CL12B_MOUSE
ID CL12B_MOUSE Reviewed; 275 AA.
AC Q149M0; Q9D403;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=C-type lectin domain family 12 member B;
GN Name=Clec12b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inhibitory receptor postulated to negatively regulate immune
CC and non-immune functions (By similarity). Upon phosphorylation,
CC recruits SH2 domain-containing PTPN6 and PTPN11 phosphatases to its
CC ITIM motif and antagonizes activation signals (By similarity). Although
CC it inhibits KLRK1/NKG2D-mediated signaling, it does not bind known
CC ligands of KLRK1/NKG2D and therefore is not its inhibitory counterpart
CC (By similarity). May limit activation of myeloid cell subsets in
CC response to infection or tissue inflammation (By similarity). May
CC protect target cells against natural killer cell-mediated lysis (By
CC similarity). May negatively regulate cell cycle and differentiation of
CC melanocytes via inactivation of STAT3 (By similarity).
CC {ECO:0000250|UniProtKB:Q2HXU8}.
CC -!- SUBUNIT: Homodimer. Interacts (via ITIM motif) with PTPN6. Interacts
CC (via ITIM motif) with PTPN11; this interaction triggers
CC dephosphorylation and activation of PTPN11.
CC {ECO:0000250|UniProtKB:Q2HXU8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2HXU8};
CC Single-pass type II membrane protein {ECO:0000255}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC {ECO:0000250|UniProtKB:Q2HXU8}.
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DR EMBL; AK016908; BAB30491.1; -; mRNA.
DR EMBL; BC117712; AAI17713.1; -; mRNA.
DR CCDS; CCDS51922.1; -.
DR RefSeq; NP_001191152.1; NM_001204223.1.
DR RefSeq; NP_081985.1; NM_027709.2.
DR RefSeq; XP_006506675.1; XM_006506612.1.
DR AlphaFoldDB; Q149M0; -.
DR SMR; Q149M0; -.
DR STRING; 10090.ENSMUSP00000107713; -.
DR GlyGen; Q149M0; 3 sites.
DR PhosphoSitePlus; Q149M0; -.
DR PaxDb; Q149M0; -.
DR PRIDE; Q149M0; -.
DR ProteomicsDB; 281636; -.
DR GeneID; 71183; -.
DR KEGG; mmu:71183; -.
DR UCSC; uc009efm.2; mouse.
DR CTD; 387837; -.
DR MGI; MGI:1918433; Clec12b.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q149M0; -.
DR OrthoDB; 1201127at2759; -.
DR PhylomeDB; Q149M0; -.
DR TreeFam; TF336674; -.
DR BioGRID-ORCS; 71183; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q149M0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q149M0; protein.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; ISS:UniProtKB.
DR GO; GO:0030547; F:signaling receptor inhibitor activity; ISO:MGI.
DR GO; GO:0097325; P:melanocyte proliferation; ISS:UniProtKB.
DR GO; GO:0002769; P:natural killer cell inhibitory signaling pathway; ISO:MGI.
DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; ISS:UniProtKB.
DR GO; GO:2000272; P:negative regulation of signaling receptor activity; ISO:MGI.
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; IPR042916; CLEC12A/B.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR013600; Ly49_N.
DR InterPro; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47647; PTHR47647; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF08391; Ly49; 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 Cell membrane; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..275
FT /note="C-type lectin domain family 12 member B"
FT /id="PRO_0000313582"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 149..263
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 5..10
FT /note="ITIM motif"
FT /evidence="ECO:0000250|UniProtKB:Q2HXU8"
FT MOD_RES 7
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q2HXU8"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 171..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 241..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 22
FT /note="Q -> R (in Ref. 1; BAB30491)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="F -> L (in Ref. 1; BAB30491)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="D -> E (in Ref. 1; BAB30491)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="A -> T (in Ref. 1; BAB30491)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="S -> R (in Ref. 1; BAB30491)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="T -> R (in Ref. 1; BAB30491)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="T -> I (in Ref. 1; BAB30491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 31186 MW; D0921B8687BA53C2 CRC64;
MSDEVTYATL MLQDSARVRG NQDGNNLRKE GHPAQSSLWR GAALSLMTLC LVLVTGLVTL
ATMFLQVSND INSDSEKLSQ LQKSIHPQQD NLSESLNSSR KSLTEESLQS QISALLERQE
QMATKLCKEF LIHASDHKCN PCPKTWQWYG NSCYYFSINE EKSWSDSRKD CIDKNATLVK
IDSTEERDLL QSQLSLTFSF FWLGLSWNSS GRNWLWEDGS FPPPTLFSDK ELASFNGSRD
CAYFERGNIY ASRCSAEIPW ICEKTASLVK TEDLD
