COL12_DANRE
ID COL12_DANRE Reviewed; 720 AA.
AC A5PMY6; Q08CB7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Collectin-12;
GN Name=colec12; ORFNames=si:ch211-212m21.5;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-560.
RC STRAIN=AB; TISSUE=Skin;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Scavenger receptor that displays several functions associated
CC with host defense. Binds to carbohydrates (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
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DR EMBL; BX927088; CAN88233.1; -; Genomic_DNA.
DR EMBL; BC124303; AAI24304.1; -; mRNA.
DR RefSeq; NP_001116312.1; NM_001122840.1.
DR AlphaFoldDB; A5PMY6; -.
DR SMR; A5PMY6; -.
DR STRING; 7955.ENSDARP00000111997; -.
DR PaxDb; A5PMY6; -.
DR PeptideAtlas; A5PMY6; -.
DR PRIDE; A5PMY6; -.
DR Ensembl; ENSDART00000086863; ENSDARP00000081297; ENSDARG00000061140.
DR GeneID; 558942; -.
DR KEGG; dre:558942; -.
DR CTD; 81035; -.
DR ZFIN; ZDB-GENE-030131-9807; colec12.
DR eggNOG; ENOG502QQKQ; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR InParanoid; A5PMY6; -.
DR OMA; TVMRHSD; -.
DR PhylomeDB; A5PMY6; -.
DR Reactome; R-DRE-3000480; Scavenging by Class A Receptors.
DR PRO; PR:A5PMY6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000061140; Expressed in zone of skin and 36 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; IBA:GO_Central.
DR GO; GO:0001570; P:vasculogenesis; IMP:ZFIN.
DR Gene3D; 3.10.100.10; -; 2.
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; IPR008160; Collagen.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF01391; Collagen; 3.
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 2: Evidence at transcript level;
KW Calcium; Coiled coil; Collagen; Disulfide bond; Lectin; Membrane;
KW Metal-binding; Receptor; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..720
FT /note="Collectin-12"
FT /id="PRO_0000318685"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..720
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 444..503
FT /note="Collagen-like 1"
FT DOMAIN 510..569
FT /note="Collagen-like 2"
FT DOMAIN 611..710
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 433..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..120
FT /evidence="ECO:0000255"
FT COILED 216..267
FT /evidence="ECO:0000255"
FT COILED 377..408
FT /evidence="ECO:0000255"
FT COMPBIAS 561..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 649
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 670
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 673
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 673
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 675
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 675
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 686
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 697
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 697
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 698
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 698
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 710
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT DISULFID 604..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 634..709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 687..701
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 80
FT /note="T -> M (in Ref. 2; AAI24304)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="Q -> R (in Ref. 2; AAI24304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 78035 MW; 0DD184C27C37E0AC CRC64;
MKDDFNDEEE VQSFGYKRFG IQEGNECTKC KNDWALRVAI ALLYVLCALL TIAVAVLGYK
VVQRMDNVTE GMQNYGGKIT AVETDLKKLD DQTGEKSENA TSELHSFKLE FQTLQKQLSD
VIVKTSNNRA VLKELQLAGE DMQSGHLSLR DLLESNANVI SKVNHTLNTY NSLIDGLKTE
TARLQSDLHV QTSEQGQNSH SISTLNFTQT QQRNLISSLQ RSVEDTGQAV QKLKNDYQSL
QQVARQTKAD ADWLREKVQN LQALAANNSL LTRSNSDSLE DVTSQLTTLS EQVQNTSTIT
DSHDQSLREL MDQQRDHDNA TSIRFDALEA RLDSNEGEMD RITGNVSFTT QLLRAISTDL
NGLRTCSETV TRHSELLHGL NNSVAETRAE STELKAQQEE LAVRLDKEVS SLSIVMDEMK
LVDNKHSQLI TNFTILQGPP GPRGPRGDKG SMGLPGKTGP KGEKGEKGAP GDAGPKGEKG
PAGPPGVPGL KGPPGSRGSP GPKGSRGSGG RQGPSGEKGD PGIPGMPGRD GQPGPTGPQG
PQGLRGPAGP AGLEGARGPV GPIGPPGPPG LPGLPAPPIV VPPVDPQGFV NRQVAPPPTT
TPGCPPQWKG FREQCYHFSA PMESLNFDEA KERCSNLSSS MLIINDEEEQ LWIKRQISGK
GYFWLGLKWK PGQPDNWSHG HEAGEDCAGL IHEASWNDFF CTERIGFICE RTNESKVPVL
