FIBA_MOUSE
ID FIBA_MOUSE Reviewed; 789 AA.
AC E9PV24; Q99K47;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Fibrinogen alpha chain;
DE Contains:
DE RecName: Full=Fibrinopeptide A {ECO:0000250|UniProtKB:P06399};
DE Contains:
DE RecName: Full=Fibrinogen alpha chain;
DE Flags: Precursor;
GN Name=Fga {ECO:0000312|MGI:MGI:1316726};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Ensembl:ENSMUSP00000133117};
RN [1] {ECO:0000312|Ensembl:ENSMUSP00000133117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000133117};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000312|EMBL:AAH05467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=7649481; DOI=10.1101/gad.9.16.2020;
RA Suh T.T., Holmback K., Jensen N.J., Daugherty C.C., Small K., Simon D.I.,
RA Potter S., Degen J.L.;
RT "Resolution of spontaneous bleeding events but failure of pregnancy in
RT fibrinogen-deficient mice.";
RL Genes Dev. 9:2020-2033(1995).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10930441; DOI=10.1172/jci9896;
RA Ni H., Denis C.V., Subbarao S., Degen J.L., Sato T.N., Hynes R.O.,
RA Wagner D.D.;
RT "Persistence of platelet thrombus formation in arterioles of mice lacking
RT both von Willebrand factor and fibrinogen.";
RL J. Clin. Invest. 106:385-392(2000).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=11389004; DOI=10.1182/blood.v97.12.3691;
RA Drew A.F., Liu H., Davidson J.M., Daugherty C.C., Degen J.L.;
RT "Wound-healing defects in mice lacking fibrinogen.";
RL Blood 97:3691-3698(2001).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12629066; DOI=10.1084/jem.20021493;
RA Johnson L.L., Berggren K.N., Szaba F.M., Chen W., Smiley S.T.;
RT "Fibrin-mediated protection against infection-stimulated immunopathology.";
RL J. Exp. Med. 197:801-806(2003).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15972474; DOI=10.1128/iai.73.7.3888-3895.2005;
RA Mullarky I.K., Szaba F.M., Berggren K.N., Parent M.A., Kummer L.W.,
RA Chen W., Johnson L.L., Smiley S.T.;
RT "Infection-stimulated fibrin deposition controls hemorrhage and limits
RT hepatic bacterial growth during listeriosis.";
RL Infect. Immun. 73:3888-3895(2005).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=19332769; DOI=10.1182/blood-2008-03-145821;
RA Yang H., Lang S., Zhai Z., Li L., Kahr W.H., Chen P., Brkic J.,
RA Spring C.M., Flick M.J., Degen J.L., Freedman J., Ni H.;
RT "Fibrinogen is required for maintenance of platelet intracellular and cell-
RT surface P-selectin expression.";
RL Blood 114:425-436(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-447, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23487423; DOI=10.4049/jimmunol.1203253;
RA Luo D., Lin J.S., Parent M.A., Mullarky-Kanevsky I., Szaba F.M.,
RA Kummer L.W., Duso D.K., Tighe M., Hill J., Gruber A., Mackman N.,
RA Gailani D., Smiley S.T.;
RT "Fibrin facilitates both innate and T cell-mediated defense against
RT Yersinia pestis.";
RL J. Immunol. 190:4149-4161(2013).
CC -!- FUNCTION: Cleaved by the protease thrombin to yield monomers which,
CC together with fibrinogen beta (FGB) and fibrinogen gamma (FGG),
CC polymerize to form an insoluble fibrin matrix. Fibrin has a major
CC function in hemostasis as one of the primary components of blood clots
CC (PubMed:7649481). In addition, functions during the early stages of
CC wound repair to stabilize the lesion and guide cell migration during
CC re-epithelialization (PubMed:11389004). Was originally thought to be
CC essential for platelet aggregation, based on in vitro studies using
CC anticoagulated blood (PubMed:7649481). However, subsequent studies have
CC shown that it is not absolutely required for thrombus formation in vivo
CC (PubMed:10930441). Enhances expression of SELP in activated platelets
CC via an ITGB3-dependent pathway (PubMed:19332769). Maternal fibrinogen
CC is essential for successful pregnancy (PubMed:7649481). Fibrin
CC deposition is also associated with infection, where it protects against
CC IFNG-mediated hemorrhage (PubMed:12629066). May also facilitate the
CC immune response via both innate and T-cell mediated pathways
CC (PubMed:23487423). {ECO:0000250|UniProtKB:P02671,
CC ECO:0000269|PubMed:10930441, ECO:0000269|PubMed:11389004,
CC ECO:0000269|PubMed:12629066, ECO:0000269|PubMed:15972474,
CC ECO:0000269|PubMed:19332769, ECO:0000269|PubMed:23487423,
CC ECO:0000269|PubMed:7649481}.
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:0000250|UniProtKB:P02671}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7649481}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9PV24-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9PV24-2; Sequence=VSP_057097, VSP_057098;
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:7649481}.
CC -!- DOMAIN: A long coiled coil structure formed by 3 polypeptide chains
CC connects the central nodule to the C-terminal domains (distal nodules).
