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Database: UniProt
Entry: Q6NYE1_DANRE
LinkDB: Q6NYE1_DANRE
Original site: Q6NYE1_DANRE 
ID   Q6NYE1_DANRE            Unreviewed;       485 AA.
AC   Q6NYE1; A0A8M1PI99;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   SubName: Full=Fibrinogen beta chain {ECO:0000313|Ensembl:ENSDARP00000016228, ECO:0000313|RefSeq:NP_997939.1};
DE   SubName: Full=Fibrinogen, B beta polypeptide {ECO:0000313|EMBL:AAH66629.1};
GN   Name=fgb {ECO:0000313|EMBL:AAH66629.1,
GN   ECO:0000313|Ensembl:ENSDARP00000016228,
GN   ECO:0000313|RefSeq:NP_997939.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-030131-9261};
GN   Synonyms=wu:fa55c11 {ECO:0000313|RefSeq:NP_997939.1}, zgc:77116
GN   {ECO:0000313|RefSeq:NP_997939.1};
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 {ECO:0000313|EMBL:AAH66629.1};
RN   [1] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11116086;
RA   Woods I.G., Kelly P.D., Chu F., Ngo-Hazelett P., Yan Y.L., Huang H.,
RA   Postlethwait J.H., Talbot W.S.;
RT   "A comparative map of the zebrafish genome.";
RL   Genome Res. 10:1903-1914(2000).
RN   [2] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15325340;
RA   Sharma M.K., Denovan-Wright E.M., Degrave A., Thisse C., Thisse B.,
RA   Wright J.M.;
RT   "Sequence, linkage mapping and early developmental expression of the
RT   intestinal-type fatty acid-binding protein gene (fabp2) from zebrafish
RT   (Danio rerio).";
RL   Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 138:391-398(2004).
RN   [3] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12949138; DOI=10.1093/molbev/msg224;
RA   Ruuskanen J.O., Xhaard H., Marjamaki A., Salaneck E., Salminen T.,
RA   Yan Y.L., Postlethwait J.H., Johnson M.S., Larhammar D., Scheinin M.;
RT   "Identification of duplicated fourth alpha2-adrenergic receptor subtype by
RT   cloning and mapping of five receptor genes in zebrafish.";
RL   Mol. Biol. Evol. 21:14-28(2004).
RN   [4] {ECO:0000313|EMBL:AAH66629.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAH66629.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18602103;
RA   Ruggeri B., Ubaldi M., Lourdusamy A., Soverchia L., Ciccocioppo R.,
RA   Hardiman G., Baker M.E., Palermo F., Polzonetti-Magni A.M.;
RT   "Variation of the genetic expression pattern after exposure to estradiol-
RT   17beta and 4-nonylphenol in male zebrafish (Danio rerio).";
RL   Gen. Comp. Endocrinol. 158:138-144(2008).
RN   [6] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19084604;
RA   Chang M.X., Wang Y.P., Nie P.;
RT   "Zebrafish peptidoglycan recognition protein SC (zfPGRP-SC) mediates
RT   multiple intracellular signaling pathways.";
RL   Fish Shellfish Immunol. 26:264-274(2009).
RN   [7] {ECO:0000313|Ensembl:ENSDARP00000016228}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000016228};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [8] {ECO:0000313|Ensembl:ENSDARP00000016228, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000016228};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   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   [9] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28252024;
RA   Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA   Choudhary J.S., Emes R.D., Grant S.G.;
RT   "Evolution of complexity in the zebrafish synapse proteome.";
RL   Nat. Commun. 8:14613-14613(2017).
RN   [10] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28300160;
RA   Eastlake K., Heywood W.E., Tracey-White D., Aquino E., Bliss E.,
RA   Vasta G.R., Mills K., Khaw P.T., Moosajee M., Limb G.A.;
RT   "Comparison of proteomic profiles in the zebrafish retina during
RT   experimental degeneration and regeneration.";
RL   Sci. Rep. 7:44601-44601(2017).
RN   [11] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29658397;
RA   Duan J., Liang S., Yu Y., Li Y., Wang L., Wu Z., Chen Y., Miller M.R.,
RA   Sun Z.;
RT   "Inflammation-coagulation response and thrombotic effects induced by silica
RT   nanoparticles in zebrafish embryos.";
RL   Nanotoxicology 12:470-484(2018).
RN   [12] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29649779;
RA   Yan C., Yang Q., Gong Z.;
RT   "Activation of Hepatic Stellate Cells During Liver Carcinogenesis Requires
RT   Fibrinogen/Integrin alphavbeta5 in Zebrafish.";
RL   Neoplasia 20:533-542(2018).
