VINC_CHICK
ID VINC_CHICK Reviewed; 1135 AA.
AC P12003; Q91024;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Vinculin;
DE AltName: Full=Metavinculin;
GN Name=VCL; Synonyms=VINC1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=3141928; DOI=10.1073/pnas.85.22.8535;
RA Coutu M.D., Craig S.W.;
RT "cDNA-derived sequence of chicken embryo vinculin.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:8535-8539(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=2497736; DOI=10.1042/bj2590453;
RA Price G.J., Jones P., Davison M.D., Patel B., Bendori R., Geiger B.,
RA Critchley D.R.;
RT "Primary sequence and domain structure of chicken vinculin.";
RL Biochem. J. 259:453-461(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=1618784; DOI=10.1016/s0021-9258(18)42353-8;
RA Byrne B.J., Kaczorowski Y.J., Coutu M.D., Craig S.W.;
RT "Chicken vinculin and meta-vinculin are derived from a single gene by
RT alternative splicing of a 207-base pair exon unique to meta-vinculin.";
RL J. Biol. Chem. 267:12845-12850(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-881.
RC TISSUE=Embryo;
RX PubMed=3117046; DOI=10.1042/bj2450595;
RA Price G.J., Jones P., Davison M.D., Patel B., Eperon I.C., Critchley D.R.;
RT "Isolation and characterization of a vinculin cDNA from chick-embryo
RT fibroblasts.";
RL Biochem. J. 245:595-603(1987).
RN [5]
RP ACETYLATION.
RX PubMed=3030822; DOI=10.1016/0014-5793(87)81536-3;
RA Kellie S., Wigglesworth N.M.;
RT "The cytoskeletal protein vinculin is acylated by myristic acid.";
RL FEBS Lett. 213:428-432(1987).
RN [6]
RP TALIN INTERACTION DOMAIN.
RX PubMed=2512301; DOI=10.1083/jcb.109.6.2917;
RA Jones P., Jackson P., Price G.J., Patel B., Ohanion V., Lear A.L.,
RA Critchley D.R.;
RT "Identification of a talin binding site in the cytoskeletal protein
RT vinculin.";
RL J. Cell Biol. 109:2917-2927(1989).
RN [7]
RP INTERACTION WITH NRAP.
RX PubMed=10320340; DOI=10.1021/bi982395t;
RA Luo G., Herrera A.H., Horowits R.;
RT "Molecular interactions of N-RAP, a nebulin-related protein of striated
RT muscle myotendon junctions and intercalated disks.";
RL Biochemistry 38:6135-6143(1999).
RN [8]
RP PHOSPHORYLATION AT TYR-100 AND TYR-1134, FUNCTION, AND MUTAGENESIS OF
RP TYR-100; TYR-160; TYR-537; TYR-692; TYR-822 AND TYR-1134.
RX PubMed=15229287; DOI=10.1091/mbc.e04-03-0264;
RA Zhang Z., Izaguirre G., Lin S.-Y., Lee H.Y., Schaefer E., Haimovich B.;
RT "The phosphorylation of vinculin on tyrosine residues 100 and 1065,
RT mediated by SRC kinases, affects cell spreading.";
RL Mol. Biol. Cell 15:4234-4247(2004).
RN [9]
RP INTERACTION WITH TLN1.
RX PubMed=20610383; DOI=10.1074/jbc.m109.095455;
RA Gingras A.R., Bate N., Goult B.T., Patel B., Kopp P.M., Emsley J.,
RA Barsukov I.L., Roberts G.C., Critchley D.R.;
RT "Central region of talin has a unique fold that binds vinculin and actin.";
RL J. Biol. Chem. 285:29577-29587(2010).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20584916; DOI=10.1083/jcb.201001149;
RA le Duc Q., Shi Q., Blonk I., Sonnenberg A., Wang N., Leckband D.,
RA de Rooij J.;
RT "Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-
RT anchored sites within adherens junctions in a myosin II-dependent manner.";
RL J. Cell Biol. 189:1107-1115(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNB1.
RX PubMed=20086044; DOI=10.1242/jcs.056432;
RA Peng X., Cuff L.E., Lawton C.D., DeMali K.A.;
RT "Vinculin regulates cell-surface E-cadherin expression by binding to beta-
RT catenin.";
RL J. Cell Sci. 123:567-577(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 881-1135 OF ISOFORM 1.
