FIBB_CHICK
ID FIBB_CHICK Reviewed; 463 AA.
AC Q02020;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Fibrinogen beta chain;
DE Contains:
DE RecName: Full=Fibrinopeptide B;
DE Contains:
DE RecName: Full=Fibrinogen beta chain;
DE Flags: Precursor; Fragment;
GN Name=FGB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-13 AND 18-39.
RX PubMed=2009266; DOI=10.1021/bi00227a017;
RA Weissbach L., Oddoux C., Procyk R., Grieninger G.;
RT "The beta chain of chicken fibrinogen contains an atypical thrombin
RT cleavage site.";
RL Biochemistry 30:3290-3294(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, AND
RP COILED COIL DOMAIN.
RX PubMed=10737772; DOI=10.1073/pnas.080065697;
RA Yang Z., Mochalkin I., Veerapandian L., Riley M., Doolittle R.F.;
RT "Crystal structure of native chicken fibrinogen at 5.5-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3907-3912(2000).
RN [3] {ECO:0007744|PDB:1M1J}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH CALCIUM, DISULFIDE
RP BONDS, SUBCELLULAR LOCATION, SUBUNIT, COILED COIL DOMAIN, AND GLYCOSYLATION
RP AT ASN-367.
RX PubMed=11601975; DOI=10.1021/bi011394p;
RA Yang Z., Kollman J.M., Pandi L., Doolittle R.F.;
RT "Crystal structure of native chicken fibrinogen at 2.7 A resolution.";
RL Biochemistry 40:12515-12523(2001).
CC -!- FUNCTION: Cleaved by the protease thrombin to yield monomers which,
CC together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG),
CC polymerize to form an insoluble fibrin matrix. Fibrin has a major
CC function in hemostasis as one of the primary components of blood clots.
CC {ECO:0000250|UniProtKB:E9PV24}.
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:0000269|PubMed:10737772, ECO:0000269|PubMed:11601975}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10737772,
CC ECO:0000269|PubMed:11601975}.
CC -!- DOMAIN: A long coiled coil structure formed by 3 polypeptide chains
CC connects the central nodule to the C-terminal domains (distal nodules).
CC The long C-terminal ends of the alpha chains fold back, contributing a
CC fourth strand to the coiled coil structure.
CC {ECO:0000269|PubMed:10737772, ECO:0000269|PubMed:11601975}.
CC -!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which
CC cleaves fibrinopeptides A and B from alpha and beta chains, and thus
CC exposes the N-terminal polymerization sites responsible for the
CC formation of the soft clot. The soft clot is converted into the hard
CC clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine
CC cross-linking between gamma chains (stronger) and between alpha chains
CC (weaker) of different monomers.
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DR EMBL; M58514; AAA48770.1; -; mRNA.
DR PIR; A38463; A38463.
DR RefSeq; NP_001161155.1; NM_001167683.1.
DR PDB; 1EI3; X-ray; 5.50 A; B/E=1-463.
DR PDB; 1M1J; X-ray; 2.70 A; B/E=1-463.
DR PDBsum; 1EI3; -.
DR PDBsum; 1M1J; -.
DR AlphaFoldDB; Q02020; -.
DR SMR; Q02020; -.
DR STRING; 9031.ENSGALP00000015057; -.
DR iPTMnet; Q02020; -.
DR PaxDb; Q02020; -.
DR GeneID; 373926; -.
DR KEGG; gga:373926; -.
DR CTD; 2244; -.
DR VEuPathDB; HostDB:geneid_373926; -.
DR eggNOG; KOG2579; Eukaryota.
DR HOGENOM; CLU_038628_13_0_1; -.
DR InParanoid; Q02020; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; Q02020; -.
DR EvolutionaryTrace; Q02020; -.
DR Proteomes; UP000000539; Unplaced.
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; IDA:CAFA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:CAFA.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
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; 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; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR InterPro; IPR037580; Fibrinogen_beta.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR19143:SF332; PTHR19143:SF332; 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; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Calcium; Coiled coil;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hemostasis;
KW Metal-binding; Reference proteome; Secreted; Sulfation.
FT PEPTIDE <1..17
FT /note="Fibrinopeptide B"
FT /evidence="ECO:0000269|PubMed:2009266"
FT /id="PRO_0000009093"
FT CHAIN 18..463
FT /note="Fibrinogen beta chain"
FT /id="PRO_0000009094"
FT DOMAIN 206..461
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11601975,
FT ECO:0007744|PDB:1M1J"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11601975,
FT ECO:0007744|PDB:1M1J"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11601975,
FT ECO:0007744|PDB:1M1J"
FT SITE 17..18
FT /note="Cleavage; by thrombin; to release fibrinopeptide B"
FT MOD_RES 5
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:11601975"
FT DISULFID 69
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:11601975, ECO:0007744|PDB:1M1J"
FT DISULFID 80
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:11601975, ECO:0007744|PDB:1M1J"
FT DISULFID 84
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 197
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:11601975, ECO:0007744|PDB:1M1J"
FT DISULFID 201
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 205..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:11601975, ECO:0007744|PDB:1M1J"
FT DISULFID 215..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:11601975, ECO:0007744|PDB:1M1J"
FT DISULFID 397..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739,
FT ECO:0000269|PubMed:11601975, ECO:0007744|PDB:1M1J"
FT NON_TER 1
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 85..162
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 164..196
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 324..334
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 343..352
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:1M1J"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:1M1J"
FT STRAND 451..459
FT /evidence="ECO:0007829|PDB:1M1J"
SQ SEQUENCE 463 AA; 52678 MW; 2044CD49BA79EC7B CRC64;
ASVEYDNEED SPQIDARAHR PLDKRQEAAP TLRPVAPPIS GTGYQPRPPK QDKQAMKKGP
IIYPDAGGCK HPLDELGVLC PTGCELQTTL LKQEKTVKPV LRDLKDRVAK FSDTSTTMYQ
YVNMIDNKLV KTQKQRKDND IILSEYNTEM ELHYNYIKDN LDNNIPSSLR VLRAVIDSLH
KKIQKLENAI ATQTDYCRSP CVASCNIPVV SGRECEDIYR KGGETSEMYI IQPDPFTTPY
RVYCDMETDN GGWTLIQNRQ DGSVNFGRAW DEYKRGFGNI AKSGGKKYCD TPGEYWLGND
KISQLTKIGP TKVLIEMEDW NGDKVSALYG GFTIHNEGNK YQLSVSNYKG NAGNALMEGA
SQLYGENRTM TIHNGMYFST YDRDNDGWLT TDPRKQCSKE DGGGWWYNRC HAANPNGRYY
WGGTYSWDMA KHGTDDGIVW MNWKGSWYSM KKMSMKIKPY FPD
