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ULBP1_HUMAN
ID   ULBP1_HUMAN             Reviewed;         244 AA.
AC   Q9BZM6; Q5VY81; Q8IZW3; Q8IZX6;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=UL16-binding protein 1;
DE   AltName: Full=ALCAN-beta;
DE   AltName: Full=NKG2D ligand 1;
DE            Short=N2DL-1;
DE            Short=NKG2DL1;
DE   AltName: Full=Retinoic acid early transcript 1I;
DE   Flags: Precursor;
GN   Name=ULBP1; Synonyms=N2DL1, RAET1I;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND GPI-ANCHOR.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=11239445; DOI=10.1016/s1074-7613(01)00095-4;
RA   Cosman D., Mullberg J., Sutherland C.L., Chin W., Armitage R., Fanslow W.,
RA   Kubin M., Chalupny N.J.;
RT   "ULBPs, novel MHC class I-related molecules, bind to CMV glycoprotein UL16
RT   and stimulate NK cytotoxicity through the NKG2D receptor.";
RL   Immunity 14:123-133(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Onda H., Shintani Y., Ohkubo S., Ogi K.;
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11827464; DOI=10.1006/geno.2001.6673;
RA   Radosavljevic M., Cuillerier B., Wilson M.J., Clement O., Wicker S.,
RA   Gilfillan S., Beck S., Trowsdale J., Bahram S.;
RT   "A cluster of ten novel MHC class I related genes on human chromosome
RT   6q24.2-q25.3.";
RL   Genomics 79:114-123(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-244.
RA   Larson J.H., Rebeiz M., Stiening C.M., Windish R., Beever J.E., Lewin H.A.;
RT   "The ULBP proteins are highly divergent among mammals.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-244.
RX   PubMed=11491531; DOI=10.1007/s002510100325;
RA   Steinle A., Li P., Morris D.L., Groh V., Lanier L.L., Strong R.K.,
RA   Spies T.;
RT   "Interactions of human NKG2D with its ligands MICA, MICB, and homologs of
RT   the mouse RAE-1 protein family.";
RL   Immunogenetics 53:279-287(2001).
RN   [10]
RP   INTERACTION WITH CMV UL16, AND SUBCELLULAR LOCATION.
RX   PubMed=12782710; DOI=10.1084/jem.20022059;
RA   Dunn C., Chalupny N.J., Sutherland C.L., Dosch S., Sivakumar P.V.,
RA   Johnson D.C., Cosman D.;
RT   "Human cytomegalovirus glycoprotein UL16 causes intracellular sequestration
RT   of NKG2D ligands, protecting against natural killer cell cytotoxicity.";
RL   J. Exp. Med. 197:1427-1439(2003).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH KLRK1.
RX   PubMed=11777960; DOI=10.4049/jimmunol.168.2.671;
RA   Sutherland C.L., Chalupny N.J., Schooley K., VandenBos T., Kubin M.,
RA   Cosman D.;
RT   "UL16-binding proteins, novel MHC class I-related proteins, bind to NKG2D
RT   and activate multiple signaling pathways in primary NK cells.";
RL   J. Immunol. 168:671-679(2002).
RN   [12]
RP   REVIEW.
RX   PubMed=12753652; DOI=10.1034/j.1399-0039.2003.00070.x;
RA   Cerwenka A., Lanier L.L.;
RT   "NKG2D ligands: unconventional MHC class I-like molecules exploited by
RT   viruses and cancer.";
RL   Tissue Antigens 61:335-343(2003).
CC   -!- FUNCTION: Binds and activates the KLRK1/NKG2D receptor, mediating
CC       natural killer cell cytotoxicity. {ECO:0000269|PubMed:11777960}.
CC   -!- SUBUNIT: Interacts with KLRK1/NKG2D (PubMed:11777960). Does not bind to
CC       beta2-microglobulin (PubMed:12782710). {ECO:0000269|PubMed:11777960,
CC       ECO:0000269|PubMed:12782710}.
CC   -!- SUBUNIT: (Microbial infection) In CMV-infected cells, interacts with
CC       the viral glycoprotein UL16; this interaction causes ULBP1 retention in
CC       the endoplasmic reticulum and cis-Golgi and prevents binding to and
CC       activation of KLRK1/NKG2D, providing CMV with an immune evasion
CC       mechanism. {ECO:0000269|PubMed:12782710}.
CC   -!- INTERACTION:
CC       Q9BZM6; P26718: KLRK1; NbExp=2; IntAct=EBI-16365037, EBI-458344;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12782710};
CC       Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12782710}. Endoplasmic
CC       reticulum {ECO:0000269|PubMed:12782710}. Note=In CMV-infected
CC       fibroblasts, detected in the endoplasmic reticulum/cis-Golgi.
CC       {ECO:0000269|PubMed:12782710}.
CC   -!- TISSUE SPECIFICITY: Expressed in T-cells, B-cells, erythroleukemia cell
CC       lines and in a wide range of tissues including heart, brain, lung,
CC       liver, testis, lymph node, thymus, tonsil and bone marrow. Also found
CC       in fetal heart, brain, lung and liver.
CC   -!- MISCELLANEOUS: UL16-binding proteins (ULBPs) are unusual members of the
CC       extended MHC class I superfamily. They do not contain the alpha 3
CC       domain and lack a transmembrane domain. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR   EMBL; AF304377; AAK13081.1; -; mRNA.