RX PubMed=10612396; DOI=10.1016/s0092-8674(00)81549-4;
RA Bakolitsa C., de Pereda J.M., Bagshaw C.R., Critchley D.R.,
RA Liddington R.C.;
RT "Crystal structure of the vinculin tail suggests a pathway for
RT activation.";
RL Cell 99:603-613(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-259 IN COMPLEX WITH APBB1IP, AND
RP INTERACTION WITH TLN1 AND APBB1IP.
RX PubMed=23389036; DOI=10.1074/jbc.m112.438119;
RA Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R.,
RA Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R., Barsukov I.L.;
RT "RIAM and vinculin binding to talin are mutually exclusive and regulate
RT adhesion assembly and turnover.";
RL J. Biol. Chem. 288:8238-8249(2013).
CC -!- FUNCTION: Actin filament (F-actin)-binding protein involved in cell-
CC matrix adhesion and cell-cell adhesion. Regulates cell-surface E-
CC cadherin expression and potentiates mechanosensing by the E-cadherin
CC complex. May also play important roles in cell morphology and
CC locomotion. {ECO:0000269|PubMed:15229287, ECO:0000269|PubMed:20086044,
CC ECO:0000269|PubMed:20584916}.
CC -!- SUBUNIT: Exhibits self-association properties. Interacts with APBB1IP,
CC NRAP and TLN1. Interacts with CTNNB1 and this interaction is necessary
CC for its localization to the cell-cell junctions and for its function in
CC regulating cell surface expression of E-cadherin.
CC {ECO:0000269|PubMed:10320340, ECO:0000269|PubMed:20086044,
CC ECO:0000269|PubMed:20610383, ECO:0000269|PubMed:23389036}.
CC -!- INTERACTION:
CC P12003; P05094-2: ACTN1; NbExp=5; IntAct=EBI-1039563, EBI-6049246;
CC P12003; P49024: PXN; NbExp=5; IntAct=EBI-1039563, EBI-2896280;
CC P12003; P26039: Tln1; Xeno; NbExp=5; IntAct=EBI-1039563, EBI-1039593;
CC P12003; P50552: VASP; Xeno; NbExp=2; IntAct=EBI-1039563, EBI-748201;
CC P12003-1; P49024: PXN; NbExp=2; IntAct=EBI-6138078, EBI-2896280;
CC P12003-1; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-6138078, EBI-367540;
CC P12003-2; P49024: PXN; NbExp=2; IntAct=EBI-6138096, EBI-2896280;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20584916};
CC Peripheral membrane protein {ECO:0000305|PubMed:20584916}; Cytoplasmic
CC side {ECO:0000305|PubMed:20584916}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20584916}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:20086044}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:P85972}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q64727}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q64727}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q64727}. Note=Recruitment to cell-cell junctions
CC occurs in a myosin II-dependent manner (PubMed:20584916). Interaction
CC with CTNNB1 is necessary for its localization to the cell-cell
CC junctions (PubMed:20086044). {ECO:0000269|PubMed:20086044,
CC ECO:0000269|PubMed:20584916}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Metavinculin;
CC IsoId=P12003-2; Sequence=Displayed;
CC Name=1; Synonyms=Vinculin;
CC IsoId=P12003-1; Sequence=VSP_010772;
CC -!- TISSUE SPECIFICITY: Isoform Metavinculin is muscle-specific.
CC -!- DOMAIN: Exists in at least two conformations. When in the closed,
CC 'inactive' conformation, extensive interactions between the head and
CC tail domains prevent detectable binding to most of its ligands. It
CC takes on an 'active' conformation after cooperative and simultaneous
CC binding of two different ligands. This activation involves displacement
CC of the head-tail interactions and leads to a significant accumulation
CC of ternary complexes. The active form then binds a number of proteins
CC that have both signaling and structural roles that are essential for
CC cell adhesion. {ECO:0000250|UniProtKB:P18206}.
