ID A0A3B3TG28_9TELE Unreviewed; 431 AA.
AC A0A3B3TG28;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Fibrinogen gamma chain {ECO:0000313|Ensembl:ENSPKIP00000041615.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000041615.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000041615.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3TG28; -.
DR Ensembl; ENSPKIT00000022651.1; ENSPKIP00000041615.1; ENSPKIG00000018048.1.
DR GeneTree; ENSGT00940000158467; -.
DR Proteomes; UP000261540; Unplaced.
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 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; IPR020837; Fibrinogen_CS.
DR NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR47221; FIBRINOGEN ALPHA CHAIN; 1.
DR PANTHER; PTHR47221:SF4; FIBRINOGEN GAMMA 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 4: Predicted;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..431
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017475019"
FT DOMAIN 163..410
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
SQ SEQUENCE 431 AA; 48865 MW; FF170EEBBD59B56A CRC64;
MAHLLIHSAL FLLLIFSMSS AEIRGDFDSC SPMDGFGKYC PTTCGVADYL NRYKPVVDRD
LNDLEYLLEE ISNQTKGAQD KVTYMRDSAT AAKKSNDPDV YIKKSTNMLD DILRFEKSII
SQESQIYKLQ ESIDSNEKRM LQLKQMILNL EQMCKLPCED TVKIQTVTGK DCQDVANKGG
RTSGLYFIKP LKAKEQFLVY CEMDNNGNGW TVLQRRRDGS VDFSRPWIPY KEGFGYLSPD
DTTEFWLGNE KMHLVTSQST VPYVLRIEMT DWEGNKKYAD YASFKVGPEA DSYRLIYAYH
LGGDAGDAFD GFDFGDDPSD KIFTSHNGMQ FSTSDRDNDK YDGNCATQDG SGWWMNRCHA
AHLNGKYYQG GKYTAEQAGP HGFDNGIIWA TWHSRWYSMK ETTMKIIPIN RMGTLGQQTT
GVKQMGGIGD I
//
