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Database: UniProt
Entry: Q30189_HUMAN
LinkDB: Q30189_HUMAN
Original site: Q30189_HUMAN 
ID   Q30189_HUMAN            Unreviewed;       304 AA.
AC   Q30189;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=HLA-C specific activatory NK receptor {ECO:0000313|EMBL:CAA67364.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:CAA67364.1};
RN   [1] {ECO:0000313|EMBL:CAA67364.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GT {ECO:0000313|EMBL:CAA67364.1};
RC   TISSUE=Lymphoid {ECO:0000313|EMBL:CAA67364.1};
RX   PubMed=9464792; DOI=10.1002/eji.1830271203;
RA   Biassoni R., Pessino A., Malaspina A., Cantoni C., Bottino C., Sivori S.,
RA   Moretta L., Moretta A.;
RT   "Role of amino acid position 70 in the binding affinity of p50.1 and p58.1
RT   receptors for HLA-Cw4 molecules.";
RL   Eur. J. Immunol. 27:3095-3099(1997).
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC       {ECO:0000256|ARBA:ARBA00008637}.
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DR   EMBL; X98858; CAA67364.1; -; mRNA.
DR   AlphaFoldDB; Q30189; -.
DR   PeptideAtlas; Q30189; -.
DR   UCSC; uc032jeh.2; human.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   PANTHER; PTHR11738:SF168; KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 2DL2-RELATED; 1.
DR   PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1.
DR   Pfam; PF00047; ig; 2.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
PE   2: Evidence at transcript level;
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|SAM:Phobius}; Receptor {ECO:0000313|EMBL:CAA67364.1};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..304
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030175646"
FT   TRANSMEM        244..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          34..114
FT                   /note="Immunoglobulin subtype"
FT                   /evidence="ECO:0000259|SMART:SM00409"
FT   DOMAIN          134..221
FT                   /note="Immunoglobulin subtype"
FT                   /evidence="ECO:0000259|SMART:SM00409"
FT   REGION          220..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   304 AA;  33648 MW;  E0868CDF5A5D2F36 CRC64;
     MSLMVVSMAC VGFFLLQGAW PHEGVHRKPS LLAHPGRLVK SEETVILQCW SDVMFEHFLL
     HREGMFNDTL RLIGEHHDGV SKANFSISRM KQDLAGTYRC YGSVTHSPYQ LSAPSDPLDI
     VIIGLYEKPS LSAQPGPTVL AGENVTLSCS SRSSYDMYHL SREGEAHERR LPAGTKVNGT
     FQANFPLGPA THGGTYRCFG SFRDSPYEWS KSSDPLLVSV TGNPSNSWPS PTEPSSETGN
     PRHLHVLIGT SVVKIPFTIL LFFLLHRWCS DKKNAAVMDQ EPAGNRTVNS EDSDEQDHQE
     VSYA
//
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