FCN1B_XENLA
ID FCN1B_XENLA Reviewed; 318 AA.
AC Q7ZT72;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ficolin-1-B {ECO:0000305};
DE Flags: Precursor;
GN Name=fcn1-b {ECO:0000305}; Synonyms=fcn-4 {ECO:0000303|PubMed:12679857};
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:BAC76378.1};
RN [1] {ECO:0000312|EMBL:BAC76378.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000312|EMBL:BAC76378.1};
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).
CC -!- FUNCTION: May function in innate immunity through activation of the
CC lectin complement pathway. Binds to GalNAc and GlcNAc carbohydrate
CC moieties. {ECO:0000250|UniProtKB:O00602, ECO:0000250|UniProtKB:Q7ZT75}.
CC -!- SUBUNIT: Homotrimer. May form higher-order oligomers.
CC {ECO:0000250|UniProtKB:O00602, ECO:0000250|UniProtKB:Q7ZT75}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q7ZT75}.
CC -!- TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes. Also
CC detected at lower levels in spleen and lung.
CC {ECO:0000269|PubMed:12679857}.
CC -!- DOMAIN: The fibrinogen C-terminal domain mediates calcium-dependent
CC binding to carbohydrates. The domain undergoes a conformational switch
CC at pH under 6.2, and loses its carbohydrate-binding ability.
CC {ECO:0000250|UniProtKB:O00602}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q7ZT75}.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
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DR EMBL; AB091342; BAC76378.1; -; mRNA.
DR RefSeq; NP_001079139.1; NM_001085670.1.
DR AlphaFoldDB; Q7ZT72; -.
DR SMR; Q7ZT72; -.
DR GeneID; 373683; -.
DR KEGG; xla:373683; -.
DR CTD; 373683; -.
DR Xenbase; XB-GENE-6252862; fcn1.S.
DR OrthoDB; 1035379at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 373683; Expressed in internal ear and 4 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:0046872; F:metal ion 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 2: Evidence at transcript level;
KW Calcium; Collagen; Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Lectin; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:Q7ZT75"
FT CHAIN 20..318
FT /note="Ficolin-1-B"
FT /id="PRO_5004295318"
FT DOMAIN 42..99
FT /note="Collagen-like"
FT /evidence="ECO:0000255"
FT DOMAIN 100..318
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 273..275
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
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 287
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 261..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 318 AA; 34512 MW; C1C12FBDA8ABB304 CRC64;
MTRWVQTFLL LVAVIRSYAE DSCPDVKVIG VGASDKLTIL RGCPGIPGVP GPQGPSGPAG
AKGEKGFPGI PGKMGPTGLK GERGISGPKG QKGDKGDPGI PVVGMAQNCK EWLDQGASIS
GWYTIYTTNG LSLTVLCDME TDGGGWIVFQ RRMDGSVDFF QDWISYKRGF GRQDSEFWLG
NNNLHLLTVT GSFQLRVDLT DFGNNRTSAS YSDFRIAAEA QNYTLSLGTF TGGDAGDSLY
GHKNKGFSTK DRDNDSSPAS CAERYRGAWW YTSCHSSNLN GLYLRGNHSS FANGVNWKSG
RGYKYSYEVS EIKFRPQP
