CTNA1_MOUSE
ID CTNA1_MOUSE Reviewed; 906 AA.
AC P26231;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Catenin alpha-1;
DE AltName: Full=102 kDa cadherin-associated protein;
DE AltName: Full=Alpha E-catenin;
DE AltName: Full=CAP102;
GN Name=Ctnna1; Synonyms=Catna1;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=129/Sv;
RX PubMed=1924379; DOI=10.1073/pnas.88.20.9156;
RA Herrenknecht K., Ozawa M., Eckerskorn C., Lottspeich F., Lenter M.,
RA Kemler R.;
RT "The uvomorulin-anchorage protein alpha catenin is a vinculin homologue.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9156-9160(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1904011; DOI=10.1016/0092-8674(91)90392-c;
RA Nagafuchi A., Takeichi M., Tsukita S.;
RT "The 102 kd cadherin-associated protein: similarity to vinculin and
RT posttranscriptional regulation of expression.";
RL Cell 65:849-857(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA Butz S., Kemler R.;
RT "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT adhesion.";
RL FEBS Lett. 355:195-200(1994).
RN [5]
RP RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
RP ACTIN BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
RA Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
RT "Deconstructing the cadherin-catenin-actin complex.";
RL Cell 123:889-901(2005).
RN [6]
RP SUBUNIT, AND FUNCTION.
RX PubMed=16325583; DOI=10.1016/j.cell.2005.09.021;
RA Drees F., Pokutta S., Yamada S., Nelson W.J., Weis W.I.;
RT "Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and
RT regulates actin-filament assembly.";
RL Cell 123:903-915(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP INTERACTION WITH LIMA1, AND LACK OF ACTIN BINDING BY THE E-CADHERIN/CATENIN
RP ADHESION COMPLEX.
RX PubMed=18093941; DOI=10.1073/pnas.0710504105;
RA Abe K., Takeichi M.;
RT "EPLIN mediates linkage of the cadherin catenin complex to F-actin and
RT stabilizes the circumferential actin belt.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-634; SER-641; THR-645;
RP SER-652; SER-655 AND THR-658, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP FUNCTION.
RX PubMed=21145499; DOI=10.1016/j.devcel.2010.11.012;
RA Varelas X., Samavarchi-Tehrani P., Narimatsu M., Weiss A., Cockburn K.,
RA Larsen B.G., Rossant J., Wrana J.L.;
RT "The Crumbs complex couples cell density sensing to Hippo-dependent control
RT of the TGF-beta-SMAD pathway.";
RL Dev. Cell 19:831-844(2010).
RN [12]
RP IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX, PHOSPHORYLATION,
RP AND MUTAGENESIS OF 641-SER--THR-658 AND SER-641.
RX PubMed=25653389; DOI=10.1242/jcs.163824;
RA Escobar D.J., Desai R., Ishiyama N., Folmsbee S.S., Novak M.N.,
RA Flozak A.S., Daugherty R.L., Mo R., Nanavati D., Sarpal R., Leckband D.,
RA Ikura M., Tepass U., Gottardi C.J.;
RT "alpha-Catenin phosphorylation promotes intercellular adhesion through a
RT dual-kinase mechanism.";
RL J. Cell Sci. 128:1150-1165(2015).
RN [13]
RP MUTAGENESIS OF LEU-436.
RX PubMed=26691986; DOI=10.1038/ng.3474;
RA Saksens N.T., Krebs M.P., Schoenmaker-Koller F.E., Hicks W., Yu M., Shi L.,
RA Rowe L., Collin G.B., Charette J.R., Letteboer S.J., Neveling K.,
RA van Moorsel T.W., Abu-Ltaif S., De Baere E., Walraedt S., Banfi S.,
RA Simonelli F., Cremers F.P., Boon C.J., Roepman R., Leroy B.P.,
RA Peachey N.S., Hoyng C.B., Nishina P.M., den Hollander A.I.;
RT "Mutations in CTNNA1 cause butterfly-shaped pigment dystrophy and perturbed
RT retinal pigment epithelium integrity.";
RL Nat. Genet. 48:144-151(2016).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 57-261 IN COMPLEX WITH CTNNB1.
RX PubMed=10882138; DOI=10.1016/s1097-2765(00)80447-5;
RA Pokutta S., Weis W.I.;
RT "Structure of the dimerization and beta-catenin-binding region of alpha-
RT catenin.";
RL Mol. Cell 5:533-543(2000).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 385-651, AND INTERACTION WITH AFDN
RP AND F-ACTIN.