RN   [13] {ECO:0000313|RefSeq:NP_997939.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29274910;
RA   Wu T.S., Lin Y.T., Huang Y.T., Cheng Y.C., Yu F.Y., Liu B.H.;
RT   "Disruption of liver development and coagulation pathway by ochratoxin A in
RT   embryonic zebrafish.";
RL   Toxicol. Appl. Pharmacol. 340:1-8(2018).
RN   [14] {ECO:0000313|RefSeq:NP_997939.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-
CC       identical chains (alpha, beta and gamma). The 2 heterotrimers are in
CC       head to head conformation with the N-termini in a small central domain.
CC       {ECO:0000256|ARBA:ARBA00025974}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; BX548256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC066629; AAH66629.1; -; mRNA.
DR   RefSeq; NP_997939.1; NM_212774.1.
DR   IntAct; Q6NYE1; 1.
DR   STRING; 7955.ENSDARP00000016228; -.
DR   PaxDb; 7955-ENSDARP00000016228; -.
DR   Ensembl; ENSDART00000011701.7; ENSDARP00000016228.6; ENSDARG00000008969.12.
DR   GeneID; 337315; -.
DR   KEGG; dre:337315; -.
DR   AGR; ZFIN:ZDB-GENE-030131-9261; -.
DR   CTD; 2244; -.
DR   ZFIN; ZDB-GENE-030131-9261; fgb.
DR   eggNOG; KOG2579; Eukaryota.
DR   HOGENOM; CLU_038628_13_0_1; -.
DR   OMA; CIHADPD; -.
DR   OrthoDB; 3134470at2759; -.
DR   TreeFam; TF336658; -.
DR   Reactome; R-DRE-114608; Platelet degranulation.
DR   Reactome; R-DRE-140875; Common Pathway of Fibrin Clot Formation.
DR   Reactome; R-DRE-216083; Integrin cell surface interactions.
DR   Reactome; R-DRE-354192; Integrin signaling.
DR   Reactome; R-DRE-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-DRE-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-DRE-5674135; MAP2K and MAPK activation.
DR   Proteomes; UP000000437; Chromosome 1.
DR   Bgee; ENSDARG00000008969; Expressed in liver and 16 other cell types or tissues.
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:0005577; C:fibrinogen complex; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0072378; P:blood coagulation, fibrin clot formation; IMP:ZFIN.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 1.20.5.50; -; 2.
DR   Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR   InterPro; IPR037579; Fibrinogen.
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; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR   NCBIfam; NF040941; GGGWT_bact; 1.
DR   PANTHER; PTHR47221; FIBRINOGEN ALPHA CHAIN; 1.
DR   PANTHER; PTHR47221:SF4; FIBRINOGEN GAMMA CHAIN; 1.
DR   Pfam; PF08702; Fib_alpha; 1.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM01212; Fib_alpha; 1.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF58010; Fibrinogen coiled-coil and central regions; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q6NYE1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_997939.1}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..485
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_997939.1"
FT                   /id="PRO_5035036007"
FT   DOMAIN          227..482
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   REGION          27..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          190..217
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        27..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  54407 MW;  A3622504448B0FF3 CRC64;
     MKLVLLLCLC AVGALAQDDY DDYGEGKKEA KEVVDPRGHR PVSRGRETYS PGPVSQPPIS
     GGTRYRGRPT AAPVGKAVQE KEEQPESGGC NHMSEKMGVL CPTGCELKKA LIKQERNVKP
     TVEQLKRAVD DLTQSTNSIH GYVLDMTAEV AQRQKVSEGN GLVVDQYTDS LETQHAYIKD
     TVDVTFPQNI KVLQGVLDKI REKIQRLEKA ITTQRAKCQA PCKVTCPIPV VSGKECEDII
     RKGGEDSQMY IIRPDPLGTP YKVFCDQTSK NGGWVLIQNR MDGSVDFGRR WDDYRRGFGN
     IAFDVGKGHC QTPGEYWLGN DRISQLSKMG ATELLVEMED WSGSKVYAQY EQFSMQGEAS
     NYILGVGRYS GTAGNTFLEG ATELFGENRT MTIHNGMMFS TYDRDNDKWI PGDPSKQCSK
     EDGGGWWYNR CHSCNPNGRY YWGGAYTKYM AKHGTDDGIV WMNWKGSWYS LKTISMKIRP
     YFKQK
//
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