ID A0A6I9YU98_9SAUR Unreviewed; 691 AA.
AC A0A6I9YU98;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE SubName: Full=Fibrinogen alpha chain {ECO:0000313|RefSeq:XP_013927611.1};
GN Name=FGA {ECO:0000313|RefSeq:XP_013927611.1};
OS Thamnophis sirtalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Colubridae; Natricinae; Thamnophis.
OX NCBI_TaxID=35019 {ECO:0000313|Proteomes:UP000504617, ECO:0000313|RefSeq:XP_013927611.1};
RN [1] {ECO:0000313|RefSeq:XP_013927611.1}
RP IDENTIFICATION.
RC TISSUE=Skeletal muscle {ECO:0000313|RefSeq:XP_013927611.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Initiates complement activation and/or interferes in platelet
CC aggregation and/or blood coagulation. {ECO:0000256|ARBA:ARBA00003654}.
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}.
CC -!- SIMILARITY: Belongs to the ficolin lectin family. Veficolin subfamily.
CC {ECO:0000256|ARBA:ARBA00006932}.
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DR RefSeq; XP_013927611.1; XM_014072136.1.
DR AlphaFoldDB; A0A6I9YU98; -.
DR GeneID; 106553597; -.
DR KEGG; tsr:106553597; -.
DR CTD; 2243; -.
DR OrthoDB; 9945370at2759; -.
DR Proteomes; UP000504617; Unplaced.
DR GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:TreeGrafter.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:TreeGrafter.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0072377; P:blood coagulation, common pathway; IEA:TreeGrafter.
DR GO; GO:0042730; P:fibrinolysis; IEA:TreeGrafter.
DR GO; GO:0070527; P:platelet aggregation; IEA:TreeGrafter.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IEA:TreeGrafter.
DR GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR CDD; cd00087; FReD; 1.
DR FunFam; 3.90.215.10:FF:000001; Tenascin isoform 1; 1.
DR Gene3D; 1.20.5.50; -; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR Gene3D; 4.10.530.10; Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2; 1.
DR InterPro; IPR037579; FIB_ANG-like.
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; IPR020837; Fibrinogen_CS.
DR NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR47221; FIBRINOGEN ALPHA CHAIN; 1.
DR PANTHER; PTHR47221:SF3; FIBRINOGEN ALPHA 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; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 3: Inferred from homology;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Complement system impairing toxin {ECO:0000256|ARBA:ARBA00023220};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Hemostasis impairing toxin {ECO:0000256|ARBA:ARBA00023240};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000504617};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Toxin {ECO:0000256|ARBA:ARBA00023240}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..691
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5026827954"
FT DOMAIN 448..689
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 424..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..176
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 424..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 77818 MW; 7570794BB15FAC5F CRC64;
MFPLRILCAL LSFSIALVTS AEPTLEEVRG LEEEIIRGPR IVEHQAQGDC KSDKDWPICG
DEHWGIKCPS GCRMQGLIDE ANQDFQNRIE NIKRALSDNQ NSYKSSNNLK QEIFNYLERY
LPSEQELNKN YGQISDDLRR RLVTLKQRVA DKVERIKTLQ NSIHNQVGEL KRLEVDIDIK
IRACKGSCAH VFNYNVDTES YTNIQKQLVQ VNAIKMVSEE EGFPLKTLKI TEVKDSPAPI
RYKSAALTEQ EVSLLDTIKL FKVVLEDPKG SSADPKYAAP EAGVFGKPPI SKAIIRPSTD
VRTSHTCIKT TTTKIIRGPG GLREETVEEY KTPDGSDCSH LEGFIKEAIS SGAGGSGSHD
FVPHHPEADS GTLTFSHTKT QEGDPFSEVG EDEFDDFSRF DDFSQGGHTK TIIGTKSRVI
ETEEIQHDEN TERNTGLEEQ SFNAEEKFGK GNIGTDCEDI HQKHTSGAQS GIFRITPAGS
AKVFSVYCDQ ETTLGGWLLI QQRLDGSLNF NRTWEDYKKG FGSLDVKGRG EFWLGNENLH
ILTQKDTVLR VELEDWEGDK VYAEYNINIG SESEGYRLRV SNYKGTAGDA LIRGSEEDGT
EYTSHTSMKF STYDRDSDQW EENCAEVYGG GWWYNNCQAA NLNGIYYSSG QYDPRNNVPY
EIENGVIWLP FRPSDYSLKV VRMKIRPVET D
//
