ID I3NCZ9_ICTTR Unreviewed; 788 AA.
AC I3NCZ9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Fibrinogen alpha chain {ECO:0000256|ARBA:ARBA00017850};
GN Name=Fga {ECO:0000313|Ensembl:ENSSTOP00000022246.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000022246.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000022246.2}
RP IDENTIFICATION.
RG Ensembl;
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; AGTP01064903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3NCZ9; -.
DR STRING; 43179.ENSSTOP00000022246; -.
DR Ensembl; ENSSTOT00000019583.2; ENSSTOP00000022246.2; ENSSTOG00000024874.2.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157467; -.
DR HOGENOM; CLU_013807_0_0_1; -.
DR InParanoid; I3NCZ9; -.
DR TreeFam; TF351984; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR CDD; cd00087; FReD; 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; 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 InterPro; IPR021996; Fibrinogen_aC.
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; PF12160; Fibrinogen_aC; 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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..788
FT /note="Fibrinogen alpha chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012858956"
FT DOMAIN 545..786
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 264..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 138..172
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 274..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 87629 MW; AF7E0538E4708127 CRC64;
MFSMRIVCLV LSVVSTVWTA DTEKDEFLKK GGGVRGPRVV EGQQSDCKVG DWPVCADEEW
NQKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFDYQKNNK DSNTLTRNIM ELLRGDFANA
NNHDNTYNQV SEDLRSRIEI LKRKVIEKVQ QIQLLQNNVR AQLIDMKRLE VDIDIKIRSC
QGSCSRSVSR EIDLKDYENQ QRQLEQIISQ NLLPSADRQY LPLIKMTPVP DLVPGHYKSQ
LQKAPPEWKA LTEMQQMRMV LERHGREGSA RGDSPSYGTG SVTERPRNPG SSGTGPWNPG
SSRPGSGGNW NPGTAGSDGT GHWNPGSGHG SFRPESGGYG NTRPANPDWG EFEEMTGNIN
PGTKKEYSTG KLVTSKGEKE LLIGNEKVTS ASTTTSRRSC SKTITKTVIG ADGRREVTKE
VVNSEDPADC GDATDLDSMH RGSLADFSRL HPEEASFFET SSIGKTFPGL LPPSFKEFGS
KIQTMGSESD TGETGSLHDF PSSGKTSSHR KLVTMETKNY KMADEAGSEA GHEEFREAHT
IKRGHAKSRP SRDCDDVLQT HPSGAQSGIF NIKLPGSSKI FSVYCDQETS LGGWLLIQQR
MDGSLNFNRT WQDYKRGFGS LNDKGEGEFW LGNDYLHLLT QRGSILRVEL EDWDGKGAYA
EYHLRVGSEE EGYALQVSSY TGTAGDALIE GSVEEGTEYT SHNAMQFSTF DRDADQWEEN
CAEVYGGGWW YNNCQAANLN GIFYPGGSYD PRNNSPYEIE NGVVWVPFRG ADYSLRVVRM
KIRPLVSQ
//