RX PubMed=11907041; DOI=10.1074/jbc.m201463200;
RA Pokutta S., Drees F., Takai Y., Nelson W.J., Weis W.I.;
RT "Biochemical and structural definition of the l-afadin- and actin-binding
RT sites of alpha-catenin.";
RL J. Biol. Chem. 277:18868-18874(2002).
CC -!- FUNCTION: Associates with the cytoplasmic domain of a variety of
CC cadherins. The association of catenins to cadherins produces a complex
CC which is linked to the actin filament network, and which seems to be of
CC primary importance for cadherins cell-adhesion properties. Can
CC associate with both E- and N-cadherins. Originally believed to be a
CC stable component of E-cadherin/catenin adhesion complexes and to
CC mediate the linkage of cadherins to the actin cytoskeleton at adherens
CC junctions. In contrast, cortical actin was found to be much more
CC dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to
CC bind to F-actin when assembled in the complex suggesting a different
CC linkage between actin and adherens junctions components. The
CC homodimeric form may regulate actin filament assembly and inhibit actin
CC branching by competing with the Arp2/3 complex for binding to actin
CC filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1-
CC dependent SMAD2 and SMAD3 nuclear accumulation (PubMed:21145499). May
CC play a crucial role in cell differentiation.
CC {ECO:0000269|PubMed:16325583, ECO:0000269|PubMed:21145499}.
CC -!- SUBUNIT: Monomer and homodimer; the monomer preferentially binds to
CC CTNNB1 and the homodimer to actin (PubMed:16325583). Component of an
CC cadherin:catenin adhesion complex composed of at least of CDH26, beta-
CC catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (By
CC similarity). Possible component of an E-cadherin/ catenin adhesion
CC complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-
CC catenin/JUP; the complex is located to adherens junctions
CC (PubMed:7982500, PubMed:16325582, PubMed:16325583, PubMed:18093941,
CC PubMed:25653389, PubMed:10882138). The stable association of CTNNA1 is
CC controversial as CTNNA1 was shown not to bind to F-actin when assembled
CC in the complex (PubMed:16325582, PubMed:18093941). Alternatively, the
CC CTNNA1-containing complex may be linked to F-actin by other proteins
CC such as LIMA1 (PubMed:18093941). Binds AFDN and F-actin
CC (PubMed:11907041). Interacts with LIMA1 (By similarity)
CC (PubMed:18093941). Interacts with ARHGAP21 (By similarity). Interacts
CC with AJUBA (By similarity). Interacts with vinculin/VCL (By
CC similarity). {ECO:0000250|UniProtKB:P35221,
CC ECO:0000269|PubMed:10882138, ECO:0000269|PubMed:11907041,
CC ECO:0000269|PubMed:16325582, ECO:0000269|PubMed:16325583,
CC ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:25653389,
CC ECO:0000269|PubMed:7982500}.
CC -!- INTERACTION:
CC P26231; P26231: Ctnna1; NbExp=2; IntAct=EBI-647895, EBI-647895;
CC P26231; Q02248: Ctnnb1; NbExp=2; IntAct=EBI-647895, EBI-397872;
CC P26231; O35889: Afdn; Xeno; NbExp=2; IntAct=EBI-647895, EBI-6654073;
CC P26231; P35222: CTNNB1; Xeno; NbExp=2; IntAct=EBI-647895, EBI-491549;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, adherens
CC junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
CC Cell junction. Note=Found at cell-cell boundaries and probably at cell-
CC matrix boundaries.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in normal tissues.
CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P35221}.
CC -!- PTM: Phosphorylation seems to contribute to the strength of cell-cell
CC adhesion rather than to the basic capacity for cell-cell adhesion.
CC {ECO:0000305|PubMed:25653389}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; X59990; CAA42607.1; -; mRNA.
DR EMBL; D90362; BAA14376.1; -; mRNA.
DR EMBL; BC048163; AAH48163.1; -; mRNA.
DR CCDS; CCDS29139.1; -.
DR PIR; A39529; A39529.
DR RefSeq; NP_033948.1; NM_009818.1.
DR RefSeq; XP_011245120.1; XM_011246818.2.
DR PDB; 1DOV; X-ray; 3.00 A; A=82-262.
DR PDB; 1DOW; X-ray; 1.80 A; A=57-261.
DR PDB; 1L7C; X-ray; 2.50 A; A/B/C=385-651.
DR PDB; 4E17; X-ray; 2.30 A; B=321-356.
DR PDB; 4E18; X-ray; 2.40 A; B=302-356.
