CL2DB_RAT
ID CL2DB_RAT Reviewed; 207 AA.
AC Q0H8B9; Q0H8B7; Q0H8B8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=C-type lectin domain family 2 member D11;
DE AltName: Full=C-type lectin-related protein B;
DE Short=Clr-b;
DE AltName: Full=Lectin-like transmembrane protein;
DE AltName: Full=Osteoclast inhibitory lectin;
GN Name=Clec2d11; Synonyms=Clrb, Ocil;
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 [MRNA], FUNCTION, AND INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=17462921; DOI=10.1016/j.immuni.2007.03.013;
RA Voigt S., Mesci A., Ettinger J., Fine J.H., Chen P., Chou W., Carlyle J.R.;
RT "Cytomegalovirus evasion of innate immunity by subversion of the NKR-
RT P1B:Ocil/Clr-b missing-self axis.";
RL Immunity 26:617-627(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Lewis, TO, and WAG;
RA Hundrieser J., Wonigeit K.;
RT "Polymorphism and expression of the rat homolog of the Ocil/Clrb gene.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-16, AND
RP IDENTIFICATION BY 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 -!- FUNCTION: Receptor for KLRB1B that protects target cells against
CC natural killer cell-mediated lysis. {ECO:0000269|PubMed:17462921}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: Down-regulated upon infection with rat cytomegalovirus.
CC {ECO:0000269|PubMed:17462921}.
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DR EMBL; EF100690; ABO15830.1; -; mRNA.
DR EMBL; DQ168417; ABA47204.1; -; mRNA.
DR EMBL; DQ168418; ABA47205.1; -; mRNA.
DR EMBL; DQ168419; ABA47206.1; -; mRNA.
DR RefSeq; NP_001041540.1; NM_001048075.1.
DR AlphaFoldDB; Q0H8B9; -.
DR SMR; Q0H8B9; -.
DR STRING; 10116.ENSRNOP00000037388; -.
DR GlyGen; Q0H8B9; 1 site.
DR iPTMnet; Q0H8B9; -.
DR PhosphoSitePlus; Q0H8B9; -.
DR PaxDb; Q0H8B9; -.
DR PRIDE; Q0H8B9; -.
DR GeneID; 362447; -.
DR KEGG; rno:362447; -.
DR UCSC; RGD:1563148; rat.
DR CTD; 70809; -.
DR RGD; 1563148; RGD1563148.
DR VEuPathDB; HostDB:ENSRNOG00000059538; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_049894_8_1_1; -.
DR InParanoid; Q0H8B9; -.
DR OMA; RCYSERG; -.
DR OrthoDB; 1289964at2759; -.
DR TreeFam; TF351467; -.
DR PRO; PR:Q0H8B9; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000059538; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; Q0H8B9; baseline and differential.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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; 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; 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 Cell membrane; Glycoprotein; Lectin; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..207
FT /note="C-type lectin domain family 2 member D11"
FT /id="PRO_0000315296"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 87..198
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 20
FT /note="G -> E (in Ref. 2; ABA47205)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="V -> F (in Ref. 2; ABA47205)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="Y -> L (in Ref. 2; ABA47205)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="G -> A (in Ref. 2; ABA47205)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="M -> L (in Ref. 2; ABA47205)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="S -> T (in Ref. 2; ABA47205)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..73
FT /note="KMTPQIST -> VKTEEISI (in Ref. 2; ABA47205)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="Y -> N (in Ref. 2; ABA47205)"
FT /evidence="ECO:0000305"
FT CONFLICT 120..121
FT /note="TE -> NQ (in Ref. 2; ABA47205)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="K -> R (in Ref. 2; ABA47206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 23537 MW; 5E7B44153111FD85 CRC64;
MSAKKASQPM LNTTGSLQEG EMGKMFHGKC LRIVSPESPA KLYCCYGVIM VLSVAVVALS
VALSVKMTPQ ISTINTYAAC PRNWIGVGNK CFYFSEYASN WTFSQTFCKA QEAELARFDT
EEELNFLSRY KGSFDYWIGL HRESSEHPWK WTDNTQYNYS LSIRGVERYA YLNDIGISSA
RVYADKRWSC SKLNSYSLQC KTPFSPM
