ID A0A2K5ILJ6_COLAP Unreviewed; 511 AA.
AC A0A2K5ILJ6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Ig-like domain-containing protein {ECO:0000259|PROSITE:PS50835};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000017588.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000017588.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K5ILJ6; -.
DR Ensembl; ENSCANT00000040535.1; ENSCANP00000017588.1; ENSCANG00000032217.1.
DR OMA; HNDSSKW; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR CDD; cd05751; IgC2_D1_LILR_KIR_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR InterPro; IPR016332; A1B_glyco/leuk_Ig-like_rcpt.
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; IPR013151; Immunoglobulin.
DR PANTHER; PTHR11738:SF170; LEUKOCYTE IMMUNOGLOBULIN-LIKE RECEPTOR SUBFAMILY A MEMBER 3; 1.
DR PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF13895; Ig_2; 1.
DR PIRSF; PIRSF001979; Alpha_1B_glycoprot_prd; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001979-1};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..511
FT /note="Ig-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014447093"
FT TRANSMEM 460..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..119
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 226..315
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 411..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 49..98
FT /evidence="ECO:0000256|PIRSR:PIRSR001979-1"
FT DISULFID 145..197
FT /evidence="ECO:0000256|PIRSR:PIRSR001979-1"
SQ SEQUENCE 511 AA; 55243 MW; 2D519763F3CDE2CA CRC64;
MTAILMVLIC LGLSLGPRTH VQAGTLPKPT LWAEPDSVIT QGSPVTLRCQ GTLETQEYRL
YREKKPALWN TWIPQEFAKN GQFPIPSITW EHAGRYRCIY GNHTAGWSEP SDPLELVVTG
AYSKPTLSAL PSPVVASGGN VTLQCDSQVA FDGFILCKEG EDEHPRCLNP QPRTRGSSWA
VFSVGPVSPS RRWSYRCYGY VSSTPYVWSL PSDLLELLVP GVSKKPSLSV QPGPVVAPGE
NLTLQCGSDA GYDRFVLYKE GECNFLQRPG WQPQAGLSQA NFTLGPVSGS HGGQYRCSGA
HNLSSEWSAP SDPLDILISG QIPDRPFLSV QTGPTVVSGQ NVTLLCQSQG WMHTFLLTKE
GAADPPLRLK SKRQPHKYQA EFPMSPVTSA HAGTYRCYGS RSSDPYLLSH PSDPLELVVS
GPSGSPSPPP TGPIPTPAGP EDQPLNPTGS DPQSGLGRHL GVVTGVSVAF VLLLSLLLLL
FLVLRHRGQG KRWTSGPVQL PTPRKKTSML P
//
