CL17A_HUMAN
ID CL17A_HUMAN Reviewed; 378 AA.
AC Q6ZS10; A8MX68; B2RTX0; B7ZMM4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=C-type lectin domain family 17, member A;
DE AltName: Full=Prolectin;
GN Name=CLEC17A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC TISSUE=Spleen;
RX PubMed=19419970; DOI=10.1074/jbc.m109.012807;
RA Graham S.A., Jegouzo S.A., Yan S., Powlesland A.S., Brady J.P.,
RA Taylor M.E., Drickamer K.;
RT "Prolectin, a glycan-binding receptor on dividing B cells in germinal
RT centers.";
RL J. Biol. Chem. 284:18537-18544(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Peripheral blood monocyte;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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: Cell surface receptor which may be involved in carbohydrate-
CC mediated communication between cells in the germinal center. Binds
CC glycans with terminal alpha-linked mannose or fucose residues.
CC {ECO:0000269|PubMed:19419970}.
CC -!- SUBUNIT: Oligomer; disulfide-linked. {ECO:0000269|PubMed:19419970}.
CC -!- INTERACTION:
CC Q6ZS10; P07307-3: ASGR2; NbExp=3; IntAct=EBI-11977093, EBI-12808270;
CC Q6ZS10; P27449: ATP6V0C; NbExp=3; IntAct=EBI-11977093, EBI-721179;
CC Q6ZS10; P56748: CLDN8; NbExp=3; IntAct=EBI-11977093, EBI-10215641;
CC Q6ZS10; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-11977093, EBI-11977093;
CC Q6ZS10; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-11977093, EBI-12019274;
CC Q6ZS10; Q07325: CXCL9; NbExp=3; IntAct=EBI-11977093, EBI-3911467;
CC Q6ZS10; Q92520: FAM3C; NbExp=3; IntAct=EBI-11977093, EBI-2876774;
CC Q6ZS10; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-11977093, EBI-13345167;
CC Q6ZS10; P24593: IGFBP5; NbExp=4; IntAct=EBI-11977093, EBI-720480;
CC Q6ZS10; O43639: NCK2; NbExp=3; IntAct=EBI-11977093, EBI-713635;
CC Q6ZS10; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-11977093, EBI-10317425;
CC Q6ZS10; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-11977093, EBI-2804156;
CC Q6ZS10; Q96FA3: PELI1; NbExp=3; IntAct=EBI-11977093, EBI-448369;
CC Q6ZS10; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-11977093, EBI-448407;
CC Q6ZS10; Q9NS64: RPRM; NbExp=4; IntAct=EBI-11977093, EBI-1052363;
CC Q6ZS10; Q15436: SEC23A; NbExp=3; IntAct=EBI-11977093, EBI-81088;
CC Q6ZS10; Q9BZL3: SMIM3; NbExp=6; IntAct=EBI-11977093, EBI-741850;
CC Q6ZS10; P48230: TM4SF4; NbExp=3; IntAct=EBI-11977093, EBI-8650934;
CC Q6ZS10; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-11977093, EBI-2844246;
CC Q6ZS10; Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-11977093, EBI-11994282;
CC Q6ZS10; A2RU14: TMEM218; NbExp=3; IntAct=EBI-11977093, EBI-10173151;
CC Q6ZS10; O00526: UPK2; NbExp=3; IntAct=EBI-11977093, EBI-10179682;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}. Note=In fibroblasts, expressed on the
CC cell surface. {ECO:0000269|PubMed:19419970}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZS10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZS10-2; Sequence=VSP_039405, VSP_039406;
CC Name=3;
CC IsoId=Q6ZS10-3; Sequence=VSP_039407, VSP_039408;
CC -!- TISSUE SPECIFICITY: Expressed on dividing B-cells of germinal centers
CC in various tissues, including lymph nodes, tonsils, stomach, intestine,
CC appendix and spleen. {ECO:0000269|PubMed:19419970}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:19419970}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW84437.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK127809; BAC87146.1; -; mRNA.
DR EMBL; AC010527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84437.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC140848; AAI40849.1; -; mRNA.
DR EMBL; BC144665; AAI44666.1; -; mRNA.
DR CCDS; CCDS46002.2; -. [Q6ZS10-3]
DR CCDS; CCDS56087.1; -. [Q6ZS10-1]
DR RefSeq; NP_001191047.1; NM_001204118.1. [Q6ZS10-1]
DR RefSeq; NP_997273.3; NM_207390.3. [Q6ZS10-3]
DR AlphaFoldDB; Q6ZS10; -.
DR SMR; Q6ZS10; -.
DR BioGRID; 132718; 23.
