CL12A_MOUSE
ID CL12A_MOUSE Reviewed; 267 AA.
AC Q504P2; Q8BN96;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=C-type lectin domain family 12 member A;
DE AltName: Full=C-type lectin-like molecule 1;
DE Short=CLL-1;
DE AltName: Full=Myeloid inhibitory C-type lectin-like receptor;
DE Short=MICL;
DE AltName: CD_antigen=CD371;
GN Name=Clec12a; Synonyms=Micl;
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=Eye;
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].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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: Cell surface receptor that modulates signaling cascades and
CC mediates tyrosine phosphorylation of target MAP kinases. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTPN6 and PTPN11. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein. Note=Ligand binding leads to internalization. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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DR EMBL; AK084335; BAC39163.1; -; mRNA.
DR EMBL; BC094904; AAH94904.1; -; mRNA.
DR CCDS; CCDS20584.1; -.
DR RefSeq; NP_808354.1; NM_177686.4.
DR RefSeq; XP_011239625.1; XM_011241323.2.
DR AlphaFoldDB; Q504P2; -.
DR SMR; Q504P2; -.
DR STRING; 10090.ENSMUSP00000063627; -.
DR GlyGen; Q504P2; 3 sites.
DR iPTMnet; Q504P2; -.
DR PhosphoSitePlus; Q504P2; -.
DR jPOST; Q504P2; -.
DR MaxQB; Q504P2; -.
DR PaxDb; Q504P2; -.
DR PRIDE; Q504P2; -.
DR ProteomicsDB; 283565; -.
DR GeneID; 232413; -.
DR KEGG; mmu:232413; -.
DR UCSC; uc009efl.2; mouse.
DR CTD; 160364; -.
DR MGI; MGI:3040968; Clec12a.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q504P2; -.
DR OrthoDB; 1201127at2759; -.
DR PhylomeDB; Q504P2; -.
DR TreeFam; TF336674; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 232413; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q504P2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q504P2; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0030545; F:signaling receptor regulator activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47647; PTHR47647; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Lectin; Membrane; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..267
FT /note="C-type lectin domain family 12 member A"
FT /id="PRO_0000313579"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 140..247
FT /note="C-type lectin"
FT MOTIF 5..10
FT /note="ITIM motif"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..246
FT /evidence="ECO:0000250"
FT DISULFID 225..238
FT /evidence="ECO:0000250"
FT CONFLICT 90
FT /note="F -> S (in Ref. 1; BAC39163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 30757 MW; 2958572936E4A35D CRC64;
MSEEIVYANL KIQDPDKKEE TQKSDKCGGK VSADASHSQQ KTVLILILLC LLLFIGMGVL
GGIFYTTLAT EMIKSNQLQR AKEELQENVF LQLKHNLNSS KKIKNLSAML QSTATQLCRE
LYSKEPEHKC KPCPKGSEWY KDSCYSQLNQ YGTWQESVMA CSARNASLLK VKNKDVLEFI
KYKKLRYFWL ALLPRKDRTQ YPLSEKMFLS EESERSTDDI DKKYCGYIDR VNVYYTYCTD
ENNIICEETA SKVQLESVLN GLPEDSR
