CL161_CAEEL
ID CL161_CAEEL Reviewed; 862 AA.
AC P34472;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=C-type lectin domain-containing protein 161;
DE Flags: Precursor;
GN Name=clec-161; ORFNames=F58A4.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; Z22179; CAA80162.3; -; Genomic_DNA.
DR PIR; S40977; S40977.
DR RefSeq; NP_499125.3; NM_066724.3.
DR AlphaFoldDB; P34472; -.
DR SMR; P34472; -.
DR STRING; 6239.F58A4.5; -.
DR PaxDb; P34472; -.
DR EnsemblMetazoa; F58A4.5.1; F58A4.5.1; WBGene00010228.
DR GeneID; 176357; -.
DR KEGG; cel:CELE_F58A4.5; -.
DR UCSC; F58A4.5; c. elegans.
DR CTD; 176357; -.
DR WormBase; F58A4.5; CE43487; WBGene00010228; clec-161.
DR eggNOG; KOG1075; Eukaryota.
DR GeneTree; ENSGT01050000244928; -.
DR HOGENOM; CLU_006736_0_0_1; -.
DR InParanoid; P34472; -.
DR OMA; WENGGEI; -.
DR OrthoDB; 29241at2759; -.
DR Reactome; R-CEL-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-CEL-1482788; Acyl chain remodelling of PC.
DR Reactome; R-CEL-1482801; Acyl chain remodelling of PS.
DR Reactome; R-CEL-1482839; Acyl chain remodelling of PE.
DR Reactome; R-CEL-1482922; Acyl chain remodelling of PI.
DR Reactome; R-CEL-1482925; Acyl chain remodelling of PG.
DR Reactome; R-CEL-1483166; Synthesis of PA.
DR Reactome; R-CEL-6803157; Antimicrobial peptides.
DR PRO; PR:P34472; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010228; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR Gene3D; 3.10.100.10; -; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 3.
DR SMART; SM00034; CLECT; 3.
DR SUPFAM; SSF56436; SSF56436; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 3.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Lectin; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..862
FT /note="C-type lectin domain-containing protein 161"
FT /id="PRO_0000017569"
FT DOMAIN 41..154
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 562..687
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 716..828
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 162..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 653..678
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 807..819
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 862 AA; 95363 MW; FB3C0287BC085D27 CRC64;
MYRRTTLWFL LLFQPILVFA QNRTELYECK IGTVNPLAST SLNACFKLYN TPKSFQAARR
YCVSLGGQLA DKINKDDSSL YSANADLEVA NSTKFWVGAS NLKCNIAWEN GGEIEFNDMW
APESRYYGVA IDKMSIGGLW HTVPVGQKLP FVCTFQGKSN EAGPAPVHAM RAPAKKRVPK
VEKPEEKDID ESLNAALSDK KEKKEVASDK KKESKKDEED INESMNAALS DERKKSASLA
SSDKKESSKK DESSDEANLS ASQVANAEMS ASISASSANS SSDESSDEAY DSAEIEMRKK
IGKTVIAMKS QEMASQSDDY DKYTEEDLLS AAASLIGGYI LNAHWADSRT TNTSSFDSQT
DEETLNMMMA IAEQIAMTMR SSKRRESSSS NTDSESASIS ESSQASEQAV MAAAMSAKSS
KKSESSSKDE SEDSASLNLE QKASAAASAA LASKSKSDSS DQSKDQKSAN VALAVVSENK
HPTKKPEDPK STKTTTEEPD IDESLNAALA NQRSTTTKNS DLTTIITTVK PNALPIAIVA
KQSEKDPACP AEWTQFNTNA TAPALCFKRY EKPMNFEDAR LFCVGKGGHL ASIHNERQLL
LLSALLHNNG PDALSDQTWI GLNRIHQKYY VYEDETAMDF TRWLPGAPNI NDCTVFTGNE
LPNYPHKGTQ YKFGDFPCEE VQKSVLCEVT LGKDKLKSQT TCQDGWSYYS HDGTAKNGKC
YKRIDQSKKF SEAREVCKVE NSYVASVQNE GEARFVSALV QTEKNYTVDE QTWIGYVKYD
RDFGWEDGNK GLQFDPWTEK MPRQKKCTVF TGNEIHENCR SQFRFVSVDC NKTQRSVLCS
KPPMKNGTPF VYKDTDNSSK KI
