BOC_MOUSE
ID BOC_MOUSE Reviewed; 1110 AA.
AC Q6AZB0; Q6KAM5; Q6P5H3; Q7TMJ3; Q8CE73; Q8CE91; Q8R377; Q923W7;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Brother of CDO;
DE Short=Protein BOC;
DE Flags: Precursor;
GN Name=Boc;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP GLN-1051.
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP VARIANT GLN-1051.
RC STRAIN=C57BL/6J, and FVB/N-3;
RC TISSUE=Fetal brain, Mammary gland, and Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-1109 (ISOFORMS 1; 3 AND 4), INDUCTION, AND
RP TISSUE SPECIFICITY.
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 regulate
RT myogenic differentiation.";
RL EMBO J. 21:114-124(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-1109 (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH CDON; CDH2; CDH15 AND CTNNB1.
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 [6]
RP STRUCTURE BY NMR OF 589-807.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the 2nd and 3rd fibronectin type III domain from
RT mouse biregional cell adhesion molecule-related/down-regulated oncogenes
RT (CDON) binding protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Component of a cell-surface receptor complex that mediates
CC cell-cell interactions between muscle precursor cells. Promotes
CC differentiation of myogenic cells.
CC -!- SUBUNIT: Part of a complex that contains BOC, CDON, NEO1, cadherins and
CC CTNNB1. Interacts with SHH, DHH and IHH. Interacts with NTN3 (By
CC similarity). Interacts with CDH2 and CTNNB1. Interacts with CDH15 only
CC during the early stages of myoblast differentiation. {ECO:0000250,
CC ECO:0000269|PubMed:12634428}.
CC -!- INTERACTION:
CC Q6AZB0; Q01721: Gas1; NbExp=2; IntAct=EBI-15610126, EBI-15729104;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6AZB0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AZB0-2; Sequence=VSP_018197, VSP_018200;
CC Name=3;
CC IsoId=Q6AZB0-3; Sequence=VSP_018198;
CC Name=4;
CC IsoId=Q6AZB0-4; Sequence=VSP_018199;
CC -!- TISSUE SPECIFICITY: Highly expressed in embryonic somites, limb buds,
CC dermomyotomes and in the neural tube. {ECO:0000269|PubMed:11782431}.
CC -!- INDUCTION: Up-regulated during early stages of myoblast
CC differentiation. {ECO:0000269|PubMed:11782431}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK71999.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK028770; BAC26110.1; -; mRNA.
DR EMBL; AK028889; BAC26176.1; -; mRNA.
DR EMBL; BC026443; AAH26443.1; -; mRNA.
DR EMBL; BC056138; AAH56138.1; -; mRNA.
DR EMBL; BC062892; AAH62892.1; -; mRNA.
DR EMBL; BC078631; AAH78631.1; -; mRNA.
DR EMBL; AF388037; AAK71999.1; ALT_FRAME; mRNA.
DR EMBL; AK131182; BAD21432.1; -; Transcribed_RNA.
DR CCDS; CCDS28186.1; -. [Q6AZB0-1]
DR RefSeq; NP_766094.1; NM_172506.2.
DR PDB; 1X4Y; NMR; -; A=707-807.
DR PDB; 1X4Z; NMR; -; A=591-698.
DR PDBsum; 1X4Y; -.
DR PDBsum; 1X4Z; -.
DR AlphaFoldDB; Q6AZB0; -.
DR SMR; Q6AZB0; -.
DR BioGRID; 228240; 2.
DR DIP; DIP-60410N; -.
DR IntAct; Q6AZB0; 2.
DR STRING; 10090.ENSMUSP00000023370; -.
DR GlyGen; Q6AZB0; 8 sites.
DR iPTMnet; Q6AZB0; -.
DR PhosphoSitePlus; Q6AZB0; -.
DR PaxDb; Q6AZB0; -.
DR PeptideAtlas; Q6AZB0; -.
DR PRIDE; Q6AZB0; -.
