KLRF2_HUMAN
ID KLRF2_HUMAN Reviewed; 207 AA.
AC D3W0D1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Killer cell lectin-like receptor subfamily F member 2;
DE Short=Lectin-like receptor F2;
DE AltName: Full=Activating coreceptor NKp65;
GN Name=KLRF2;
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], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT,
RP GLYCOSYLATION, INTERACTION WITH CLEC2A, AND MUTAGENESIS OF TYR-7.
RX PubMed=20194751; DOI=10.1073/pnas.0913108107;
RA Spreu J., Kuttruff S., Stejfova V., Dennehy K.M., Schittek B., Steinle A.;
RT "Interaction of C-type lectin-like receptors NKp65 and KACL facilitates
RT dedicated immune recognition of human keratinocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5100-5105(2010).
RN [2]
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 [3]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 63-207 IN COMPLEX WITH CLEC2A,
RP INTERACTION WITH CLEC2A, AND DISULFIDE BONDS.
RX PubMed=23803857; DOI=10.1073/pnas.1303300110;
RA Li Y., Wang Q., Chen S., Brown P.H., Mariuzza R.A.;
RT "Structure of NKp65 bound to its keratinocyte ligand reveals basis for
RT genetically linked recognition in natural killer gene complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11505-11510(2013).
CC -!- FUNCTION: C-type lectin-like receptor involved in natural killer cell
CC mediated cytotoxicity and cytokine secretion in keratinocytes via its
CC interaction with CLEC2A. {ECO:0000269|PubMed:20194751}.
CC -!- SUBUNIT: Homodimer; non disulfide-linked. Interacts with CLEC2A.
CC {ECO:0000269|PubMed:20194751, ECO:0000269|PubMed:23803857}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20194751};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:20194751}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20194751}.
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DR EMBL; GQ398770; ADC80446.1; -; mRNA.
DR EMBL; AC091814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS53743.1; -.
DR RefSeq; NP_001177694.1; NM_001190765.1.
DR PDB; 4IOP; X-ray; 3.20 A; B=63-207.
DR PDBsum; 4IOP; -.
DR AlphaFoldDB; D3W0D1; -.
DR SMR; D3W0D1; -.
DR DIP; DIP-58610N; -.
DR IntAct; D3W0D1; 1.
DR STRING; 9606.ENSP00000438244; -.
DR GlyGen; D3W0D1; 2 sites.
DR iPTMnet; D3W0D1; -.
DR PhosphoSitePlus; D3W0D1; -.
DR BioMuta; KLRF2; -.
DR PaxDb; D3W0D1; -.
DR PRIDE; D3W0D1; -.
DR Antibodypedia; 69740; 58 antibodies from 12 providers.
DR DNASU; 100431172; -.
DR Ensembl; ENST00000535540.1; ENSP00000438244.1; ENSG00000256797.1.
DR GeneID; 100431172; -.
DR KEGG; hsa:100431172; -.
DR MANE-Select; ENST00000535540.1; ENSP00000438244.1; NM_001190765.1; NP_001177694.1.
DR UCSC; uc021quy.1; human.
DR CTD; 100431172; -.
DR GeneCards; KLRF2; -.
DR HGNC; HGNC:37646; KLRF2.
DR HPA; ENSG00000256797; Tissue enriched (skin).
DR MIM; 618814; gene.
DR neXtProt; NX_D3W0D1; -.
DR OpenTargets; ENSG00000256797; -.
DR VEuPathDB; HostDB:ENSG00000256797; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000163993; -.
DR HOGENOM; CLU_049894_8_2_1; -.
DR InParanoid; D3W0D1; -.
DR OMA; ENEDGYM; -.
DR OrthoDB; 1341815at2759; -.
DR PhylomeDB; D3W0D1; -.
DR TreeFam; TF337735; -.
DR PathwayCommons; D3W0D1; -.
DR SignaLink; D3W0D1; -.
DR BioGRID-ORCS; 100431172; 13 hits in 1008 CRISPR screens.
DR Pharos; D3W0D1; Tbio.
DR PRO; PR:D3W0D1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; D3W0D1; protein.
DR Bgee; ENSG00000256797; Expressed in skin of leg and 35 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043320; P:natural killer cell degranulation; TAS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; TAS:UniProtKB.
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 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Lectin;
KW Membrane; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..207
FT /note="Killer cell lectin-like receptor subfamily F member
FT 2"
FT /id="PRO_0000404560"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 85..194
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:23803857"
FT DISULFID 106..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:23803857"
FT DISULFID 172..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:23803857"
FT MUTAGEN 7
FT /note="Y->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:20194751"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4IOP"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:4IOP"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:4IOP"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:4IOP"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4IOP"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4IOP"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4IOP"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4IOP"
SQ SEQUENCE 207 AA; 24008 MW; 561D6DD84D7B2156 CRC64;
MENEDGYMTL SFKNRCKSKQ KSKDFSLYPQ YYCLLLIFGC IVILIFIMTG IDLKFWHKKM
DFSQNVNVSS LSGHNYLCPN DWLLNEGKCY WFSTSFKTWK ESQRDCTQLQ AHLLVIQNLD
ELEFIQNSLK PGHFGWIGLY VTFQGNLWMW IDEHFLVPEL FSVIGPTDDR SCAVITGNWV
YSEDCSSTFK GICQRDAILT HNGTSGV
