVVEPPWMN
VTWRFNGKEL NGSDDALGVF ITRGTLVIAA LNNHTVGRYQ CVARMPAGAV ASVPATVTLA
NLQDFKLDVQ HVIEVDEGNT AVIACHLPES HPKAQVRYSV KQEWLEASRD NYLIMPSGNL
QIVNASQEDE GMYKCAAYNP VTQEVKTSGS GDRLRVRRST AEAARIIYPL EAQTVIVTKG
QSLILECVAS GIPPPRVTWA KDGSSIAAYN KTRFLLSNLL IDTTSEEDSG TYRCMASNGV
GDPGAAVILY NVQVFEPPEV TVELSQLVIP WGQSAKLTCE VRGNPPPSVL WLRNAVPLTS
SQRLRLSRRA LRVVSVGPED EGVYQCMAEN AVGSAHAVVQ LRTARPDTTL RPGRDTKPIA
ATPPMPPSRP SRPDQMLREQ PGLVKPPTSS VQPTSLKCPG EEQVAPAEAP IILSSPRTSK
TDSYELVWRP RHEGSSRTPI LYYVVKHRKV TNSSDDWTIS GIPANQHRLT LTRLDPGSLY
EVEMAAYNCA GEGQTAMVTF RTGRRPKPEI VASKEQQIQR DDPGASLQSS SQPDHGRLSP
PEAPDRPTIS TASETSVYVT WIPRGNGGFP IQSFRVEYKK LKKVGDWILA TSAIPPSRLS
VEITGLEKGI SYKFRVRALN MLGESEPSAP SRPYVVSGYS GRVYERPVAG PYITFTDAVN
ETTIMLKWMY IPASNNNTPI HGFYIYYRPT DSDNDSDYKK DMVEGDRYWH SISHLQPETS
YDIKMQCFNE GGESEFSNVM ICETKARKFS GQPGRPPPLT LAPPQPPPLE TMERPVGTGA
MVARASDLPY LIVGVVLGSI VLIIVTFIPF CLWRAWSKQK HTTDLGFPRS ALLSSSCQYT
MVPLEGLPGH QANGQPYLGG VSGRACVSRV HGSRGCPAAT VGCPGRKPQQ HCPGELAQQR
EDTNSQLRQP IVSNGYDLQN QQVARGPQCA SGVGAFLYTL PDDSTHQLLQ PQDCCHLQKQ
PVTTCQTAVR RTSESPGLES SWDPPYHSGP RCCLGLVPVE EVDSSDSCQV GGGDWSSQHP
SGTYTGQERG MRFSPSPSVH VSFETPPPTI


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