FBCD1_MOUSE
ID FBCD1_MOUSE Reviewed; 459 AA.
AC A2AV25; Q6P9R8; Q8BJE7; Q8BL54;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Fibrinogen C domain-containing protein 1;
GN Name=Fibcd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acetyl group-binding receptor which shows a high-affinity and
CC calcium-dependent binding to acetylated structures such as chitin, some
CC N-acetylated carbohydrates, and amino acids, but not to their non-
CC acetylated counterparts. Can facilitate the endocytosis of acetylated
CC components (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AV25-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AV25-2; Sequence=VSP_026621;
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DR EMBL; AK046338; BAC32685.1; -; mRNA.
DR EMBL; AK084379; BAC39169.1; -; mRNA.
DR EMBL; AL929275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060634; AAH60634.2; -; mRNA.
DR CCDS; CCDS50564.1; -. [A2AV25-1]
DR RefSeq; NP_849218.2; NM_178887.4. [A2AV25-1]
DR AlphaFoldDB; A2AV25; -.
DR SMR; A2AV25; -.
DR STRING; 10090.ENSMUSP00000028188; -.
DR GlyGen; A2AV25; 1 site.
DR iPTMnet; A2AV25; -.
DR PhosphoSitePlus; A2AV25; -.
DR PaxDb; A2AV25; -.
DR PRIDE; A2AV25; -.
DR ProteomicsDB; 267574; -. [A2AV25-1]
DR ProteomicsDB; 267575; -. [A2AV25-2]
DR Antibodypedia; 31542; 80 antibodies from 17 providers.
DR DNASU; 98970; -.
DR Ensembl; ENSMUST00000028188; ENSMUSP00000028188; ENSMUSG00000026841. [A2AV25-1]
DR GeneID; 98970; -.
DR KEGG; mmu:98970; -.
DR UCSC; uc008jee.2; mouse. [A2AV25-1]
DR CTD; 84929; -.
DR MGI; MGI:2138953; Fibcd1.
DR VEuPathDB; HostDB:ENSMUSG00000026841; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000155976; -.
DR HOGENOM; CLU_038628_5_1_1; -.
DR InParanoid; A2AV25; -.
DR OMA; PQRMSCG; -.
DR OrthoDB; 523014at2759; -.
DR PhylomeDB; A2AV25; -.
DR TreeFam; TF351983; -.
DR BioGRID-ORCS; 98970; 4 hits in 74 CRISPR screens.
DR PRO; PR:A2AV25; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AV25; protein.
DR Bgee; ENSMUSG00000026841; Expressed in Ammon's horn and 49 other tissues.
DR Genevisible; A2AV25; MM.
DR GO; GO:0062023; C:collagen-containing 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:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
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; 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 Alternative splicing; Calcium; Chitin-binding; Disulfide bond;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..459
FT /note="Fibrinogen C domain-containing protein 1"
FT /id="PRO_0000294317"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 233..456
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 403
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 413
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 429
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT SITE 430
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 242..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 399..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VAR_SEQ 1..190
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026621"
FT CONFLICT 427
FT /note="A -> V (in Ref. 1; BAC32685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 50602 MW; 63D94371CB91A900 CRC64;
MVHERWKTVG SASQLEDRPR DKPQRASCSY VLCTVLLSLA VLLAVAVTGV VLFLNHTHTP
GTAPPPIVST GTAGANSALV TVERADSSHL SLLIDPRCPD LTDSFARLEG IQASILRALS
EHQAQPRLDG APELLDALAD QLPRLLTRAS ELQAECAGLR KGHSLLGQGL STLQSEQGRL
IQLLSESQGH MAHLVNSVSD VLEALQRERG LGRPRVKADL QRAPSRGARP RGCANGSRPR
DCLDVLLSGQ QDDGVYSIFP THYPAGFQVY CDMRTDGGGW TVFQRREDGS VNFFRGWEAY
REGFGKLTGE HWLGLKRIHA LTTQAAYELH VDLEDFDNGT AYAHYGSFGV GLFSVDPEED
GYPLTVADYS GTAGDSLLKH SGMRFTTKDR DSDHSENNCA AFYRGAWWYR NCHTSNLNGQ
YLRGAHASYA DGVEWSSWTG WQYSLKFSEM KIRPVREDR