CC -!- DOMAIN: The N-terminal globular head (Vh) comprises of subdomains D1-
CC D4. The C-terminal tail (Vt) binds F-actin and cross-links actin
CC filaments into bundles. An intramolecular interaction between Vh and Vt
CC masks the F-actin-binding domain located in Vt. The binding of talin
CC and alpha-actinin to the D1 subdomain of vinculin induces a helical
CC bundle conversion of this subdomain, leading to the disruption of the
CC intramolecular interaction and the exposure of the cryptic F-actin-
CC binding domain of Vt. Vt inhibits actin filament barbed end elongation
CC without affecting the critical concentration of actin assembly.
CC {ECO:0000250|UniProtKB:P18206}.
CC -!- PTM: Phosphorylated; on serines, threonines and tyrosines.
CC Phosphorylation on Tyr-1134 in activated platelets affects head-tail
CC interactions and cell spreading but has no effect on actin binding nor
CC on localization to focal adhesion plaques.
CC {ECO:0000269|PubMed:15229287}.
CC -!- PTM: Acetylated; mainly by myristic acid but also by a small amount of
CC palmitic acid. {ECO:0000269|PubMed:3030822}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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; J04126; AAA49136.1; -; mRNA.
DR EMBL; M87837; AAA49135.1; -; Genomic_DNA.
DR EMBL; Y00312; CAA68412.1; -; mRNA.
DR PIR; A31346; A29997.
DR RefSeq; NP_990772.1; NM_205441.1. [P12003-1]
DR RefSeq; XP_015143689.1; XM_015288203.1. [P12003-2]
DR PDB; 1QKR; X-ray; 1.80 A; A/B=879-1135.
DR PDB; 1ST6; X-ray; 3.10 A; A=1-1135.
DR PDB; 1T01; X-ray; 2.06 A; A=1-254.
DR PDB; 1U6H; X-ray; 2.38 A; A=1-259.
DR PDB; 1XWJ; X-ray; 2.60 A; A=2-259.
DR PDB; 1ZVZ; X-ray; 1.80 A; A=2-259.
DR PDB; 1ZW2; X-ray; 2.10 A; A=2-259.
DR PDB; 1ZW3; X-ray; 3.30 A; A=2-259.
DR PDB; 2GDC; X-ray; 2.74 A; A=1-266.
DR PDB; 3JBI; EM; 8.50 A; V=879-1130.
DR PDB; 3ZDL; X-ray; 2.30 A; A=1-259.
DR PDB; 4E17; X-ray; 2.30 A; A=1-259.
DR PDB; 4E18; X-ray; 2.40 A; A=1-259.
DR PDB; 6FQ4; X-ray; 2.89 A; A=1-259.
DR PDB; 6NR7; X-ray; 3.00 A; A=1-1135.
DR PDBsum; 1QKR; -.
DR PDBsum; 1ST6; -.
DR PDBsum; 1T01; -.
DR PDBsum; 1U6H; -.
DR PDBsum; 1XWJ; -.
DR PDBsum; 1ZVZ; -.
DR PDBsum; 1ZW2; -.
DR PDBsum; 1ZW3; -.
DR PDBsum; 2GDC; -.
DR PDBsum; 3JBI; -.
DR PDBsum; 3ZDL; -.
DR PDBsum; 4E17; -.
DR PDBsum; 4E18; -.
DR PDBsum; 6FQ4; -.
DR PDBsum; 6NR7; -.
DR AlphaFoldDB; P12003; -.
DR SMR; P12003; -.
DR BioGRID; 676671; 2.
DR DIP; DIP-35191N; -.
DR ELM; P12003; -.
DR IntAct; P12003; 16.
DR MINT; P12003; -.
DR STRING; 9031.ENSGALP00000008131; -.
DR iPTMnet; P12003; -.
DR PaxDb; P12003; -.
DR PRIDE; P12003; -.
DR DNASU; 396422; -.
DR Ensembl; ENSGALT00000008145; ENSGALP00000008131; ENSGALG00000005079. [P12003-2]
DR Ensembl; ENSGALT00000061988; ENSGALP00000048583; ENSGALG00000005079. [P12003-1]
DR GeneID; 396422; -.
DR KEGG; gga:396422; -.
DR CTD; 7414; -.
DR VEuPathDB; HostDB:geneid_396422; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_012338_0_0_1; -.
DR InParanoid; P12003; -.
DR OMA; ANNLCEL; -.
DR PhylomeDB; P12003; -.
DR Reactome; R-GGA-114608; Platelet degranulation.
