ID M7B959_CHEMY Unreviewed; 985 AA.
AC M7B959;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Brother of CDO {ECO:0000313|EMBL:EMP33684.1};
GN ORFNames=UY3_09216 {ECO:0000313|EMBL:EMP33684.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP33684.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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DR EMBL; KB535353; EMP33684.1; -; Genomic_DNA.
DR AlphaFoldDB; M7B959; -.
DR STRING; 8469.M7B959; -.
DR eggNOG; ENOG502QUNT; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
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; BROTHER OF CDO; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF16625; ISET-FN3_linker; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..985
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004079914"
FT TRANSMEM 845..868
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..112
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 115..211
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 231..300
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 319..403
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 466..564
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 598..693
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 702..802
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 405..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 107785 MW; E42A83366B616729 CRC64;
MTMTLGRKRP TAAVACLILA AAGCFANLGE SLQVTVQPAS AVQKYGGLVS LGCVVQPLKV
NVTWRLNGKE LVGSDEALGI RIELGKLIIM ALNNHTVGRY QCIARMPEGV VASVPATVTL
AKIKDFKFDG QHVIEVDEGN TAVIACDLPE SHPKAQVRYS VKQEWLEASR DNYLIMPSGN
LQIVNASQED EGTYKCAAYN PVTQEVKTSV SSDRLRVRRS AAEAARIIYP PEAQTIIVTK
GQSLILECVA SGIPPPRVTW AKNGSSISGY NKTRFLLSNL LIDATSEEDS GTYSCMADNG
VGEAGAVFIF YNVQVFEPPE VTMELSQQII PWGQSAKFTC EVRGNPQPSV MWLRNAVPLS
SNHRFRLSRK ALRVMSVGPE DDGIYQCVAE NEVGSAQAMV HLRTAQPGTT MKPWRDSRSG
SAQSPTPPSS DKALKEKAML QRPKPTALEA SLHCVTNRGQ VSPAEAPIIL SSPRTSKTDC
YELVWRPRHD GRAPILYYTV KHRKIMNSSA NWTVRDIPAT QHRLTLTRLD PGSLYEVEMA
AYNCAGEGQT AMVTFRTGRR PKPDIVASKE QQIQRDDPGT STQSSNPLDN SRLSPPEAPD
RPTISTASET SVYVTWIPRG NGGFPIQSFR VEYKKLKKLG DWVLATSDIP PSRLSVEITG
LEKGTSYKFR VRALNILGES DPSTASKPYV VSGYSNRVYE RPVAGPYITF TDAINETTIM
LKWMYIPASN NNTPIHGFYI YYRPTDSDND SDYKKDVVEG DRYWHSISHL QPETSYDIKM
QCFNEGGESE FSNVMICETK ARKSLGLPGR LPPSTVPPQQ HPALSGGHSG LGTGAMVARS
SDLPYLIVGI VLGSIVLIIV AFIPLCLWRA WSKQKQTIDL GFSGTRLLVS SCQYTMVPLR
GVPTPRANGQ PYANGVHLNG SCPSGGTGYP STKSRDYRPD EGSLMLDQKT VPSSVASQMT
PPTSCSSHMM IAAIFKNNLL AYITQ
//
