KLRF1_HUMAN
ID KLRF1_HUMAN Reviewed; 231 AA.
AC Q9NZS2; A0A0C4DGY9; Q4KMT5; Q96PR2; Q96PR3; Q9NZS1;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Killer cell lectin-like receptor subfamily F member 1;
DE Short=Lectin-like receptor F1;
DE AltName: Full=Activating coreceptor NKp80;
DE AltName: Full=C-type lectin domain family 5 member C;
GN Name=KLRF1; Synonyms=CLEC5C, ML;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=10671213;
RX DOI=10.1002/1521-4141(200002)30:2<568::aid-immu568>3.0.co;2-y;
RA Roda-Navarro P., Arce I., Renedo M., Montgomery K., Kucherlapati R.,
RA Fernandez-Ruiz E.;
RT "Human KLRF1, a novel member of the killer cell lectin-like receptor gene
RT family: molecular characterization, genomic structure, physical mapping to
RT the NK gene complex and expression analysis.";
RL Eur. J. Immunol. 30:568-576(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RX PubMed=11513955; DOI=10.1016/s0167-4781(01)00261-5;
RA Roda-Navarro P., Hernanz-Falcon P., Arce I., Fernandez-Ruiz E.;
RT "Molecular characterization of two novel alternative spliced variants of
RT the KLRF1 gene and subcellular distribution of KLRF1 isoforms.";
RL Biochim. Biophys. Acta 1520:141-146(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RC TISSUE=Lymphoid tissue;
RX PubMed=11265639;
RX DOI=10.1002/1521-4141(200101)31:1<233::aid-immu233>3.0.co;2-4;
RA Vitale M., Falco M., Castriconi R., Parolini S., Zambello R., Semenzato G.,
RA Biassoni R., Bottino C., Moretta L., Moretta A.;
RT "Identification of NKp80, a novel triggering molecule expressed by human
RT natural killer cells.";
RL Eur. J. Immunol. 31:233-242(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC -!- FUNCTION: Involved in the natural killer (NK)-mediated cytolysis of
CC PHA-induced lymphoblasts.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11265639}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NZS2-1; Sequence=Displayed;
CC Name=2; Synonyms=KLRF1-s1;
CC IsoId=Q9NZS2-2; Sequence=VSP_010391;
CC Name=3; Synonyms=KLRF1-s3;
CC IsoId=Q9NZS2-3; Sequence=VSP_010390, VSP_010392;
CC Name=4; Synonyms=KLRF1-s2;
CC IsoId=Q9NZS2-4; Sequence=VSP_010393, VSP_010394;
CC -!- TISSUE SPECIFICITY: Strongly expressed in peripheral blood leukocytes
CC and spleen, with weaker expression in lymph node and adult liver, and
CC no expression detected in bone marrow, thymus, and fetal liver. Not
CC expressed in brain, heart, placenta, lung, kidney, skeletal muscle, and
CC pancreas. Within peripheral blood leukocyte and immunocyte cell lines,
CC expression was predominant in NK cells but was also detected in
CC monocytes. {ECO:0000269|PubMed:10671213}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=KLRF1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_241";
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DR EMBL; AF175206; AAF37804.1; -; mRNA.
DR EMBL; AF175207; AAF37805.1; -; mRNA.
DR EMBL; AF267244; AAL14873.1; -; mRNA.
DR EMBL; AF267245; AAL14874.1; -; mRNA.
DR EMBL; AJ305370; CAC29425.1; -; mRNA.
DR EMBL; AC007068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF573680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96124.1; -; Genomic_DNA.
DR EMBL; BC098354; AAH98354.1; -; mRNA.
DR CCDS; CCDS41750.1; -. [Q9NZS2-1]
DR CCDS; CCDS76526.1; -. [Q9NZS2-2]
DR CCDS; CCDS76527.1; -. [Q9NZS2-3]
DR RefSeq; NP_001278751.1; NM_001291822.1. [Q9NZS2-2]
DR RefSeq; NP_001278752.1; NM_001291823.1. [Q9NZS2-3]
DR RefSeq; NP_057607.1; NM_016523.2. [Q9NZS2-1]
DR AlphaFoldDB; Q9NZS2; -.
DR SMR; Q9NZS2; -.
DR BioGRID; 119491; 19.
DR DIP; DIP-58613N; -.
