ID G1Q856_MYOLU Unreviewed; 437 AA.
AC G1Q856;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Fibrinogen gamma chain {ECO:0000313|Ensembl:ENSMLUP00000019889.1};
GN Name=FGG {ECO:0000313|Ensembl:ENSMLUP00000019889.1};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000019889.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000019889.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000019889.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAPE02001620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006081876.1; XM_006081814.2.
DR AlphaFoldDB; G1Q856; -.
DR Ensembl; ENSMLUT00000028309.1; ENSMLUP00000019889.1; ENSMLUG00000005542.2.
DR GeneTree; ENSGT00940000158467; -.
DR HOGENOM; CLU_038628_13_0_1; -.
DR Proteomes; UP000001074; 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 CDD; cd00890; Prefoldin; 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 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:UP000001074};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003418062"
FT DOMAIN 170..416
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT COILED 59..89
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 437 AA; 49864 MW; ADA770C1E869E820 CRC64;
MHWSLHPRSL ILYIYTLLFL SSTCLAFVPP TDNCCISEKR FGRYCPTTCG IADFLLNYQT
EVDQDLQSVE ETLRKIKNNT SEAKELIKKI QSVYNPDGLP KSDKIQAAIK ESQKMMEDII
KFESLIISHE SSIRFLKDIY NSNSQKIATL KQKVVQLEAK CQEPCKDTVK IHDITGRDCQ
DIANKGGKES GLYFIKPLTT QQQFLVYCEM ERNGNGWTVL QKRLDGSEDF KKNWIQYKQG
FGHLSPTGTT EFWLGNEKMH LITTQSTIPY VLRVELEDWT GRIATADYAM FSVGNEADKY
RLKYAYFMSG DAGDAFDGFD FGDDPSDKFF TSHNGMQFST WDNDNDKFDG NCAAQDGSGW
WMNKCHAGHL NGVYYQGGTY SKTSTPNGYD NGIIWATWKS RWYSMKKTTM KIIPFNRINI
EEGQQHNIGG SKQAGDV
//
