CLC4F_MOUSE
ID CLC4F_MOUSE Reviewed; 548 AA.
AC P70194; Q8BLZ8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 160.
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 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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Takezawa R., Wagatsuma H., Nomoto C., Watanabe Y., Akaike T.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta;
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].
RC STRAIN=FVB/N; TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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_mou_Ctlect_166";
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DR EMBL; D88577; BAA13647.1; -; mRNA.
DR EMBL; AK040696; BAC30671.1; -; mRNA.
DR EMBL; BC013647; AAH13647.1; -; mRNA.
DR CCDS; CCDS20281.1; -.
DR RefSeq; NP_058031.2; NM_016751.3.
DR PDB; 6JJJ; X-ray; 2.79 A; A/B/C/D/E/F=389-548.
DR PDBsum; 6JJJ; -.
DR AlphaFoldDB; P70194; -.
DR SMR; P70194; -.
DR STRING; 10090.ENSMUSP00000014686; -.
DR UniLectin; P70194; -.
DR GlyGen; P70194; 6 sites.
DR iPTMnet; P70194; -.
DR PhosphoSitePlus; P70194; -.
DR CPTAC; non-CPTAC-3567; -.
DR jPOST; P70194; -.
DR MaxQB; P70194; -.
DR PaxDb; P70194; -.
DR PeptideAtlas; P70194; -.
DR PRIDE; P70194; -.
DR ProteomicsDB; 285468; -.
DR ABCD; P70194; 24 sequenced antibodies.
DR DNASU; 51811; -.
DR GeneID; 51811; -.
DR KEGG; mmu:51811; -.
DR UCSC; uc009cnv.1; mouse.
DR CTD; 165530; -.
DR MGI; MGI:1859834; Clec4f.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P70194; -.
DR OrthoDB; 988771at2759; -.
DR PhylomeDB; P70194; -.
DR TreeFam; TF333341; -.
DR BioGRID-ORCS; 51811; 4 hits in 73 CRISPR screens.
DR PRO; PR:P70194; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70194; protein.
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; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0005534; F:galactose binding; IDA:MGI.
DR GO; GO:0051861; F:glycolipid binding; IDA:MGI.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0051132; P:NK T cell activation; IMP:MGI.
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 3D-structure; Disulfide bond; Endocytosis; Glycoprotein; Lectin; Membrane;
KW Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..548
FT /note="C-type lectin domain family 4 member F"
FT /id="PRO_0000046623"
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..548
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 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
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"
FT CONFLICT 366
FT /note="T -> S (in Ref. 2; BAC30671)"
FT /evidence="ECO:0000305"
FT HELIX 397..413
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:6JJJ"
FT HELIX 433..442
FT /evidence="ECO:0007829|PDB:6JJJ"
FT HELIX 453..463
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 516..526
FT /evidence="ECO:0007829|PDB:6JJJ"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:6JJJ"
SQ SEQUENCE 548 AA; 61269 MW; 6F6495E820E73BD9 CRC64;
MKEAELNRDM ARYCTDNQCV SLQPQGLGPK SAALMAPRTL RHVQVILALM VVTVIFSLLA
LFVVASQPWR PEWNKEPPSL LLRGSNNSGH DNHSQFVRET EMQVAIQRLR DYEENSSSCH
KEVQILKYQM DNVSSLVQLL GSHLEDVNAD ILQTKDVLKE SGALALETQA LRSSLEVASA
DIHSLRGDLE KANAMTSQTR GLLKSSTENT SAELHVLGRG LEEAQSEIQA LRGSLQSAND
LSSQTQGFLQ HSMDNISAQI QTVRDGMERA GEKMNSLKKE LETLTAQTQK ANGHLEQTDA
QIQGLKAELK STSSLNSRIE VVNGQMKDAS RELQTLRRDL SDVSALKSNV QMLQSNLQRA
KTEMQTLKAD LQATKALTAK IQGEQNRLGA LQEAVAAQKQ EQKTQNQVLQ LIAQNWKYFN
GNFYYFSRDK KPWREAEKFC TSQGAHLASV TSQEEQAFLV QTTSSGDHWI GLTDQGTEGI
WRWVDGTPFN NAQSKGFWGK NQPDNWRHRN GEREDCVHVR QQWNDMACGS SYPWVCKKST
GWSAARVG
