CLC2G_MOUSE
ID CLC2G_MOUSE Reviewed; 269 AA.
AC Q9D676; Q1AFZ6; Q3UUY2; Q80Z35; Q8BHH6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=C-type lectin domain family 2 member G;
DE AltName: Full=DDV10;
DE AltName: Full=Osteoclast inhibitory lectin-related protein 1;
DE Short=Ocil-related protein 1;
GN Name=Clec2g; Synonyms=Clec2f, Ddv10, Ocilrp1;
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 [GENOMIC DNA / MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/Sv, and C57BL/6J;
RX PubMed=12374791; DOI=10.1074/jbc.m209059200;
RA Zhou H., Kartsogiannis V., Quinn J.M.W., Ly C., Gange C., Elliott J.,
RA Ng K.W., Gillespie M.T.;
RT "Osteoclast inhibitory lectin, a family of new osteoclast inhibitors.";
RL J. Biol. Chem. 277:48808-48815(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [3]
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 112-269, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Vagina;
RX PubMed=12746323; DOI=10.1210/en.2002-220980;
RA Katsu Y., Lubahn D.B., Iguchi T.;
RT "Expression of a novel C-type lectin in the mouse vagina.";
RL Endocrinology 144:2597-2605(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-261.
RC STRAIN=BALB/cByJ;
RX PubMed=16751398; DOI=10.4049/jimmunol.176.12.7511;
RA Carlyle J.R., Mesci A., Ljutic B., Belanger S., Tai L.-H., Rousselle E.,
RA Troke A.D., Proteau M.-F., Makrigiannis A.P.;
RT "Molecular and genetic basis for strain-dependent NK1.1 alloreactivity of
RT mouse NK cells.";
RL J. Immunol. 176:7511-7524(2006).
CC -!- FUNCTION: Inhibits osteoclast formation. {ECO:0000269|PubMed:12374791}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D676-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D676-2; Sequence=VSP_030529;
CC -!- TISSUE SPECIFICITY: Detected in vagina, eye, tongue, stomach and
CC spleen. {ECO:0000269|PubMed:12374791, ECO:0000269|PubMed:12746323}.
CC -!- INDUCTION: Constitutively expressed in bone marrow cells. Up-regulated
CC in vagina after 17-beta-estradiol treatment. Down-regulated after
CC removal of ovaries. {ECO:0000269|PubMed:12746323}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY137339; AAN15948.1; -; Genomic_DNA.
DR EMBL; AY137341; AAN15949.1; -; mRNA.
DR EMBL; AY137342; AAN15950.1; -; mRNA.
DR EMBL; AK014570; BAB29435.1; -; mRNA.
DR EMBL; AK137753; BAE23491.1; -; mRNA.
DR EMBL; BC117543; AAI17544.1; -; mRNA.
DR EMBL; AB091386; BAC65234.1; -; mRNA.
DR EMBL; DQ143107; ABA43358.1; -; Genomic_DNA.
DR CCDS; CCDS20578.1; -. [Q9D676-1]
DR CCDS; CCDS51921.1; -. [Q9D676-2]
DR RefSeq; NP_001161695.1; NM_001168223.1.
DR RefSeq; NP_001161696.1; NM_001168224.1. [Q9D676-2]
DR RefSeq; NP_001303681.1; NM_001316752.1.
DR RefSeq; NP_081838.1; NM_027562.4. [Q9D676-1]
DR AlphaFoldDB; Q9D676; -.
DR SMR; Q9D676; -.
DR STRING; 10090.ENSMUSP00000000254; -.
DR GlyGen; Q9D676; 1 site.
DR PhosphoSitePlus; Q9D676; -.
DR jPOST; Q9D676; -.
DR MaxQB; Q9D676; -.
DR PaxDb; Q9D676; -.
DR PRIDE; Q9D676; -.
DR ProteomicsDB; 279101; -. [Q9D676-1]
DR ProteomicsDB; 279102; -. [Q9D676-2]
DR DNASU; 70809; -.
DR Ensembl; ENSMUST00000000254; ENSMUSP00000000254; ENSMUSG00000000248. [Q9D676-1]
DR Ensembl; ENSMUST00000075789; ENSMUSP00000075192; ENSMUSG00000000248. [Q9D676-2]
DR Ensembl; ENSMUST00000142388; ENSMUSP00000115140; ENSMUSG00000000248. [Q9D676-2]
DR GeneID; 70809; -.
DR KEGG; mmu:70809; -.
DR UCSC; uc009eew.2; mouse. [Q9D676-1]
DR CTD; 70809; -.
DR MGI; MGI:1918059; Clec2g.
DR VEuPathDB; HostDB:ENSMUSG00000000248; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155319; -.
DR HOGENOM; CLU_049894_8_1_1; -.
DR InParanoid; Q9D676; -.
DR OMA; CRREKWN; -.
DR OrthoDB; 1289964at2759; -.
DR PhylomeDB; Q9D676; -.
DR TreeFam; TF351467; -.
DR BioGRID-ORCS; 70809; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q9D676; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9D676; protein.
DR Bgee; ENSMUSG00000000248; Expressed in lip and 30 other tissues.
DR ExpressionAtlas; Q9D676; baseline and differential.
DR Genevisible; Q9D676; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IC:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; IPI:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:MGI.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 2.
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; 2.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein; Lectin;
KW Membrane; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..269
FT /note="C-type lectin domain family 2 member G"
FT /id="PRO_0000315289"
FT TOPO_DOM 1..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 150..254
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 171..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12374791,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_030529"
FT CONFLICT 128
FT /note="A -> V (in Ref. 1; AAN15948/AAN15949/AAN15950)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="A -> V (in Ref. 4; BAC65234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30884 MW; D990E1B54C684152 CRC64;
MNITRASLPM LNTTCSCRRE KWNFLGRYEG TFDYWIGLHR ASSKHPWMWT DNTEYNNMFV
YHMNAQCLKK PEEGESSPGT GGVHSYKILQ RNSLRAISPE SSAKLYCCCG VIMVLTVAVV
ALSVALPATK TEQILINKTY AACPKNWIGV GNKCFYFSEY TSNWTFAQTF CMAQEAQLAR
FDNEKELNFL MRYKANFDSW IGLHRESSEH PWKWTDNTEY NNMIPIQGVE TCAYLSGNGI
SSSRHYIPRI WICSKLNNYS LHCPTPVPV