DR   EMBL; AB052907; BAB61049.1; -; mRNA.
DR   EMBL; AF346416; AAL76416.1; -; mRNA.
DR   EMBL; AK292519; BAF85208.1; -; mRNA.
DR   EMBL; AK316582; BAG38170.1; -; mRNA.
DR   EMBL; AL355497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW47776.1; -; Genomic_DNA.
DR   EMBL; BC035416; AAH35416.1; -; mRNA.
DR   EMBL; AF425265; AAN32759.1; -; mRNA.
DR   EMBL; AF346595; AAN40838.1; -; mRNA.
DR   CCDS; CCDS5223.1; -.
DR   RefSeq; NP_001304018.1; NM_001317089.1.
DR   RefSeq; NP_079494.1; NM_025218.3.
DR   AlphaFoldDB; Q9BZM6; -.
DR   SMR; Q9BZM6; -.
DR   BioGRID; 123241; 18.
DR   CORUM; Q9BZM6; -.
DR   IntAct; Q9BZM6; 7.
DR   STRING; 9606.ENSP00000229708; -.
DR   GlyGen; Q9BZM6; 1 site.
DR   BioMuta; ULBP1; -.
DR   jPOST; Q9BZM6; -.
DR   MassIVE; Q9BZM6; -.
DR   PaxDb; Q9BZM6; -.
DR   PeptideAtlas; Q9BZM6; -.
DR   PRIDE; Q9BZM6; -.
DR   ProteomicsDB; 79879; -.
DR   Antibodypedia; 2344; 273 antibodies from 27 providers.
DR   DNASU; 80329; -.
DR   Ensembl; ENST00000229708.4; ENSP00000229708.2; ENSG00000111981.5.
DR   GeneID; 80329; -.
DR   KEGG; hsa:80329; -.
DR   MANE-Select; ENST00000229708.4; ENSP00000229708.2; NM_025218.4; NP_079494.1.
DR   UCSC; uc003qnp.5; human.
DR   CTD; 80329; -.
DR   DisGeNET; 80329; -.
DR   GeneCards; ULBP1; -.
DR   HGNC; HGNC:14893; ULBP1.
DR   HPA; ENSG00000111981; Group enriched (brain, lung, testis).
DR   MIM; 605697; gene.
DR   neXtProt; NX_Q9BZM6; -.
DR   OpenTargets; ENSG00000111981; -.
DR   PharmGKB; PA37915; -.
DR   VEuPathDB; HostDB:ENSG00000111981; -.
DR   eggNOG; ENOG502TM6M; Eukaryota.
DR   GeneTree; ENSGT01040000240396; -.
DR   HOGENOM; CLU_086235_0_0_1; -.
DR   InParanoid; Q9BZM6; -.
DR   OMA; VDTHCLC; -.
DR   OrthoDB; 1092787at2759; -.
DR   PhylomeDB; Q9BZM6; -.
DR   TreeFam; TF341724; -.
DR   PathwayCommons; Q9BZM6; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   SignaLink; Q9BZM6; -.
DR   BioGRID-ORCS; 80329; 11 hits in 1077 CRISPR screens.
DR   GeneWiki; ULBP1; -.
DR   GenomeRNAi; 80329; -.
DR   Pharos; Q9BZM6; Tbio.
DR   PRO; PR:Q9BZM6; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9BZM6; protein.
DR   Bgee; ENSG00000111981; Expressed in stromal cell of endometrium and 83 other tissues.
DR   Genevisible; Q9BZM6; HS.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0046703; F:natural killer cell lectin-like receptor binding; IDA:UniProtKB.
DR   GO; GO:0030101; P:natural killer cell activation; IDA:UniProtKB.
DR   GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR   Gene3D; 3.30.500.10; -; 1.
DR   InterPro; IPR011161; MHC_I-like_Ag-recog.
DR   InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR   InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR   Pfam; PF00129; MHC_I; 1.
DR   SUPFAM; SSF54452; SSF54452; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   GPI-anchor; Host-virus interaction; Immunity; Lipoprotein; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..216
FT                   /note="UL16-binding protein 1"
FT                   /id="PRO_0000019015"
FT   PROPEP          217..244
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000019016"
FT   REGION          26..117
FT                   /note="MHC class I alpha-1 like"
FT   REGION          118..208
FT                   /note="MHC class I alpha-2 like"
FT   LIPID           216
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        127..190
FT                   /evidence="ECO:0000250"
FT   VARIANT         101
FT                   /note="L -> I (in dbSNP:rs6903584)"
FT                   /id="VAR_050407"
SQ   SEQUENCE   244 AA;  27997 MW;  6094B17CE383DC6D CRC64;
     MAAAASPAFL LCLPLLHLLS GWSRAGWVDT HCLCYDFIIT PKSRPEPQWC EVQGLVDERP
     FLHYDCVNHK AKAFASLGKK VNVTKTWEEQ TETLRDVVDF LKGQLLDIQV ENLIPIEPLT
     LQARMSCEHE AHGHGRGSWQ FLFNGQKFLL FDSNNRKWTA LHPGAKKMTE KWEKNRDVTM
     FFQKISLGDC KMWLEEFLMY WEQMLDPTKP PSLAPGTTQP KAMATTLSPW SLLIIFLCFI
     LAGR
 
 
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