DR IntAct; Q9NZS2; 1.
DR STRING; 9606.ENSP00000483713; -.
DR GlyGen; Q9NZS2; 4 sites.
DR iPTMnet; Q9NZS2; -.
DR PhosphoSitePlus; Q9NZS2; -.
DR BioMuta; KLRF1; -.
DR DMDM; 317373373; -.
DR PaxDb; Q9NZS2; -.
DR PeptideAtlas; Q9NZS2; -.
DR PRIDE; Q9NZS2; -.
DR Antibodypedia; 23183; 229 antibodies from 26 providers.
DR DNASU; 51348; -.
DR Ensembl; ENST00000279545.7; ENSP00000279545.4; ENSG00000150045.12. [Q9NZS2-2]
DR Ensembl; ENST00000354855.7; ENSP00000346919.3; ENSG00000150045.12. [Q9NZS2-3]
DR Ensembl; ENST00000612321.4; ENSP00000483880.1; ENSG00000150045.12. [Q9NZS2-4]
DR Ensembl; ENST00000617889.5; ENSP00000483713.1; ENSG00000150045.12. [Q9NZS2-1]
DR GeneID; 51348; -.
DR KEGG; hsa:51348; -.
DR MANE-Select; ENST00000617889.5; ENSP00000483713.1; NM_016523.3; NP_057607.1.
DR UCSC; uc009zgy.4; human. [Q9NZS2-1]
DR CTD; 51348; -.
DR DisGeNET; 51348; -.
DR GeneCards; KLRF1; -.
DR HGNC; HGNC:13342; KLRF1.
DR HPA; ENSG00000150045; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 605029; gene.
DR neXtProt; NX_Q9NZS2; -.
DR OpenTargets; ENSG00000150045; -.
DR PharmGKB; PA30169; -.
DR VEuPathDB; HostDB:ENSG00000150045; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000163227; -.
DR HOGENOM; CLU_197693_0_0_1; -.
DR InParanoid; Q9NZS2; -.
DR OMA; SWSDSYR; -.
DR OrthoDB; 1341815at2759; -.
DR PhylomeDB; Q9NZS2; -.
DR TreeFam; TF337735; -.
DR PathwayCommons; Q9NZS2; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q9NZS2; -.
DR BioGRID-ORCS; 51348; 8 hits in 1064 CRISPR screens.
DR ChiTaRS; KLRF1; human.
DR GenomeRNAi; 51348; -.
DR Pharos; Q9NZS2; Tbio.
DR PRO; PR:Q9NZS2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NZS2; protein.
DR Bgee; ENSG00000150045; Expressed in granulocyte and 99 other tissues.
DR ExpressionAtlas; Q9NZS2; baseline and differential.
DR Genevisible; Q9NZS2; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0032393; F:MHC class I receptor activity; TAS:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..231
FT /note="Killer cell lectin-like receptor subfamily F member
FT 1"
FT /id="PRO_0000046591"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 121..230
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 208..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 62..78
FT /note="VSQGVLLKCQKGSCSNA -> GFYTEKPKTIKLRMDWA (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:11513955"
FT /id="VSP_010393"
FT VAR_SEQ 62..64
FT /note="VSQ -> DSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11513955"
FT /id="VSP_010390"
FT VAR_SEQ 63..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10671213"
FT /id="VSP_010391"
FT VAR_SEQ 65..231
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11513955"
FT /id="VSP_010392"
FT VAR_SEQ 79..231
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11513955"
FT /id="VSP_010394"
FT VARIANT 67
FT /note="L -> F (in dbSNP:rs2232548)"
FT /id="VAR_047544"
SQ SEQUENCE 231 AA; 26563 MW; A2F7BE6D4341AFDE CRC64;
MQDEERYMTL NVQSKKRSSA QTSQLTFKDY SVTLHWYKIL LGISGTVNGI LTLTLISLIL
LVSQGVLLKC QKGSCSNATQ YEDTGDLKVN NGTRRNISNK DLCASRSADQ TVLCQSEWLK
YQGKCYWFSN EMKSWSDSYV YCLERKSHLL IIHDQLEMAF IQKNLRQLNY VWIGLNFTSL
KMTWTWVDGS PIDSKIFFIK GPAKENSCAA IKESKIFSET CSSVFKWICQ Y