DR ProteomicsDB; 273753; -. [Q6AZB0-1]
DR ProteomicsDB; 273754; -. [Q6AZB0-2]
DR ProteomicsDB; 273755; -. [Q6AZB0-3]
DR ProteomicsDB; 273756; -. [Q6AZB0-4]
DR DNASU; 117606; -.
DR GeneID; 117606; -.
DR KEGG; mmu:117606; -.
DR UCSC; uc007zhl.1; mouse. [Q6AZB0-1]
DR UCSC; uc007zhm.1; mouse. [Q6AZB0-4]
DR CTD; 91653; -.
DR MGI; MGI:2151153; Boc.
DR eggNOG; ENOG502QUNT; Eukaryota.
DR InParanoid; Q6AZB0; -.
DR OrthoDB; 102649at2759; -.
DR PhylomeDB; Q6AZB0; -.
DR TreeFam; TF332268; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR Reactome; R-MMU-5635838; Activation of SMO.
DR BioGRID-ORCS; 117606; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Boc; mouse.
DR EvolutionaryTrace; Q6AZB0; -.
DR PRO; PR:Q6AZB0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6AZB0; protein.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0009986; C:cell surface; TAS:HGNC-UCL.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0030030; P:cell projection organization; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:HGNC-UCL.
DR GO; GO:0016202; P:regulation of striated muscle tissue development; ISO:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR032982; BOC.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR44170:SF3; PTHR44170:SF3; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
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; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1110
FT /note="Brother of CDO"
FT /id="PRO_0000234053"
FT TOPO_DOM 26..850
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 851..871
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 872..1110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..118
FT /note="Ig-like C2-type 1"
FT DOMAIN 124..208
FT /note="Ig-like C2-type 2"
FT DOMAIN 229..310
FT /note="Ig-like C2-type 3"
FT DOMAIN 318..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 469..566
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 603..698
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 707..807
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 407..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 145..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 247..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 339..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..680
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018197"
FT VAR_SEQ 449
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11782431,
FT ECO:0000303|PubMed:15449545, ECO:0000303|PubMed:15489334"
FT /id="VSP_018198"
FT VAR_SEQ 958
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11782431,
FT ECO:0000303|PubMed:15449545, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018199"
FT VAR_SEQ 985..1109
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018200"
FT VARIANT 1051
FT /note="R -> Q (in strain: C57BL/6)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16141072"
FT CONFLICT 9
FT /note="P -> A (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="L -> P (in Ref. 2; AAH78631)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="R -> G (in Ref. 3; AAK71999)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="D -> E (in Ref. 3; AAK71999)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="T -> N (in Ref. 3; AAK71999)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="M -> L (in Ref. 3; AAK71999)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="G -> V (in Ref. 2; AAH62892)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="P -> S (in Ref. 4; BAD21432)"
FT /evidence="ECO:0000305"
FT CONFLICT 878
FT /note="K -> E (in Ref. 1; BAC26110)"
FT /evidence="ECO:0000305"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:1X4Z"
FT STRAND 608..611
FT /evidence="ECO:0007829|PDB:1X4Z"
FT STRAND 614..620
FT /evidence="ECO:0007829|PDB:1X4Z"
FT STRAND 633..643
FT /evidence="ECO:0007829|PDB:1X4Z"
FT STRAND 648..654
FT /evidence="ECO:0007829|PDB:1X4Z"
FT STRAND 660..665
FT /evidence="ECO:0007829|PDB:1X4Z"
FT STRAND 671..680
FT /evidence="ECO:0007829|PDB:1X4Z"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:1X4Y"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:1X4Y"
FT STRAND 724..729
FT /evidence="ECO:0007829|PDB:1X4Y"
FT STRAND 742..747
FT /evidence="ECO:0007829|PDB:1X4Y"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:1X4Y"
FT STRAND 761..764
FT /evidence="ECO:0007829|PDB:1X4Y"
FT STRAND 769..772
FT /evidence="ECO:0007829|PDB:1X4Y"
FT STRAND 780..788
FT /evidence="ECO:0007829|PDB:1X4Y"
FT STRAND 800..803
FT /evidence="ECO:0007829|PDB:1X4Y"
SQ 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
