ID CL180_CAEEL Reviewed; 896 AA.
AC Q19970; W6RRY7; W6RTK1; W6SBE9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 4.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=C-type lectin domain-containing protein 180;
DE Flags: Precursor;
GN Name=clec-180; ORFNames=F32E10.3;
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], AND ALTERNATIVE SPLICING.
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).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-133, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b;
CC IsoId=Q19970-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q19970-2; Sequence=VSP_054945;
CC Name=c;
CC IsoId=Q19970-3; Sequence=VSP_054946;
CC Name=d;
CC IsoId=Q19970-4; Sequence=VSP_054946, VSP_054945;
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DR EMBL; FO081278; CCD70434.1; -; Genomic_DNA.
DR EMBL; FO081278; CDM63532.1; -; Genomic_DNA.
DR EMBL; FO081278; CDM63533.1; -; Genomic_DNA.
DR EMBL; FO081278; CDM63534.1; -; Genomic_DNA.
DR RefSeq; NP_001294174.1; NM_001307245.1. [Q19970-1]
DR RefSeq; NP_001294175.1; NM_001307246.1.
DR RefSeq; NP_001294176.1; NM_001307247.1.
DR RefSeq; NP_501229.2; NM_068828.3. [Q19970-2]
DR AlphaFoldDB; Q19970; -.
DR SMR; Q19970; -.
DR BioGRID; 42652; 1.
DR STRING; 6239.F32E10.3b.1; -.
DR GlyCosmos; Q19970; 3 sites, No reported glycans.
DR iPTMnet; Q19970; -.
DR EPD; Q19970; -.
DR PaxDb; 6239-F32E10-3; -.
DR PeptideAtlas; Q19970; -.
DR EnsemblMetazoa; F32E10.3a.1; F32E10.3a.1; WBGene00017991. [Q19970-2]
DR EnsemblMetazoa; F32E10.3b.1; F32E10.3b.1; WBGene00017991. [Q19970-1]
DR EnsemblMetazoa; F32E10.3c.1; F32E10.3c.1; WBGene00017991. [Q19970-3]
DR EnsemblMetazoa; F32E10.3d.1; F32E10.3d.1; WBGene00017991. [Q19970-4]
DR GeneID; 177534; -.
DR KEGG; cel:CELE_F32E10.3; -.
DR UCSC; F32E10.3; c. elegans. [Q19970-1]
DR AGR; WB:WBGene00017991; -.
DR WormBase; F32E10.3a; CE37227; WBGene00017991; clec-180. [Q19970-2]
DR WormBase; F32E10.3b; CE29306; WBGene00017991; clec-180. [Q19970-1]
DR WormBase; F32E10.3c; CE49552; WBGene00017991; clec-180. [Q19970-3]
DR WormBase; F32E10.3d; CE49559; WBGene00017991; clec-180. [Q19970-4]
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_013642_0_0_1; -.
DR InParanoid; Q19970; -.
DR OMA; DCEATTR; -.
DR OrthoDB; 2883044at2759; -.
DR PRO; PR:Q19970; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00017991; Expressed in embryo and 4 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR45710; C-TYPE LECTIN DOMAIN-CONTAINING PROTEIN 180; 1.
DR PANTHER; PTHR45710:SF26; FI15750P1-RELATED; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Lectin;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..896
FT /note="C-type lectin domain-containing protein 180"
FT /id="PRO_0000250556"
FT DOMAIN 54..178
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 243..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 154..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 1..475
FT /note="Missing (in isoform c and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_054946"
FT VAR_SEQ 588..607
FT /note="Missing (in isoform a and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_054945"
SQ SEQUENCE 896 AA; 100266 MW; D7C62C7B2601ADC2 CRC64;
MRHLIFTGFV LTLTALEAVN VAKSTDNDIV LKVSTEKHSS RDSHHFSGEW LESPWGDLYQ
FRAGDQNWLT AREHCLSLNA DLAAIRNVEQ LDWILSHYAP LSSRFAQRLV QIGLYAPEGQ
THEWKWLNGN EINKTLLWSS GEPYDHSMEG RERCGLLNVE KRVLDDVDCE STSPDHHAQR
YICQRTSENH KQQQRSNNYI WQKIENLFSF FGIGGSPTPH NATIPNDYED EVLKNETSAT
VKSTVKFSDS EEETSSEEEE SVSKTLAALP KIEGSGESTA LKELQEPEGS GQIVEKKAIE
TTGDLVSGVD EEKLDKMINK MEEMIKSIDD LTVPPAVLER TTVSTVVLKK EEIVKQEKTD
EKKVEDKKET LANELNDNKI SESIEGDFDQ AQSKDMPKAD IEPPKEEDCD EEGSGSGSGE
EDEKDESSEK IELAPEKEDK IKEFLGVLRL FLDRAEHGDL RKLLDDQSGK TLLERMKNAV
REANRREFEM LEKLENSKKS EEEKEELAKK DQMSTEEQKD LYKKISSAVM KAAKIHKIEE
ADKVQDEQAM EKFNIAKVKA DSEEAESEGT VEVLKSAKEG KAEIKEKVGN DDYYGDYLDD
NNVIKIQNRE KKDAKEESSS DDKKSTDEKK KEIKKIEKTN KVNHDEPKKE EKKNEEQVKE
TKLESSTTVA KKEDVTTVAS TTEEPKSDKD SEGSGSDIEE STVSSAKPAE AEENEAELEA
SGHEEVSTTT ESTTVAVKEV PVDEIEKIAK LEAKQHTEDE KVTVETKQET AVTPAPTTSE
KTSTTAAPST KPAEETTTTT EAPSTTTKPV TVAVKKVSPE EMEKLVKKES TEKVTLLPPL
PTFTFPTLAP FTFPTLPTLA TTKPSPAPKV PTLEEILGNL NDQFKKLLSP PKPLPK
//
