CLC2L_RAT
ID CLC2L_RAT Reviewed; 211 AA.
AC Q0ZCA7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=C-type lectin domain family 2 member L;
GN Name=Clec2l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-211.
RC STRAIN=Sprague-Dawley;
RA Cadet J.L., Cai N.S., Deng X.L., Jayanthi S., Ladenheim B., McCoy M.T.;
RT "Characterization of a novel CD69-like protein.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABG00196.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AABR03034016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03035221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ630549; ABG00196.1; ALT_INIT; mRNA.
DR RefSeq; NP_001037698.2; NM_001044233.2.
DR AlphaFoldDB; Q0ZCA7; -.
DR SMR; Q0ZCA7; -.
DR STRING; 10116.ENSRNOP00000060718; -.
DR iPTMnet; Q0ZCA7; -.
DR PhosphoSitePlus; Q0ZCA7; -.
DR PaxDb; Q0ZCA7; -.
DR Ensembl; ENSRNOT00000067097; ENSRNOP00000060718; ENSRNOG00000029644.
DR GeneID; 296985; -.
DR KEGG; rno:296985; -.
DR UCSC; RGD:1565373; rat.
DR CTD; 154790; -.
DR RGD; 1565373; Clec2l.
DR eggNOG; KOG1766; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162503; -.
DR HOGENOM; CLU_049894_8_4_1; -.
DR InParanoid; Q0ZCA7; -.
DR OMA; DCLMTRP; -.
DR OrthoDB; 1201127at2759; -.
DR PRO; PR:Q0ZCA7; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000029644; Expressed in frontal cortex and 18 other tissues.
DR ExpressionAtlas; Q0ZCA7; baseline and differential.
DR Genevisible; Q0ZCA7; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Lectin; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..211
FT /note="C-type lectin domain family 2 member L"
FT /id="PRO_0000339387"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 104..206
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT DISULFID 97..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 125..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 184..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 211 AA; 23623 MW; C04B5192E8760A4B CRC64;
MEPAREPPAR ARPPPPAARP APAAPRPRSP AEAEARGPEG LLRRSGSGYE GSTSWKAALE
DTTTRLLLGA IAVLLFAILV VMSILASKGC IKCETPCPED WLLYGRKCYY FSEEPRDWNT
GRQYCHTHEA ALAVIQSQKE LEFMFKFTRR EPWIGLRRVG DDFHWVNGDP FDPDTFTISG
TGECVFVEPT RLVSTECLTT RPWVCSKMAY T
