FCN1A_XENLA
ID FCN1A_XENLA Reviewed; 315 AA.
AC Q7ZT75; Q3B8A5; Q5XG23;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ficolin-1-A {ECO:0000305};
DE Flags: Precursor;
GN Name=fcn1-a {ECO:0000305};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:BAC76375.1};
RN [1] {ECO:0000312|EMBL:BAC76375.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-54, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Liver {ECO:0000312|EMBL:BAC76375.1};
RX PubMed=12679857; DOI=10.1007/s00251-003-0552-2;
RA Kakinuma Y., Endo Y., Takahashi M., Nakata M., Matsushita M.,
RA Takenoshita S., Fujita T.;
RT "Molecular cloning and characterization of novel ficolins from Xenopus
RT laevis.";
RL Immunogenetics 55:29-37(2003).
RN [2] {ECO:0000312|EMBL:AAH84648.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-315.
RC TISSUE=Liver {ECO:0000312|EMBL:AAI06667.1}, and
RC Spleen {ECO:0000312|EMBL:AAH84648.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function in innate immunity through activation of the
CC lectin complement pathway (By similarity). Binds to GalNAc and GlcNAc
CC carbohydrate moieties (PubMed:12679857). {ECO:0000250|UniProtKB:O00602,
CC ECO:0000269|PubMed:12679857}.
CC -!- SUBUNIT: Homotrimer (By similarity). May form higher-order oligomers
CC (PubMed:12679857). {ECO:0000250|UniProtKB:O00602,
CC ECO:0000269|PubMed:12679857}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12679857}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in spleen, liver and heart. Also
CC detected at lower levels in lung. {ECO:0000269|PubMed:12679857}.
CC -!- DOMAIN: The fibrinogen C-terminal domain mediates binding to
CC carbohydrates. {ECO:0000250|UniProtKB:O00602}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12679857}.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC76375.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB091339; BAC76375.1; ALT_FRAME; mRNA.
DR EMBL; BC084648; AAH84648.1; -; mRNA.
DR EMBL; BC106666; AAI06667.1; -; mRNA.
DR RefSeq; NP_001082604.1; NM_001089135.1.
DR RefSeq; XP_018084222.1; XM_018228733.1.
DR AlphaFoldDB; Q7ZT75; -.
DR SMR; Q7ZT75; -.
DR GeneID; 398598; -.
DR KEGG; xla:398598; -.
DR CTD; 398598; -.
DR Xenbase; XB-GENE-6256022; fcn1.L.
DR OrthoDB; 1035379at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 398598; Expressed in liver and 14 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Collagen; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunity; Innate immunity; Lectin; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:12679857"
FT CHAIN 20..315
FT /note="Ficolin-1-A"
FT /id="PRO_5004298665"
FT DOMAIN 42..99
FT /note="Collagen-like"
FT /evidence="ECO:0000255"
FT DOMAIN 100..315
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 75..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 270..272
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 109..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 258..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CONFLICT 62
FT /note="K -> N (in Ref. 2; AAI06667)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="Q -> K (in Ref. 2; AAI06667)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="T -> P (in Ref. 2; AAI06667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 34353 MW; 3A9A12B6336414B5 CRC64;
MTRWVQTFLL LVAVIRSYAE DSCPDVKVIG VGASDKLTIL RGCPGIQGVP GPQGPAGPVG
AKGFAGARGI PGDIGPTGLK GEQGYPGARG LKGEKGDPGV PVPGTAQNCK EWLDQGVTIS
GWYTIYTPNG LTLSVLCDME TDGGGWIVFQ RRADGSVDFN RDWNSYKRGF GRKDSEFWLG
NDNLHLLTAT GNFQLRVDLT DFSDKSTYAS YSNFSIAEES QSYTLSLRSF MGGDAGDSLS
GHKNFSFSTK DRDNKSNCAH TFKGGWWYET CHYSNLNGLY LHGNHTSYAN GVNWSTGRGY
HYSYKVSEMK FRPQP
