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Database: UniProt
Entry: A0A3M0KRB0_HIRRU
LinkDB: A0A3M0KRB0_HIRRU
Original site: A0A3M0KRB0_HIRRU 
ID   A0A3M0KRB0_HIRRU        Unreviewed;       794 AA.
AC   A0A3M0KRB0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Fibrinogen alpha chain {ECO:0000256|ARBA:ARBA00017850};
GN   ORFNames=DUI87_08957 {ECO:0000313|EMBL:RMC13874.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC13874.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMC13874.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMC13874.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMC13874.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) 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:RMC13874.1}.
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DR   EMBL; QRBI01000105; RMC13874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0KRB0; -.
DR   STRING; 333673.A0A3M0KRB0; -.
DR   Proteomes; UP000269221; 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; 1.
DR   Gene3D; 1.20.5.50; -; 1.
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   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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          551..792
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   REGION          299..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  88396 MW;  E3A07722A935381C CRC64;
     MRAESKGEWS LRQSIQRRIM NEQSQKLSFF EFEWEIFHGP QYILFDTNMQ AQDGESTFEQ
     VGAGVRGPRI VEHKSPSSCQ SEKSWPICAD DDWGTKCPSG CRMQGLIDEK DQEFSHRIDK
     IKKLLSDNQN NYKKSNQIIV ETVNALKPNL DSAQELDETY GRLSGELRRR IVTLKQRVVT
     QVNRIKALQS SIQEQVVEMK RLEVDIDIKI RACKGTCARS FDYKVDKESY DNIQKQLAQA
     NSINLHPELQ TTTLSTLKMR PLKDSNVPDH FKHKPLPEMQ ALNIINNIKQ MEVVLERPGT
     DAKLSRGDSS YHTAESRGDE PSHTSKLVIP THGRETLSLG DKTSSTVRRC TKTTTKKIVS
     GPDGPREEVV ERTVSSDGSD CSYLAGNVGG EGSTYHFSGA DGLHKLETVF PELESFFTPD
     SPSTATKHVS GSSSFTTSRH TTGTGSSHIG TGVSSHSGTY GGKDKLGDLG DEEEDDFGRL
     QPSGLPSGSA SHSKTVATSS SSFKNKGGSF ETKSVKIREI NERLGGLEHD QSAEDTPDFQ
     ARSFRPSGGK RRTPSTGKDC DDIRQKHTSG AKSGIFKIKP AGSNKVLSVY CDQETTLGGW
     LLIQQRMDGS VNFNRTWQDY KKGFGSVDGR GQGEFWLGNE NLHLLTQNGT LLRVELEDWD
     GNAVFAEYLV QVGSEAEGYT LAVSSYEGTA GDALIAGWLE EGTEYTSHAQ MKFSTFDRDQ
     DHWEENCAEM YGGGWWYNSC QAANLNGIYY PGGHYDPRYN VPYEIENGVV WLPFKASDYS
     LKTVRMKIRP IETL
//
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