CLC4F_RAT
ID CLC4F_RAT Reviewed; 550 AA.
AC P10716; Q4KMB0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=C-type lectin domain family 4 member F;
DE AltName: Full=C-type lectin superfamily member 13;
DE Short=C-type lectin 13;
DE AltName: Full=Kupffer cell receptor;
GN Name=Clec4f; Synonyms=Clecsf13, Kclr;
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], AND PROTEIN SEQUENCE OF 83-104.
RX PubMed=2836387; DOI=10.1016/s0021-9258(18)68524-2;
RA Hoyle G.W., Hill R.L.;
RT "Molecular cloning and sequencing of a cDNA for a carbohydrate binding
RT receptor unique to rat Kupffer cells.";
RL J. Biol. Chem. 263:7487-7492(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1846367; DOI=10.1016/s0021-9258(18)52371-1;
RA Hoyle G.W., Hill R.L.;
RT "Structure of the gene for a carbohydrate-binding receptor unique to rat
RT Kupffer cells.";
RL J. Biol. Chem. 266:1850-1857(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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: Receptor with an affinity for galactose and fucose. Could be
CC involved in endocytosis.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Kupffer cells.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Kupffer cell receptor;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_rat_Ctlect_367";
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DR EMBL; J03734; AAA41472.1; -; mRNA.
DR EMBL; M55532; AAA40892.1; -; Genomic_DNA.
DR EMBL; BC098661; AAH98661.1; -; mRNA.
DR PIR; A38674; A28166.
DR RefSeq; NP_446205.1; NM_053753.1.
DR AlphaFoldDB; P10716; -.
DR SMR; P10716; -.
DR STRING; 10116.ENSRNOP00000017643; -.
DR GlyGen; P10716; 6 sites.
DR PaxDb; P10716; -.
DR PRIDE; P10716; -.
DR Ensembl; ENSRNOT00000017643; ENSRNOP00000017643; ENSRNOG00000013137.
DR GeneID; 114598; -.
DR KEGG; rno:114598; -.
DR UCSC; RGD:621062; rat.
DR CTD; 165530; -.
DR RGD; 621062; Clec4f.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01030000234575; -.
DR HOGENOM; CLU_030099_1_0_1; -.
DR InParanoid; P10716; -.
DR OMA; FQYSCYF; -.
DR OrthoDB; 988771at2759; -.
DR PhylomeDB; P10716; -.
DR TreeFam; TF333341; -.
DR PRO; PR:P10716; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000013137; Expressed in liver and 3 other tissues.
DR Genevisible; P10716; RN.
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:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0005534; F:galactose binding; ISO:RGD.
DR GO; GO:0051861; F:glycolipid binding; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; TAS:RGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0051132; P:NK T cell activation; ISO:RGD.
DR CDD; cd03590; CLECT_DC-SIGN_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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
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 Direct protein sequencing; Disulfide bond; Endocytosis; Glycoprotein;
KW Lectin; Membrane; Receptor; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..550
FT /note="C-type lectin domain family 4 member F"
FT /id="PRO_0000046624"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..69
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 438..538
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 440..536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 516..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 550 AA; 61104 MW; 9358A6CF4C306270 CRC64;
MKEAELNRDV AKFCTDNQCV ILQPQGLGPK SAAPMAPRTL RHVQAIVALV VVTVFFSLLA
LFVVVLQPWR QKQNEDHPVK AGLHGGNYSG SDNCSQFVRR AEMQEAIQSL RASGNSSSCH
KEIQTLKYQM DNVSSQVQLL GGHLEEANAD IQQAKDVLKG TGALASETQA LRSSLEVASA
DIHSLRGDLE KANAMTSQTQ GLLKSSTDNT SAELHVLGRG LEEAQSEIQA LRGSLQSSND
LGSRTQNFLQ HSMDNISAEI QAMRDGMQRA GEEMTSLKKD LETLTAQIQN ANGHLEQTDT
QIQGLKAQLK STSSLNSQIE VVNGKLKDSS RELQTLRRDL SDVSALKSNV QMLQSNLQKA
KAEVQSLKTG LEATKTLAAK IQGQQSDLEA LQKAVAAHTQ GQKTQNQVLQ LIMQDWKYFN
GKFYYFSRDK KSWHEAENFC VSQGAHLASV TSQEEQAFLV QITNAVDHWI GLTDQGTEGN
WRWVDGTPFD YVQSRRFWRK GQPDNWRHGN GEREDCVHLQ RMWNDMACGT AYNWVCKKST
DWSVARTDQS
