ID A0A0Q3PZX3_AMAAE Unreviewed; 1198 AA.
AC A0A0Q3PZX3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Fibrinogen alpha chain {ECO:0000256|ARBA:ARBA00017850};
GN ORFNames=AAES_83371 {ECO:0000313|EMBL:KQK81492.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK81492.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK81492.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK81492.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK81492.1}.
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DR EMBL; LMAW01002336; KQK81492.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3PZX3; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
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; 2.
DR Gene3D; 1.20.5.50; -; 2.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 2.
DR Gene3D; 4.10.530.10; Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2; 2.
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; 2.
DR Pfam; PF12160; Fibrinogen_aC; 1.
DR Pfam; PF00147; Fibrinogen_C; 2.
DR SMART; SM00186; FBG; 2.
DR SMART; SM01212; Fib_alpha; 2.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 2.
DR SUPFAM; SSF58010; Fibrinogen coiled-coil and central regions; 2.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 2.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 2.
PE 4: Predicted;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1198
FT /note="Fibrinogen alpha chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006206698"
FT DOMAIN 169..416
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DOMAIN 955..1196
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 822..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 134940 MW; C3C0D953F7F44681 CRC64;
MMVLRLQKWA ALGPLLSLLF STSVAYIATR ENCCILDERF GSYCPTTCGI ADFFNKYHLT
MDNELQEMER ILREIANSSI TADHLIQHIQ SLYPAEKQTL PNSVEDFTKK SKKIIEEIIR
YENTIFTHES TIQQLTDAHI MNSNRIAQLK QKIAHLESEC QEPCRDTAEI QETTGRDCQD
IANKGARKSG LYFIKPQKAK QSFLVYCEID SYGNGWTVLQ RRLDGSEDFR RNWVQYKEGF
GHLSPDDTTE FWLGNEKIHL ITTQSTLPYT LRIELEDWSG KKSTADYAVF KVGSEEDKYR
LTYAYFIGGE AGDAFDGFDF GDDPSDKSFT YHNGMRFSTY DNDNDNFAGN CAEQDGSGWW
MNRCHAGHLN GKYYIDGVYT SKDAGPSGYD NGIIWATWRD RWYSMKKTAM KIIPFNRLSV
DGQQHNLGSA KQMISMRILC VLLCLNLAWA QDGESTFEKE GGGVRGPRIV EHMSQSTCQY
EKNWPICADD DWGIKCPSGC RMQGLIDETD QDYSHRIDKI RKLLLENQNN YKKSNRIVVE
TVNVLKPNLD SAQKIDDDYG RVSGELRQRI VXLKQRVVTQ VNRIKALQSS IXEQVTEMKR
LEVDIDIKIR ACRGTCERSF DYQVDKESYD NIQKQLTQAN SINLHPELQT STLSTLKMRP
IKDSNVPEHF KHKPLPEMQA LNIINNIKQM QVVLERSETD TKPSRGDSVY LAAESRGDGP
SHTSKLVTPT HGRETISLGD KTSSTVRRCT KTTTKRVVTG PDGPREEVVE KTVSSDGSDC
SYLQGAGNVR EEGSVYHVGG TDGFHKLERI FPELESFFTP DSASTASKHF GGSSXVSSSS
HTTGTGSSHL GTGISSHSGT YGGKGKFTDL GEEEEDDFGG LHLQPSGFPS GSASHSKTVV
TSASSSFNKG GSTFETKSLK TREITEELGG VQHDQSAEDT PDFQARSIRP SRMKQRRAST
GKDCDDIRQK HTFGAKSGIF KIKPAGSNKV LSVYCDQETT LGGWLLIQQR MDGSVNFNRT
WQDYKRGFGS VDGKGQGEFW LGNENIHLLT QNNTLLRVEL EDWDGNAEYA EYIIQVGSEA
EGYALAVSSY EGTAGDALIE GWLEDGTEYT SHAQMRFSTF DRDQDRWEES CAEMYGGGWW
YNSCQAANLN GIYYLGGHYD PRYNVPYEIE NGVVWLPFRA SDYSLKIVRM KIRPIETM
//
