FCN2_PIG
ID FCN2_PIG Reviewed; 323 AA.
AC Q29041;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ficolin-2;
DE AltName: Full=Collagen/fibrinogen domain-containing protein 2;
DE AltName: Full=Ficolin-B;
DE AltName: Full=Ficolin-beta;
DE AltName: Full=L-ficolin;
DE Flags: Precursor;
GN Name=FCN2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=7686157; DOI=10.1016/s0021-9258(19)85267-5;
RA Ichijo H., Hellman U., Wernstedt C., Gonez L.J., Claesson-Welsh L.,
RA Heldin C.H., Miyazono K.;
RT "Molecular cloning and characterization of ficolin, a multimeric protein
RT with fibrinogen- and collagen-like domains.";
RL J. Biol. Chem. 268:14505-14513(1993).
CC -!- FUNCTION: May function in innate immunity through activation of the
CC lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin
CC (By similarity). {ECO:0000250|UniProtKB:Q15485}.
CC -!- SUBUNIT: Homotrimer. Interacts with elastin. Interacts with MASP1 and
CC MASP2. {ECO:0000250|UniProtKB:Q15485}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in skeletal muscle.
CC {ECO:0000269|PubMed:7686157}.
CC -!- DOMAIN: The fibrinogen-like domain (FBG) contains calcium-binding sites
CC that may be involved in carbohydrate binding.
CC {ECO:0000250|UniProtKB:Q15485}.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}.
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DR EMBL; L12344; AAA92455.1; -; mRNA.
DR PIR; A47172; A47172.
DR RefSeq; NP_999033.1; NM_213868.1.
DR AlphaFoldDB; Q29041; -.
DR SMR; Q29041; -.
DR PaxDb; Q29041; -.
DR PeptideAtlas; Q29041; -.
DR GeneID; 396881; -.
DR KEGG; ssc:396881; -.
DR CTD; 2220; -.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; Q29041; -.
DR OrthoDB; 1035379at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0001867; P:complement activation, lectin pathway; 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 Calcium; Collagen; Complement activation lectin pathway; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Lectin; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..323
FT /note="Ficolin-2"
FT /id="PRO_0000269571"
FT DOMAIN 52..102
FT /note="Collagen-like"
FT DOMAIN 106..323
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 55..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..136
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT DISULFID 115..143
FT /evidence="ECO:0000250|UniProtKB:O00602"
FT DISULFID 267..280
FT /evidence="ECO:0000250|UniProtKB:O00602"
SQ SEQUENCE 323 AA; 34682 MW; 849BF031D77E16B7 CRC64;
MDTRGVAAAM RPLVLLVAFL CTAAPALDTC PEVKVVGLEG SDKLSILRGC PGLPGAAGPK
GEAGASGPKG GQGPPGAPGE PGPPGPKGDR GEKGEPGPKG ESWETEQCLT GPRTCKELLT
RGHILSGWHT IYLPDCQPLT VLCDMDTDGG GWTVFQRRSD GSVDFYRDWA AYKRGFGSQL
GEFWLGNDHI HALTAQGTNE LRVDLVDFEG NHQFAKYRSF QVADEAEKYM LVLGAFVEGN
AGDSLTSHNN SLFTTKDQDN DQYASNCAVL YQGAWWYNSC HVSNLNGRYL GGSHGSFANG
VNWSSGKGYN YSYKVSEMKF RAT
