ID C3ZIG5_BRAFL Unreviewed; 424 AA.
AC C3ZIG5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Ig-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_80767 {ECO:0000313|EMBL:EEN47690.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN47690.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN47690.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN47690.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR EMBL; GG666627; EEN47690.1; -; Genomic_DNA.
DR RefSeq; XP_002591679.1; XM_002591633.1.
DR AlphaFoldDB; C3ZIG5; -.
DR STRING; 7739.C3ZIG5; -.
DR eggNOG; KOG0613; Eukaryota.
DR eggNOG; KOG4348; Eukaryota.
DR InParanoid; C3ZIG5; -.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR11640:SF31; IRREGULAR CHIASM C-ROUGHEST PROTEIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR11640; NEPHRIN; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 271..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..258
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 360..419
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 319..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 46767 MW; 47C2072E35180617 CRC64;
MNDSGQGRRL DYIDARNSRP GNCSSVFIKA TLNLHCDVIM TAMMRVQPCV GCQSVPTIHL
KLPERMEAIS GDPVTLPATY STDRRVMNIA WYKLDPREPT SRTQIFSYYP PLQTRESYGD
YVGRTSLEDQ ASLRIARTKP ADEGKYILSV SVEGVGSSEG QVQLILMDPP SILSISDSLS
ATVADSVSVQ CVADGNPPPN ITWSRDGTRL RSAVHSVTSD MRTSTVKLGN VRVNDSGKYV
CQASNGVGRG ASSSLVLTIR ESRLGVTSST VAVVVGASAG GLWFIVCVAL AAYLVKRRRL
QDEKKKFAFY YNMGRREPTE RGELGEDKEP PPYTATPGKP SNKAPNYGGI NTIRKSIGRK
ERRYARAVYS YRPREENELR LEMDDVIEVL EGEDGGWCLG YLRGRIGLFP SNYVRFISSS
EGYI
//
