CO3_RAT
ID CO3_RAT Reviewed; 1663 AA.
AC P01026; Q9ET19; Q9QV57; Q9QV58;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Complement C3;
DE Contains:
DE RecName: Full=Complement C3 beta chain;
DE Contains:
DE RecName: Full=C3-beta-c;
DE Short=C3bc;
DE AltName: Full=Neutrophil chemotactic factor-2;
DE Short=ENCF-2;
DE Contains:
DE RecName: Full=Complement C3 alpha chain;
DE Contains:
DE RecName: Full=C3a anaphylatoxin;
DE AltName: Full=Neutrophil chemotactic factor-1;
DE Short=ENCF-1;
DE Contains:
DE RecName: Full=Acylation stimulating protein;
DE Short=ASP;
DE AltName: Full=C3adesArg;
DE Contains:
DE RecName: Full=Complement C3b alpha' chain;
DE Contains:
DE RecName: Full=Complement C3c alpha' chain fragment 1;
DE Contains:
DE RecName: Full=Complement C3dg fragment;
DE Contains:
DE RecName: Full=Complement C3g fragment;
DE Contains:
DE RecName: Full=Complement C3d fragment;
DE Contains:
DE RecName: Full=Complement C3f fragment;
DE Contains:
DE RecName: Full=Complement C3c alpha' chain fragment 2;
DE Flags: Precursor;
GN Name=C3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=2336397; DOI=10.1093/nar/18.8.2178;
RA Misumi Y., Sohda M., Ikehara Y.;
RT "Nucleotide and deduced amino acid sequence of rat complement C3.";
RL Nucleic Acids Res. 18:2178-2178(1990).
RN [2]
RP PROTEIN SEQUENCE OF 568-592 AND 671-687, IDENTIFICATION OF C3A
RP ANAPHYLATOXIN AND C3-BETA-C, AND FUNCTION.
RC TISSUE=Neutrophil;
RX PubMed=8352775; DOI=10.1006/bbrc.1993.1947;
RA Nakagawa H., Komorita N.;
RT "Complement component C3-derived neutrophil chemotactic factors purified
RT from exudate of rat carrageenin-induced inflammation.";
RL Biochem. Biophys. Res. Commun. 194:1181-1187(1993).
RN [3]
RP PROTEIN SEQUENCE OF 671-748.
RX PubMed=309768; DOI=10.1021/bi00616a027;
RA Jacobs J.W., Rubin J.S., Hugli T.E., Bogardt R.A. Jr., Mariz I.K.,
RA Daniels J.S., Daughaday W.H., Bradshaw R.A.;
RT "Purification, characterization, and amino acid sequence of rat
RT anaphylatoxin (C3a).";
RL Biochemistry 17:5031-5038(1978).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 671-748.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Wahrmann M., Krieger S., Liewehr A.;
RT "Nucleotide and deduced amino acid sequence of rat complement component C3a
RT derived from Sprague-Dawley strain.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 960-969, AND X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF
RP 1010-1286.
RX PubMed=10825534; DOI=10.1016/s0167-4838(00)00040-6;
RA Zanotti G., Bassetto A., Battistutta R., Folli C., Arcidiaco P.,
RA Stoppini M., Berni R.;
RT "Structure at 1.44 A resolution of an N-terminally truncated form of the
RT rat serum complement C3d fragment.";
RL Biochim. Biophys. Acta 1478:232-238(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1316-1595.
RX PubMed=2674144; DOI=10.1016/s0021-9258(19)84798-1;
RA Sundstrom S.A., Komm B.S., Ponce-De-Leon H., Yi Z., Teuscher C.,
RA Lyttle C.R.;
RT "Estrogen regulation of tissue-specific expression of complement C3.";
RL J. Biol. Chem. 264:16941-16947(1989).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: C3 plays a central role in the activation of the complement
CC system. Its processing by C3 convertase is the central reaction in both
CC classical and alternative complement pathways. After activation C3b can
CC bind covalently, via its reactive thioester, to cell surface
CC carbohydrates or immune aggregates. {ECO:0000269|PubMed:8352775}.
CC -!- FUNCTION: Derived from proteolytic degradation of complement C3, C3a
CC anaphylatoxin is a mediator of local inflammatory process. It induces
CC the contraction of smooth muscle, increases vascular permeability and
CC causes histamine release from mast cells and basophilic leukocytes. In
CC chronic inflammation, acts as a chemoattractant for neutrophils
CC (PubMed:8352775). {ECO:0000269|PubMed:8352775}.
CC -!- FUNCTION: [C3-beta-c]: Acts as a chemoattractant for neutrophils in
CC chronic inflammation. {ECO:0000269|PubMed:8352775}.