CC The long C-terminal ends of the alpha chains fold back, contributing a
CC fourth strand to the coiled coil structure.
CC {ECO:0000250|UniProtKB:P02671}.
CC -!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which
CC cleaves fibrinopeptides A and B from alpha and beta chains, and thus
CC exposes the N-terminal polymerization sites responsible for the
CC formation of the soft clot. The soft clot is converted into the hard
CC clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine
CC cross-linking between gamma chains (stronger) and between alpha chains
CC (weaker) of different monomers. {ECO:0000250|UniProtKB:P02671}.
CC -!- PTM: Forms F13A-mediated cross-links between a glutamine and the
CC epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen
CC heteropolymers. {ECO:0000250|UniProtKB:P02671}.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P02671}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are viable but only males are
CC fertile (PubMed:7649481). Neonates frequently develop spontaneous
CC hemorrhages, but in spite of this over 90% of mice survive the neonatal
CC period (PubMed:7649481). However only half survive beyond 70 days of
CC age; lethality is most often due to intra-abdominal hemorrhage
CC (PubMed:7649481). Pregnancy in female mice fails at around 10 days of
CC gestation, associated with severe intrauterine bleeding
CC (PubMed:7649481). Secondary loss of FGB and FGG from circulating blood
CC is observed, although FGB and FGG mRNA is normally expressed in
CC hepatocytes (thought to be the main site of fibrinogen synthesis)
CC (PubMed:7649481). In vitro, blood fails to clot and platelet
CC aggregations do not form (PubMed:7649481). In vivo, platelet
CC aggregation in injured arterioles initially occurs normally although
CC thrombi are unstable and readily embolize (PubMed:10930441). In double
CC knockouts of FGA and VWF, platelet aggregation is delayed and thrombi
CC frequently embolize (PubMed:10930441). Mice succumb more rapidly to Y.
CC pestis infection, associated with increased bacterial loads in liver
CC and lung; however induction of the inflammatory response factors TNF,
CC IFNG, CXCL1, and LCN2 is not affected (PubMed:23487423). Mice succumb
CC more rapidly to T. gondii infection, with increased hemorrhagic
CC pathology; however parasite numbers are not significantly increased and
CC induction of the inflammatory response markers IL12, IFNG, TNF, IL10,
CC and nitric oxide is not affected (PubMed:12629066). Mice succumb more
CC rapidly to L. monocytogenes infection, with increased hemorrhagic
CC pathology and increased bacterial burdens in hepatic tissue; however
CC there is little effect on peritoneal bacterial numbers or bacterial
CC dissemination to other tissues, and also no effect on induction of the
CC inflammatory markers IFNG, TNF and NOS2 (PubMed:15972474).
CC {ECO:0000269|PubMed:10930441, ECO:0000269|PubMed:12629066,
CC ECO:0000269|PubMed:15972474, ECO:0000269|PubMed:23487423,
CC ECO:0000269|PubMed:7649481}.
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DR EMBL; AC138394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005467; AAH05467.1; -; mRNA.
DR CCDS; CCDS17431.1; -. [E9PV24-2]
DR CCDS; CCDS50939.1; -. [E9PV24-1]
DR RefSeq; NP_001104518.1; NM_001111048.2. [E9PV24-1]
DR RefSeq; NP_034326.1; NM_010196.4. [E9PV24-2]
DR AlphaFoldDB; E9PV24; -.
DR SMR; E9PV24; -.
DR BioGRID; 199636; 19.
DR ComplexPortal; CPX-1916; Fibrinogen.
DR IntAct; E9PV24; 2.
DR STRING; 10090.ENSMUSP00000133117; -.
DR GlyGen; E9PV24; 1 site.
DR iPTMnet; E9PV24; -.
DR PhosphoSitePlus; E9PV24; -.
DR CPTAC; non-CPTAC-3709; -.
DR EPD; E9PV24; -.
DR jPOST; E9PV24; -.
DR MaxQB; E9PV24; -.
DR PaxDb; E9PV24; -.
DR PeptideAtlas; E9PV24; -.
DR PRIDE; E9PV24; -.
DR ProteomicsDB; 267583; -. [E9PV24-1]
DR ProteomicsDB; 267584; -. [E9PV24-2]
DR Antibodypedia; 3395; 1039 antibodies from 42 providers.
DR DNASU; 14161; -.
DR Ensembl; ENSMUST00000029630; ENSMUSP00000029630; ENSMUSG00000028001. [E9PV24-2]
DR Ensembl; ENSMUST00000166581; ENSMUSP00000133117; ENSMUSG00000028001. [E9PV24-1]
DR GeneID; 14161; -.
DR KEGG; mmu:14161; -.
DR UCSC; uc008ppf.2; mouse. [E9PV24-2]
DR UCSC; uc012cqw.1; mouse. [E9PV24-1]
DR CTD; 2243; -.
DR MGI; MGI:1316726; Fga.
DR VEuPathDB; HostDB:ENSMUSG00000028001; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157467; -.