DR IntAct; Q6ZS10; 22.
DR STRING; 9606.ENSP00000393719; -.
DR GlyGen; Q6ZS10; 3 sites.
DR iPTMnet; Q6ZS10; -.
DR PhosphoSitePlus; Q6ZS10; -.
DR BioMuta; CLEC17A; -.
DR DMDM; 300669632; -.
DR MassIVE; Q6ZS10; -.
DR PaxDb; Q6ZS10; -.
DR PeptideAtlas; Q6ZS10; -.
DR PRIDE; Q6ZS10; -.
DR ProteomicsDB; 68178; -. [Q6ZS10-1]
DR ProteomicsDB; 68179; -. [Q6ZS10-2]
DR ProteomicsDB; 68180; -. [Q6ZS10-3]
DR Antibodypedia; 50548; 53 antibodies from 11 providers.
DR DNASU; 388512; -.
DR Ensembl; ENST00000339847.9; ENSP00000341620.5; ENSG00000187912.12. [Q6ZS10-2]
DR Ensembl; ENST00000417570.6; ENSP00000393719.2; ENSG00000187912.12. [Q6ZS10-1]
DR Ensembl; ENST00000547437.5; ENSP00000450065.1; ENSG00000187912.12. [Q6ZS10-3]
DR GeneID; 388512; -.
DR KEGG; hsa:388512; -.
DR MANE-Select; ENST00000417570.6; ENSP00000393719.2; NM_001204118.2; NP_001191047.1.
DR UCSC; uc010dzn.3; human. [Q6ZS10-1]
DR CTD; 388512; -.
DR DisGeNET; 388512; -.
DR GeneCards; CLEC17A; -.
DR HGNC; HGNC:34520; CLEC17A.
DR HPA; ENSG00000187912; Group enriched (intestine, lymphoid tissue).
DR MIM; 616838; gene.
DR neXtProt; NX_Q6ZS10; -.
DR OpenTargets; ENSG00000187912; -.
DR PharmGKB; PA164717947; -.
DR VEuPathDB; HostDB:ENSG00000187912; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000163153; -.
DR HOGENOM; CLU_063069_0_0_1; -.
DR InParanoid; Q6ZS10; -.
DR OMA; FAEHNFV; -.
DR OrthoDB; 985894at2759; -.
DR PhylomeDB; Q6ZS10; -.
DR TreeFam; TF343491; -.
DR PathwayCommons; Q6ZS10; -.
DR SignaLink; Q6ZS10; -.
DR BioGRID-ORCS; 388512; 7 hits in 1061 CRISPR screens.
DR GenomeRNAi; 388512; -.
DR Pharos; Q6ZS10; Tbio.
DR PRO; PR:Q6ZS10; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6ZS10; protein.
DR Bgee; ENSG00000187912; Expressed in lymph node and 73 other tissues.
DR ExpressionAtlas; Q6ZS10; baseline and differential.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0042806; F:fucose binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Alternative splicing; Calcium; Disulfide bond; Glycoprotein; Lectin;
KW Mannose-binding; Membrane; Metal-binding; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..378
FT /note="C-type lectin domain family 17, member A"
FT /id="PRO_0000319428"
FT TOPO_DOM 1..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..378
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 261..373
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 254..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 282..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 350..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 248..265
FT /note="DCRRITCPEGWLPFEGKC -> EFCGQGPWLSTGVLAGAE (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039405"
FT VAR_SEQ 266..378
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039406"
FT VAR_SEQ 299..306
FT /note="NFVAKAHG -> LLGARGTQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039407"
FT VAR_SEQ 307..378
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039408"
SQ SEQUENCE 378 AA; 42935 MW; A2F0747289DABB6E CRC64;
MHNLYSITGY PDPPGTMEEE EEDDDYENST PPYKDLPPKP GTMEEEEEDD DYENSTPPYK
DLPPKPGTME EEEEDDDYEN STPPYKDLPP KPGSSAPPRP PRAAKETEKP PLPCKPRNMT
GLDLAAVTCP PPQLAVNLEP SPLQPSLAAT PVPWLNQRSG GPGCCQKRWM VYLCLLVVTS
LFLGCLGLTV TLIKYQELME ELRMLSFQQM TWRTNMTGMA GLAGLKHDIA RVRADTNQSL
VELWGLLDCR RITCPEGWLP FEGKCYYFSP STKSWDEARM FCQENYSHLV IINSFAEHNF
VAKAHGSPRV YWLGLNDRAQ EGDWRWLDGS PVTLSFWEPE EPNNIHDEDC ATMNKGGTWN
DLSCYKTTYW ICERKCSC