DR Reactome; R-GGA-445355; Smooth Muscle Contraction.
DR Reactome; R-GGA-5674135; MAP2K and MAPK activation.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR SABIO-RK; P12003; -.
DR EvolutionaryTrace; P12003; -.
DR PRO; PR:P12003; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000005079; Expressed in colon and 14 other tissues.
DR ExpressionAtlas; P12003; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:AgBase.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:AgBase.
DR GO; GO:0044291; C:cell-cell contact zone; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0043034; C:costamere; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IDA:AgBase.
DR GO; GO:0090637; C:inner dense plaque of desmosome; IDA:AgBase.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005927; C:muscle tendon junction; IDA:AgBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:AgBase.
DR GO; GO:0090636; C:outer dense plaque of desmosome; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0002102; C:podosome; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; IDA:AgBase.
DR GO; GO:0098723; C:skeletal muscle myofibril; IDA:AgBase.
DR GO; GO:0001725; C:stress fiber; IDA:AgBase.
DR GO; GO:1990357; C:terminal web; IDA:AgBase.
DR GO; GO:0030018; C:Z disc; IDA:AgBase.
DR GO; GO:0005915; C:zonula adherens; IDA:AgBase.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0051393; F:alpha-actinin binding; IDA:AgBase.
DR GO; GO:0045294; F:alpha-catenin binding; IDA:BHF-UCL.
DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL.
DR GO; GO:0002162; F:dystroglycan binding; IEA:Ensembl.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IMP:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:0097110; F:scaffold protein binding; IPI:AgBase.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0017166; F:vinculin binding; IDA:AgBase.
DR GO; GO:0034333; P:adherens junction assembly; IDA:BHF-UCL.
DR GO; GO:0043297; P:apical junction assembly; IEA:Ensembl.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IDA:BHF-UCL.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:1904702; P:regulation of protein localization to adherens junction; IEA:Ensembl.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR46180; PTHR46180; 2.
DR Pfam; PF01044; Vinculin; 2.
DR SUPFAM; SSF47220; SSF47220; 8.
DR PROSITE; PS00663; VINCULIN_1; 1.
DR PROSITE; PS00664; VINCULIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell adhesion;
KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Lipoprotein;
KW Membrane; Myristate; Palmitate; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P26234"
FT CHAIN 2..1135
FT /note="Vinculin"
FT /id="PRO_0000064255"
FT REPEAT 259..369
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 370..479
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 480..589
FT /note="3"
FT /evidence="ECO:0000255"
FT REGION 2..835
FT /note="N-terminal globular head"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 168..208
FT /note="Talin-interaction"
FT /evidence="ECO:0000269|PubMed:2512301"
FT REGION 259..589
FT /note="3 X 112 AA tandem repeats"
FT /evidence="ECO:0000255"
FT REGION 836..878
FT /note="Linker (Pro-rich)"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 837..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..1135
FT /note="C-terminal tail"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 1004..1047
FT /note="Facilitates phospholipid membrane insertion"
FT /evidence="ECO:0000250|UniProtKB:Q64727"
FT REGION 1121..1135
FT /note="Facilitates phospholipid membrane insertion"
FT /evidence="ECO:0000250|UniProtKB:Q64727"
FT COMPBIAS 859..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:15229287"
FT MOD_RES 537
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305"
FT MOD_RES 822
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 1134
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000269|PubMed:15229287"
FT VAR_SEQ 916..984
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:2497736,
FT ECO:0000303|PubMed:3141928"
FT /id="VSP_010772"
FT MUTAGEN 100
FT /note="Y->F: Some reduction of phosphorylation levels in
FT platelets. Little change in cell spreading. Complete loss
FT of phosphorylation. No change in subcellular location nor
FT on in vitro actin binding. 40% decrease in cell spreading;
FT when associated with F-1134."
FT /evidence="ECO:0000269|PubMed:15229287"
FT MUTAGEN 160
FT /note="Y->F: No change of phosphorylation levels in
FT platelets."
FT /evidence="ECO:0000269|PubMed:15229287"
FT MUTAGEN 537
FT /note="Y->F: No change of phosphorylation levels in
FT platelets."
FT /evidence="ECO:0000269|PubMed:15229287"
FT MUTAGEN 692
FT /note="Y->F: No change of phosphorylation levels in
FT platelets."