DR HOGENOM; CLU_013807_0_0_1; -.
DR InParanoid; E9PV24; -.
DR OMA; WVSFRGA; -.
DR OrthoDB; 363208at2759; -.
DR PhylomeDB; E9PV24; -.
DR TreeFam; TF351984; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-354192; Integrin signaling.
DR Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 14161; 0 hits in 61 CRISPR screens.
DR ChiTaRS; Fga; mouse.
DR PRO; PR:E9PV24; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; E9PV24; protein.
DR Bgee; ENSMUSG00000028001; Expressed in left lobe of liver and 48 other tissues.
DR Genevisible; E9PV24; MM.
DR GO; GO:0072562; C:blood microparticle; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005577; C:fibrinogen complex; ISO:MGI.
DR GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0072377; P:blood coagulation, common pathway; ISO:MGI.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0042730; P:fibrinolysis; ISO:MGI.
DR GO; GO:0043152; P:induction of bacterial agglutination; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0031639; P:plasminogen activation; ISO:MGI.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0051258; P:protein polymerization; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
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; IPR037579; Fibrinogen_alpha.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR47221; PTHR47221; 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; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Blood coagulation; Calcium;
KW Coiled coil; Disulfide bond; Glycoprotein; Hemostasis; Hydroxylation;
KW Immunity; Innate immunity; Metal-binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:P06399, ECO:0000255"
FT PEPTIDE 20..36
FT /note="Fibrinopeptide A"
FT /evidence="ECO:0000250|UniProtKB:P06399"
FT /id="PRO_0000430789"
FT CHAIN 37..789
FT /note="Fibrinogen alpha chain"
FT /id="PRO_0000430790"
FT DOMAIN 546..787
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 263..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..554
FT /evidence="ECO:0000250|UniProtKB:P14448"
FT COMPBIAS 263..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 714
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT BINDING 716
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT BINDING 718
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT BINDING 720
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT SITE 36..37
FT /note="Cleavage; by thrombin; to release fibrinopeptide A"
FT /evidence="ECO:0000250|UniProtKB:P06399"
FT SITE 101..102
FT /note="Cleavage; by plasmin; to break down fibrin clots"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT SITE 122..123
FT /note="Cleavage; by hementin; to prevent blood coagulation"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT SITE 124..125
FT /note="Cleavage; by plasmin; to break down fibrin clots"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 504
FT /note="4-hydroxyproline; by P4HA1"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT DISULFID 56
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT DISULFID 65
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT DISULFID 69
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT DISULFID 181
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT DISULFID 185
FT /note="Interchain (with C-213 in beta chain)"
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT DISULFID 408..438
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT DISULFID 722..735
FT /evidence="ECO:0000250|UniProtKB:P02671"
FT VAR_SEQ 554..557
FT /note="DCDD -> GIDT (in isoform 2)"
FT /evidence="ECO:0000305|PubMed:15489334"
FT /id="VSP_057097"
FT VAR_SEQ 558..789
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305|PubMed:15489334"
FT /id="VSP_057098"
SQ SEQUENCE 789 AA; 87429 MW; 16B968D6E4952CF7 CRC64;
MLSLRVTCLI LSVASTVWTT DTEDKGEFLS EGGGVRGPRV VERHQSQCKD SDWPFCSDDD
WNHKCPSGCR MKGLIDEANQ DFTNRINKLK NSLFDFQRNN KDSNSLTRNI MEYLRGDFAN
ANNFDNTYGQ VSEDLRRRIE ILRRKVIEKA QQIQALQSNV RAQLIDMKRL EVDIDIKIRS
CKGSCSRAVN REINLQDYEG HQKQLQQVIA KELLPTKDRQ YLPALKMSPV PDLVPGSFKS
QLQEAPPEWK ALTEMRQMRM ELERPGKDGG SRGDSPGDSR GDSRGDFATR GPGSKAENPT
NPGPGGSGYW RPGNSGSGSD GNRNPGTTGS DGTGDWGTGS PRPGSDSGNF RPANPNWGVF
SEFGDSSSPA TRKEYHTGKA VTSKGDKELL IGKEKVTSSG TSTTHRSCSK TITKTVTGPD
GRREVVKEVI TSDDGSDCGD ATELDISHSF SGSLDELSER HPDLSGFFDN HFGLISPNFK
EFGSKTHSDS DILTNIEDPS SHVPEFSSSS KTSTVKKQVT KTYKMADEAG SEAHREGETR
NTKRGRARAR PTRDCDDVLQ TQTSGAQNGI FSIKPPGSSK VFSVYCDQET SLGGWLLIQQ
RMDGSLNFNR TWQDYKRGFG SLNDKGEGEF WLGNDYLHLL TLRGSVLRVE LEDWAGKEAY
AEYHFRVGSE AEGYALQVSS YRGTAGDALV QGSVEEGTEY TSHSNMQFST FDRDADQWEE
NCAEVYGGGW WYNSCQAANL NGIYYPGGTY DPRNNSPYEI ENGVVWVPFR GADYSLRAVR
MKIRPLVGQ