CC -!- FUNCTION: [Acylation stimulating protein]: Adipogenic hormone that
CC stimulates triglyceride (TG) synthesis and glucose transport in
CC adipocytes, regulating fat storage and playing a role in postprandial
CC TG clearance. Appears to stimulate TG synthesis via activation of the
CC PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the
CC phosphorylation, ARRB2-mediated internalization and recycling of C5AR2
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: C3 precursor is first processed by the removal of 4 Arg
CC residues, forming two chains, beta and alpha, linked by a disulfide
CC bond. C3 convertase activates C3 by cleaving the alpha chain, releasing
CC C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). Forms
CC the pro-C3-convertase enzyme complex by binding to Complement factor B
CC Bb fragment (Bb), which is then stabilized by binding CFP, allowing the
CC complex to become active (By similarity). The interaction with Bb is
CC dependent on Mg2+ (By similarity). C3b interacts with CR1 (via Sushi 8
CC and Sushi 9 domains). C3b interacts with CFH. C3d interacts with CFH.
CC C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2).
CC During pregnancy, C3dg exists as a complex (probably a 2:2:2
CC heterohexamer) with AGT and the proform of PRG2. Interacts with VSIG4.
CC Interacts with S.aureus immunoglobulin-binding protein sbi, this
CC prevents interaction between C3dg and CR2. Interacts with S.aureus fib.
CC Interacts (both C3a and ASP) with C5AR2; the interaction occurs with
CC higher affinity for ASP, enhancing the phosphorylation and activation
CC of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of
CC GRP77. {ECO:0000250|UniProtKB:P01024}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: C3b is rapidly split in two positions by factor I and a cofactor
CC to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is
CC slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha'
CC chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other
CC proteases produce other fragments such as C3d or C3g. C3a is further
CC processed by carboxypeptidases to release the C-terminal arginine
CC residue generating the acylation stimulating protein (ASP). Levels of
CC ASP are increased in adipocytes in the postprandial period and by
CC dietary chylomicrons (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000250|UniProtKB:P01024}.
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DR EMBL; X52477; CAA36716.1; -; mRNA.
DR EMBL; AF286158; AAG00532.1; -; mRNA.
DR EMBL; M29866; AAA40837.1; -; mRNA.
DR PIR; S15764; C3RT.
DR RefSeq; NP_058690.2; NM_016994.2.
DR PDB; 1QQF; X-ray; 1.45 A; A=1010-1286.
DR PDB; 1QSJ; X-ray; 1.90 A; A/B/C/D=1010-1286.
DR PDBsum; 1QQF; -.
DR PDBsum; 1QSJ; -.
DR AlphaFoldDB; P01026; -.
DR SMR; P01026; -.
DR BioGRID; 246419; 3.
DR IntAct; P01026; 1.
DR MINT; P01026; -.
DR STRING; 10116.ENSRNOP00000066885; -.
DR MEROPS; I39.950; -.
DR CarbonylDB; P01026; -.
DR GlyGen; P01026; 2 sites.
DR iPTMnet; P01026; -.
DR PhosphoSitePlus; P01026; -.
DR jPOST; P01026; -.
DR PaxDb; P01026; -.
DR PRIDE; P01026; -.
DR GeneID; 24232; -.
DR KEGG; rno:24232; -.
DR CTD; 718; -.
DR RGD; 2232; C3.
DR eggNOG; KOG1366; Eukaryota.
DR InParanoid; P01026; -.
DR OrthoDB; 23785at2759; -.
DR PhylomeDB; P01026; -.
DR Reactome; R-RNO-173736; Alternative complement activation.
DR Reactome; R-RNO-174577; Activation of C3 and C5.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR EvolutionaryTrace; P01026; -.
DR PRO; PR:P01026; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:RGD.
DR GO; GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; ISS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IDA:RGD.
DR GO; GO:0097242; P:amyloid-beta clearance; ISO:RGD.
DR GO; GO:0007596; P:blood coagulation; IMP:RGD.
DR GO; GO:1905114; P:cell surface receptor signaling pathway involved in cell-cell signaling; ISO:RGD.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0006956; P:complement activation; IDA:RGD.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; TAS:RGD.
DR GO; GO:0097278; P:complement-dependent cytotoxicity; ISO:RGD.
DR GO; GO:0150062; P:complement-mediated synapse pruning; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0016322; P:neuron remodeling; ISO:RGD.
DR GO; GO:0008228; P:opsonization; ISO:RGD.
DR GO; GO:0035846; P:oviduct epithelium development; ISO:RGD.
DR GO; GO:0001970; P:positive regulation of activation of membrane attack complex; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:2000427; P:positive regulation of apoptotic cell clearance; ISO:RGD.
DR GO; GO:0048639; P:positive regulation of developmental growth; IDA:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; ISO:RGD.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0030449; P:regulation of complement activation; ISO:RGD.
DR GO; GO:0030451; P:regulation of complement activation, alternative pathway; ISO:RGD.
DR GO; GO:0010866; P:regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
DR GO; GO:1901555; P:response to paclitaxel; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0002507; P:tolerance induction; IEP:RGD.
DR GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0150064; P:vertebrate eye-specific patterning; ISO:RGD.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd03583; NTR_complement_C3; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
DR InterPro; IPR041425; C3/4/5_MG1.
DR InterPro; IPR035711; Complement_C3-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR035815; NTR_complement_C3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF81; PTHR11412:SF81; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF17790; MG1; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR PRINTS; PR00004; ANAPHYLATOXN.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SUPFAM; SSF47686; SSF47686; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cleavage on pair of basic residues;
KW Complement alternate pathway; Complement pathway;
KW Direct protein sequencing; Disulfide bond; Fatty acid metabolism;
KW Glycoprotein; Immunity; Inflammatory response; Innate immunity;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Secreted; Signal;
KW Thioester bond.
FT SIGNAL 1..24
FT CHAIN 25..1663
FT /note="Complement C3"
FT /id="PRO_0000005937"
FT CHAIN 25..666
FT /note="Complement C3 beta chain"
FT /id="PRO_0000005938"
FT CHAIN 568..666
FT /note="C3-beta-c"
FT /id="PRO_0000395292"
FT CHAIN 671..1663
FT /note="Complement C3 alpha chain"
FT /id="PRO_0000005939"
FT CHAIN 671..748
FT /note="C3a anaphylatoxin"
FT /id="PRO_0000005940"
FT CHAIN 671..747
FT /note="Acylation stimulating protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000419937"
FT CHAIN 749..1663
FT /note="Complement C3b alpha' chain"
FT /id="PRO_0000005941"
FT CHAIN 749..959
FT /note="Complement C3c alpha' chain fragment 1"
FT /id="PRO_0000273950"
FT CHAIN 960..1303
FT /note="Complement C3dg fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273951"
FT CHAIN 960..1001
FT /note="Complement C3g fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273952"
FT CHAIN 1002..1303
FT /note="Complement C3d fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273953"
FT PEPTIDE 1304..1320
FT /note="Complement C3f fragment"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273954"
FT CHAIN 1321..1663
FT /note="Complement C3c alpha' chain fragment 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000273955"
FT DOMAIN 693..728
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 1518..1661
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 1634..1659
FT /note="Interaction with CFP/properdin"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT SITE 747..748
FT /note="Cleavage; by carboxypeptidases"
FT /evidence="ECO:0000250"
FT SITE 748..749
FT /note="Cleavage; by C3 convertase"
FT SITE 959..960
FT /note="Cleavage; by factor I"
FT /evidence="ECO:0000255"
FT SITE 1303..1304
FT /note="Cleavage; by factor I"
FT /evidence="ECO:0000250"
FT SITE 1320..1321
FT /note="Cleavage; by factor I"
FT /evidence="ECO:0000250"
FT SITE 1663
FT /note="Coordinates Mg2+ for interaction with Complement
FT factor B Bb fragment"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01024"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 1617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 558..816