FT /evidence="ECO:0000269|PubMed:15229287"
FT MUTAGEN 822
FT /note="Y->F: No change of phosphorylation levels in
FT platelets."
FT /evidence="ECO:0000269|PubMed:15229287"
FT MUTAGEN 1134
FT /note="Y->F: Greatly reduced phosphorylation levels in
FT platelets. Little change in cell spreading. Complete loss
FT of phosphorylation. No change in subcellular location nor
FT on in vitro actin binding. 40% decrease in cell spreading;
FT when associated with F-100."
FT /evidence="ECO:0000269|PubMed:15229287"
FT CONFLICT 442..447
FT /note="TAKLSD -> QLSCQI (in Ref. 2 and 4; CAA68412)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="Q -> H (in Ref. 2 and 4; CAA68412)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="E -> K (in Ref. 4; CAA68412)"
FT /evidence="ECO:0000305"
FT HELIX 7..28
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT HELIX 41..63
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT HELIX 75..97
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT HELIX 102..146
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3ZDL"
FT HELIX 154..181
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT HELIX 185..215
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1T01"
FT HELIX 222..249
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:3ZDL"
FT HELIX 258..276
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:6NR7"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 297..311
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 316..340
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 347..396
FT /evidence="ECO:0007829|PDB:6NR7"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 406..420
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 425..450
FT /evidence="ECO:0007829|PDB:6NR7"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:6NR7"
FT TURN 457..460
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 461..482
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 493..501
FT /evidence="ECO:0007829|PDB:6NR7"
FT TURN 509..513
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 514..530
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 535..560
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 566..569
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 572..598
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 604..614
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 622..650
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 655..684
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 690..714
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 719..741
FT /evidence="ECO:0007829|PDB:6NR7"
FT TURN 742..744
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 747..751
FT /evidence="ECO:0007829|PDB:6NR7"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 755..773
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 777..791
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 795..797
FT /evidence="ECO:0007829|PDB:6NR7"
FT TURN 799..804
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 811..814
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 817..835
FT /evidence="ECO:0007829|PDB:6NR7"
FT STRAND 864..866
FT /evidence="ECO:0007829|PDB:6NR7"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:1ST6"
FT STRAND 892..894
FT /evidence="ECO:0007829|PDB:1ST6"
FT HELIX 896..910
FT /evidence="ECO:0007829|PDB:6NR7"
FT HELIX 961..964
FT /evidence="ECO:0007829|PDB:1QKR"
FT HELIX 966..978
FT /evidence="ECO:0007829|PDB:1QKR"
FT HELIX 987..1005
FT /evidence="ECO:0007829|PDB:1QKR"
FT HELIX 1010..1012
FT /evidence="ECO:0007829|PDB:1QKR"
FT HELIX 1013..1040
FT /evidence="ECO:0007829|PDB:1QKR"
FT HELIX 1044..1054
FT /evidence="ECO:0007829|PDB:1QKR"
FT HELIX 1057..1074
FT /evidence="ECO:0007829|PDB:1QKR"
FT STRAND 1075..1077
FT /evidence="ECO:0007829|PDB:1ST6"
FT HELIX 1082..1113
FT /evidence="ECO:0007829|PDB:1QKR"
FT HELIX 1121..1123
FT /evidence="ECO:0007829|PDB:1QKR"
SQ SEQUENCE 1135 AA; 124560 MW; 28CC2699C9511058 CRC64;
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA VSNLVRVGKE
TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR
QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM QKAQQVSQGL
DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG GSEGEEHIRG IMSEARKVAE
LCEEPKERDD ILRSLGEISA LTAKLSDLRR HGKGDSPEAR ALAKQIATSL QNLQSKTNRA
VANTRPVKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD
LLAKCDRVDQ LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS
DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV GTANKTTVEG
IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK
SLLDASEEAI KKDLDKCKVA MANMQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP
DFPPPPPDLE HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM
AARQLHDEAR KWSSKPVTVI NEAAEAGVDI DEEDDADVEF SLPSDIEDDY EPELLLMPTN
QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA EMSRLVRGGS GNKRALIQCA
KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL LQVCERIPTI STQLKILSTV KATMLGRTNI
SDEESEQATE MLVHNAQNLM QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ
