CTNA2_MOUSE
ID CTNA2_MOUSE Reviewed; 953 AA.
AC Q61301; Q3TY37; Q61300; Q6AXD1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Catenin alpha-2;
DE AltName: Full=Alpha N-catenin;
GN Name=Ctnna2; Synonyms=Catna2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8174789; DOI=10.1006/dbio.1994.1124;
RA Uchida N., Shimamura K., Miyatani S., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Takeichi M.;
RT "Mouse alpha N-catenin: two isoforms, specific expression in the nervous
RT system, and chromosomal localization of the gene.";
RL Dev. Biol. 163:75-85(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12089526; DOI=10.1038/ng908;
RA Park C., Falls W., Finger J.H., Longo-Guess C.M., Ackerman S.L.;
RT "Deletion in Catna2, encoding alpha N-catenin, causes cerebellar and
RT hippocampal lamination defects and impaired startle modulation.";
RL Nat. Genet. 31:279-284(2002).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12123610; DOI=10.1016/s0896-6273(02)00748-1;
RA Togashi H., Abe K., Mizoguchi A., Takaoka K., Chisaka O., Takeichi M.;
RT "Cadherin regulates dendritic spine morphogenesis.";
RL Neuron 35:77-89(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-901, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15034585; DOI=10.1038/nn1212;
RA Abe K., Chisaka O., Van Roy F., Takeichi M.;
RT "Stability of dendritic spines and synaptic contacts is controlled by alpha
RT N-catenin.";
RL Nat. Neurosci. 7:357-363(2004).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=16185771; DOI=10.1016/j.devbrainres.2005.08.004;
RA Ajioka I., Nakajima K.;
RT "Switching of alpha-catenin from alphaE-catenin in the cortical ventricular
RT zone to alphaN-catenin II in the intermediate zone.";
RL Brain Res. Dev. Brain Res. 160:106-111(2005).
RN [9]
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=16457793; DOI=10.1016/j.brainres.2005.12.057;
RA Stocker A.M., Chenn A.;
RT "Differential expression of alpha-E-catenin and alpha-N-catenin in the
RT developing cerebral cortex.";
RL Brain Res. 1073:151-158(2006).
RN [10]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=16691566; DOI=10.1002/dvdy.20841;
RA Uemura M., Takeichi M.;
RT "Alpha N-catenin deficiency causes defects in axon migration and nuclear
RT organization in restricted regions of the mouse brain.";
RL Dev. Dyn. 235:2559-2566(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632; SER-640; SER-651;
RP SER-901 AND SER-939, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, 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).
CC -!- FUNCTION: May function as a linker between cadherin adhesion receptors
CC and the cytoskeleton to regulate cell-cell adhesion and differentiation
CC in the nervous system (PubMed:12123610, PubMed:15034585). Required for
CC proper regulation of cortical neuronal migration and neurite growth. It
CC acts as negative regulator of Arp2/3 complex activity and Arp2/3-
CC mediated actin polymerization. It thereby suppresses excessive actin
CC branching which would impair neurite growth and stability (By
CC similarity). Regulates morphological plasticity of synapses and
CC cerebellar and hippocampal lamination during development. Functions in
CC the control of startle modulation (PubMed:12089526).
CC {ECO:0000250|UniProtKB:P26232, ECO:0000269|PubMed:12089526,
CC ECO:0000269|PubMed:12123610, ECO:0000269|PubMed:15034585}.
CC -!- SUBUNIT: Interacts with CDH1 and CDH2 (By similarity). Interacts with
CC ZNF639; recruits CTNNA2 to the nucleus (By similarity). Interacts with
CC F-actin (By similarity). {ECO:0000250|UniProtKB:P26232,
CC ECO:0000250|UniProtKB:P30997}.
CC -!- INTERACTION:
CC Q61301; Q61301: Ctnna2; NbExp=2; IntAct=EBI-774089, EBI-774089;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16457793};
CC Peripheral membrane protein {ECO:0000305|PubMed:16457793}; Cytoplasmic
CC side {ECO:0000305|PubMed:16457793}. Cytoplasm
CC {ECO:0000269|PubMed:16457793}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:15034585}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:16457793, ECO:0000269|PubMed:16691566}. Cell
CC projection, axon {ECO:0000269|PubMed:16457793,
CC ECO:0000269|PubMed:16691566}. Nucleus {ECO:0000250|UniProtKB:P26232}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=alpha N-catenin II;
CC IsoId=Q61301-1; Sequence=Displayed;
CC Name=2; Synonyms=alpha N-catenin I;
CC IsoId=Q61301-2; Sequence=VSP_006734;
CC Name=3;
CC IsoId=Q61301-3; Sequence=VSP_038010, VSP_006734;
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in the nervous system.
CC {ECO:0000269|PubMed:8174789}.
CC -!- DEVELOPMENTAL STAGE: The ratio of the two isoforms changes during
CC development; isoform 1 is more abundant than isoform 2 in earlier
CC embryonic stages, whereas isoform 2 is predominant in the adult stage.
CC Expressed in the ventricular zone and in neurons of the developing
CC cortical plate (at protein level). Expressed in migrating neurons of
CC the external granule cell layer at 13.5 dpc while expression appears in
CC the Purkinje cell layer at 17.5 dpc (at protein level). Expressed
CC postnatally in Purkinje cells and hippocampus (at protein level).
CC {ECO:0000269|PubMed:12089526, ECO:0000269|PubMed:16185771,
CC ECO:0000269|PubMed:16457793, ECO:0000269|PubMed:8174789}.
CC -!- DISRUPTION PHENOTYPE: Mice generally die within 24 hours after birth.
CC They display altered Purkinje cells migration, unstable synaptic
CC junctions, defective ventricular architecture, impaired axon migration,
CC reduced number of neurons in specific nuclei, and disordered laminar
CC formation. {ECO:0000269|PubMed:12089526, ECO:0000269|PubMed:12123610,
CC ECO:0000269|PubMed:15034585, ECO:0000269|PubMed:16691566}.
CC -!- MISCELLANEOUS: The cdf (cerebellar deficient folia) mice are viable but
CC are ataxic and have cerebellar hypoplasia associated with abnormal
CC lobulation of the cerebellum. They also display defects in Purkinje
CC cells positioning and in packing density and lamination. Fear
CC conditioning and prepulse inhibition of the startle response are
CC altered in cdf mice. Those phenotypes are associated with alteration of
CC the Ctnna2 gene which results in the C-terminal truncation of the
CC protein and are rescued by expression of a Ctnna2 transgene (isoform
CC 2).
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; D25282; BAA04970.1; -; mRNA.
DR EMBL; D25281; BAA04969.1; -; mRNA.
DR EMBL; AK158916; BAE34726.1; -; mRNA.
DR EMBL; BC079648; AAH79648.1; -; mRNA.
DR CCDS; CCDS20250.1; -. [Q61301-1]
DR CCDS; CCDS39521.1; -. [Q61301-2]
DR PIR; I49499; I49499.
DR PIR; I49500; I49500.
DR RefSeq; NP_001103234.1; NM_001109764.1. [Q61301-1]
DR RefSeq; NP_033949.2; NM_009819.2. [Q61301-1]
DR RefSeq; NP_663785.2; NM_145732.2. [Q61301-2]
DR RefSeq; XP_011239496.1; XM_011241194.2.
DR RefSeq; XP_017176861.1; XM_017321372.1.
DR PDB; 4K1O; X-ray; 2.60 A; A=651-953.
DR PDB; 4ONS; X-ray; 2.80 A; A/C=18-264.
DR PDB; 4P9T; X-ray; 2.50 A; A/B/C/D=13-261.
DR PDB; 5XFL; X-ray; 2.45 A; A/B/C/D=260-632.
DR PDB; 6DUY; X-ray; 2.81 A; A/B=651-953.
DR PDBsum; 4K1O; -.
DR PDBsum; 4ONS; -.
DR PDBsum; 4P9T; -.
DR PDBsum; 5XFL; -.
DR PDBsum; 6DUY; -.
DR AlphaFoldDB; Q61301; -.
DR SMR; Q61301; -.
DR BioGRID; 198511; 11.
DR DIP; DIP-31971N; -.
DR IntAct; Q61301; 6.
DR MINT; Q61301; -.
DR STRING; 10090.ENSMUSP00000124376; -.
DR iPTMnet; Q61301; -.
DR PhosphoSitePlus; Q61301; -.
DR SwissPalm; Q61301; -.
DR EPD; Q61301; -.
DR jPOST; Q61301; -.
DR MaxQB; Q61301; -.
DR PaxDb; Q61301; -.
DR PeptideAtlas; Q61301; -.
DR PRIDE; Q61301; -.
DR ProteomicsDB; 277922; -. [Q61301-1]
DR ProteomicsDB; 277923; -. [Q61301-2]
DR ProteomicsDB; 277924; -. [Q61301-3]
DR Antibodypedia; 8335; 143 antibodies from 28 providers.
DR DNASU; 12386; -.
DR Ensembl; ENSMUST00000075340; ENSMUSP00000074809; ENSMUSG00000063063. [Q61301-2]
DR Ensembl; ENSMUST00000159626; ENSMUSP00000124376; ENSMUSG00000063063. [Q61301-1]
DR Ensembl; ENSMUST00000161846; ENSMUSP00000123714; ENSMUSG00000063063. [Q61301-3]
DR GeneID; 12386; -.
DR KEGG; mmu:12386; -.
DR UCSC; uc009cjq.2; mouse. [Q61301-1]
DR UCSC; uc012enl.1; mouse. [Q61301-2]
DR CTD; 1496; -.
DR MGI; MGI:88275; Ctnna2.
DR VEuPathDB; HostDB:ENSMUSG00000063063; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; Q61301; -.
DR PhylomeDB; Q61301; -.
DR TreeFam; TF313686; -.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 12386; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ctnna2; mouse.
DR PRO; PR:Q61301; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q61301; protein.
DR Bgee; ENSMUSG00000063063; Expressed in cortical plate and 119 other tissues.
DR ExpressionAtlas; Q61301; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; IMP:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0098888; C:extrinsic component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007409; P:axonogenesis; IMP:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0060134; P:prepulse inhibition; IMP:UniProtKB.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:UniProtKB.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR030046; CTNNA2.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR18914:SF23; PTHR18914:SF23; 1.
DR Pfam; PF01044; Vinculin; 2.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; SSF47220; 4.
DR PROSITE; PS00663; VINCULIN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..953
FT /note="Catenin alpha-2"
FT /id="PRO_0000064264"
FT REGION 912..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 632
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1
FT /note="M -> MTDIHSSYTYTGSM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038010"
FT VAR_SEQ 811..858
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8174789"
FT /id="VSP_006734"
FT CONFLICT 103
FT /note="M -> K (in Ref. 1; BAA04970/BAA04969)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="I -> M (in Ref. 1; BAA04970/BAA04969)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="Y -> D (in Ref. 1; BAA04970/BAA04969)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="M -> I (in Ref. 3; AAH79648)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="D -> Y (in Ref. 1; BAA04970/BAA04969)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="Missing (in Ref. 3; AAH79648)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="D -> R (in Ref. 1; BAA04970/BAA04969)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="F -> S (in Ref. 1; BAA04970)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="A -> S (in Ref. 1; BAA04970/BAA04969)"
FT /evidence="ECO:0000305"
FT CONFLICT 911
FT /note="P -> S (in Ref. 2; BAE34726)"
FT /evidence="ECO:0000305"
FT HELIX 22..39
FT /evidence="ECO:0007829|PDB:4P9T"
FT HELIX 55..81
FT /evidence="ECO:0007829|PDB:4P9T"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4P9T"
FT HELIX 86..112
FT /evidence="ECO:0007829|PDB:4P9T"
FT HELIX 117..165
FT /evidence="ECO:0007829|PDB:4P9T"
FT HELIX 169..196
FT /evidence="ECO:0007829|PDB:4P9T"
FT HELIX 200..229
FT /evidence="ECO:0007829|PDB:4P9T"
FT HELIX 234..258
FT /evidence="ECO:0007829|PDB:4P9T"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:5XFL"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 296..319
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 325..350
FT /evidence="ECO:0007829|PDB:5XFL"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 360..391
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 397..406
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 411..437
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 442..471
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 476..502
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 506..529
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 533..558
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 565..579
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 581..597
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 607..627
FT /evidence="ECO:0007829|PDB:5XFL"
FT HELIX 668..673
FT /evidence="ECO:0007829|PDB:4K1O"
FT HELIX 677..702
FT /evidence="ECO:0007829|PDB:4K1O"
FT HELIX 710..729
FT /evidence="ECO:0007829|PDB:4K1O"
FT HELIX 738..763
FT /evidence="ECO:0007829|PDB:4K1O"
FT HELIX 769..791
FT /evidence="ECO:0007829|PDB:4K1O"
FT STRAND 798..802
FT /evidence="ECO:0007829|PDB:4K1O"
FT STRAND 805..809
FT /evidence="ECO:0007829|PDB:4K1O"
FT HELIX 859..894
FT /evidence="ECO:0007829|PDB:4K1O"
SQ SEQUENCE 953 AA; 105286 MW; 52DC5230A4A4A159 CRC64;
MTSATSPIIL KWDPKSLEIR TLTVERLLEP LVTQVTTLVN TSNKGPSGKK KGRSKKAHVL
AASVEQATQN FLEKGEQIAK ESQDLKEELV AAVEDVRKQG ETMRIASSEF ADDPCSSVKR
GTMVRAARAL LSAVTRLLIL ADMADVMRLL SHLKIVEEAL EAVKNATNEQ DLANRFKEFG
KEMVKLNYVA ARRQQELKDP HCRDEMAAAR GALKKNATML YTASQAFLRH PDVAATRANR
DYVFKQVQEA IAGISSAAQA TSPTDEAKGH TGIGELAAAL NEFDNKIILD PMTFSEARFR
PSLEERLESI ISGAALMADS SCTRDDRRER IVAECNAVRQ ALQDLLSEYM NNTGRKEKGD
PLNIAIDKMT KKTRDLRRQL RKAVMDHISD SFLETNVPLL VLIEAAKSGN EKEVKEYAQV
FREHANKLVE VANLACSISN NEEGVKLVRM AATQIDSLCP QVINAALTLA ARPQSKVAQD
NMDVFKDQWE KQVRVLTEAV DDITSVDDFL SVSENHILED VNKCVIALQE GDVDTLDRTA
GAIRGRAARV IHIINAEMEN YEAGVYTEKV LEATKLLSET VMPRFAEQVE VAIEALSANV
PQPFEENEFI DASRLVYDGV RDIRKAVLMI RTPEELEDDS DFEQEDYDVR SRTSVQTEDD
QLIAGQSARA IMAQLPQEEK AKIAEQVEIF HQEKSKLDAE VAKWDDSGND IIVLAKQMCM
IMMEMTDFTR GKGPLKNTSD VINAAKKIAE AGSRMDKLAR AVADQCPDSA CKQDLLAYLQ
RIALYCHQLN ICSKVKAEVQ NLGGELIVSG TGVQSTFTTF YEVDCDVIDG GRASQLSTHL
PTCAEGAPIG SGSSDSSMLD SATSLIQAAK NLMNAVVLTV KASYVASTKY QKVYGTAAVN
SPVVSWKMKA PEKKPLVKRE KPEEFQTRVR RGSQKKHISP VQALSEFKAM DSF