FT /note="Interchain (between beta and alpha chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022,
FT ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 626..661
FT /evidence="ECO:0000250"
FT DISULFID 693..720
FT /evidence="ECO:0000250"
FT DISULFID 694..727
FT /evidence="ECO:0000250"
FT DISULFID 707..728
FT /evidence="ECO:0000250"
FT DISULFID 873..1513
FT /evidence="ECO:0000250"
FT DISULFID 1101..1158
FT /evidence="ECO:0000250"
FT DISULFID 1358..1489
FT /evidence="ECO:0000250"
FT DISULFID 1389..1458
FT /evidence="ECO:0000250"
FT DISULFID 1506..1511
FT /evidence="ECO:0000250"
FT DISULFID 1518..1590
FT /evidence="ECO:0000250"
FT DISULFID 1537..1661
FT /evidence="ECO:0000250"
FT CROSSLNK 1010..1013
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT CONFLICT 704
FT /note="P -> K (in Ref. 4; AAG00532)"
FT /evidence="ECO:0000305"
FT CONFLICT 721..722
FT /note="LK -> KL (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 1013..1031
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1034..1037
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1039..1041
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1042..1057
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1076..1089
FT /evidence="ECO:0007829|PDB:1QQF"
FT TURN 1090..1092
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1097..1111
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1127..1134
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1139..1158
FT /evidence="ECO:0007829|PDB:1QQF"
FT TURN 1159..1161
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1165..1180
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1186..1198
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1206..1213
FT /evidence="ECO:0007829|PDB:1QQF"
FT TURN 1216..1218
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1226..1242
FT /evidence="ECO:0007829|PDB:1QQF"
FT TURN 1246..1248
FT /evidence="ECO:0007829|PDB:1QSJ"
FT HELIX 1249..1258
FT /evidence="ECO:0007829|PDB:1QQF"
FT HELIX 1269..1285
FT /evidence="ECO:0007829|PDB:1QQF"
SQ SEQUENCE 1663 AA; 186460 MW; 2F87CCB143CDD4BC CRC64;
MGPTSGSQLL VLLLLLASSL LALGSPMYSI ITPNVLRLES EETFILEAHD AQGDVPVTVT
VQDFLKKQVL TSEKTVLTGA TGHLNRVFIK IPASKEFNAD KGHKYVTVVA NFGATVVEKA
VLVSFQSGYL FIQTDKTIYT PGSTVFYRIF TVDNNLLPVG KTVVIVIETP DGVPIKRDIL
SSHNQYGILP LSWNIPELVN MGQWKIRAFY EHAPKQTFSA EFEVKEYVLP SFEVLVEPTE
KFYYIHGPKG LEVSITARFL YGKNVDGTAF VIFGVQDEDK KISLALSLTR VLIEDGSGEA
VLSRKVLMDG VRPSSPEALV GKSLYVSVTV ILHSGSDMVE AERSGIPIVT SPYQIHFTKT
PKFFKPAMPF DLMVFVTNPD GSPARRVPVV TQGSDAQALT QDDGVAKLSV NTPNNRQPLT
ITVSTKKEGI PDARQATRTM QAQPYSTMHN SNNYLHLSVS RVELKPGDNL NVNFHLRTDA
GQEAKIRYYT YLVMNKGKLL KAGRQVREPG QDLVVLSLPI TPEFIPSFRL VAYYTLIGAN
GQREVVADSV WVDVKDSCVG TLVVKGDPRD NRQPAPGHQT TLRIEGNQGA RVGLVAVDKG
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLTFKTNQG LQTDQREDPE
CAKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD IPMPYSCQRR ARLITQGESC
LKAFMDCCNY ITKLREQHRR DHVLGLARSD VDEDIIPEED IISRSHFPES WLWTIEELKE
PEKNGISTKV MNIFLKDSIT TWEILAVSLS DKKGICVADP YEITVMQDFF IDLRLPYSVV
RNEQVEIRAV LFNYREQEKL KVRVELLHNP AFCSMATAKK RYYQTIEIPP KSSVAVPYVI
VPLKIGLQEV EVKAAVFNHF ISDGVKKILK VVPEGMRVNK TVAVRTLDPE HLNQGGVQRE
DVNAADLSDQ VPDTDSETRI LLQGTPVAQM AEDAVDGERL KHLIVTPSGC GEQNMIGMTP
TVIAVHYLDQ TEQWEKFGLE KRQEALELIK KGYTQQLAFK QPISAYAAFN NRPPSTWLTA
MWSRSFSLAA NLIAIDSQVL CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNTKEAD
VSLTAFVLIA LQEARDICEG QVNSLPGSIN KAGEYLEASY LNLQRPYTVA IAGYALALMN
KLEEPYLTKF LNTAKDRNRW EEPGQQLYNV EATSYALLAL LLLKDFDSVP PVVRWLNDER
YYGGGYGSTQ ATFMVFQALA QYRADVPDHK DLNMDVSLHL PSRSSPTVFR LLWESGSLLR
SEETKQNEGF SLTAKGKGQG TLSVVTVYHA KVKGKTTCKK FDLRVTIKPA PETAKKPQDA
KSSMILDICT RYLGDVDATM SILDISMMTG FIPDTNDLEL LSSGVDRYIS KYEMDKAFSN
KNTLIIYLEK ISHSEEDCLS FKVHQFFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG
MLSKLCHNEM CRCAEENCFM HQSQDQVSLN ERLDKACEPG VDYVYKTKLT TIELSDDFDE
YIMTIEQVIK SGSDEVQAGQ ERRFISHVKC RNALKLQKGK QYLMWGLSSD LWGEKPNTSY
IIGKDTWVEH WPEAEERQDQ KNQKQCEDLG AFTETMVVFG CPN