DR PDB; 4K1N; X-ray; 6.50 A; A/B=1-906.
DR PDB; 5Y04; X-ray; 2.85 A; B=276-375.
DR PDB; 6DV1; X-ray; 2.20 A; A/B=652-906.
DR PDB; 6O3E; X-ray; 4.00 A; A/B=82-883.
DR PDB; 6WVT; EM; 3.56 A; K/L/N/O/Q/X=671-906.
DR PDBsum; 1DOV; -.
DR PDBsum; 1DOW; -.
DR PDBsum; 1L7C; -.
DR PDBsum; 4E17; -.
DR PDBsum; 4E18; -.
DR PDBsum; 4K1N; -.
DR PDBsum; 5Y04; -.
DR PDBsum; 6DV1; -.
DR PDBsum; 6O3E; -.
DR PDBsum; 6WVT; -.
DR AlphaFoldDB; P26231; -.
DR SMR; P26231; -.
DR BioGRID; 198510; 30.
DR DIP; DIP-35299N; -.
DR IntAct; P26231; 19.
DR MINT; P26231; -.
DR STRING; 10090.ENSMUSP00000049007; -.
DR iPTMnet; P26231; -.
DR PhosphoSitePlus; P26231; -.
DR SwissPalm; P26231; -.
DR EPD; P26231; -.
DR jPOST; P26231; -.
DR PaxDb; P26231; -.
DR PeptideAtlas; P26231; -.
DR PRIDE; P26231; -.
DR ProteomicsDB; 277921; -.
DR Antibodypedia; 3431; 788 antibodies from 44 providers.
DR DNASU; 12385; -.
DR Ensembl; ENSMUST00000042345; ENSMUSP00000049007; ENSMUSG00000037815.
DR GeneID; 12385; -.
DR KEGG; mmu:12385; -.
DR UCSC; uc008ely.1; mouse.
DR CTD; 1495; -.
DR MGI; MGI:88274; Ctnna1.
DR VEuPathDB; HostDB:ENSMUSG00000037815; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_2_0_1; -.
DR InParanoid; P26231; -.
DR OMA; DIGHRDQ; -.
DR OrthoDB; 953344at2759; -.
DR PhylomeDB; P26231; -.
DR TreeFam; TF313686; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-525793; Myogenesis.
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR BioGRID-ORCS; 12385; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Ctnna1; mouse.
DR EvolutionaryTrace; P26231; -.
DR PRO; PR:P26231; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P26231; protein.
DR Bgee; ENSMUSG00000037815; Expressed in renal medulla collecting duct and 281 other tissues.
DR ExpressionAtlas; P26231; baseline and differential.
DR Genevisible; P26231; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0016342; C:catenin complex; ISO:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016600; C:flotillin complex; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005915; C:zonula adherens; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0017166; F:vinculin binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0043297; P:apical junction assembly; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISO:MGI.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:MGI.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0016264; P:gap junction assembly; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:2000146; P:negative regulation of cell motility; IMP:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:2001045; P:negative regulation of integrin-mediated signaling pathway; IMP:MGI.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:MGI.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IGI:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
DR IDEAL; IID50072; -.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR030047; CTNNA1/CTNNA3.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR18914:SF24; PTHR18914:SF24; 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; Acetylation; Cell adhesion; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Isopeptide bond;
KW Membrane; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT CHAIN 2..906
FT /note="Catenin alpha-1"
FT /id="PRO_0000064262"
FT REGION 2..228
FT /note="Involved in homodimerization"
FT /evidence="ECO:0000250"
FT REGION 97..148
FT /note="Interaction with JUP and CTNNB1"
FT /evidence="ECO:0000250"
FT REGION 325..394
FT /note="Interaction with alpha-actinin"
FT /evidence="ECO:0000250"
FT REGION 864..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MOD_RES 634
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 645
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 658
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT CROSSLNK 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35221"
FT MUTAGEN 436
FT /note="L->P: Mice bearing this mutation exhibit several
FT retinal pigment epithelium (RPE) anomalies, including
FT pigmentary abnormalities, focal thickening, elevated
FT lesions, and decreased light-activated responses. Mutant
FT animals show dysmorphology in the form of RPE cell shedding
FT and accumulation of large multinucleated RPE cells."
FT /evidence="ECO:0000269|PubMed:26691986"
FT MUTAGEN 641..658
FT /note="SDFETEDFDVRSRTSVQT->ADFETEDFDVRARAAVQA: No effect on
FT cell aggregation or E-cadherin/catenin complex assembly.
FT Decreases strength of cell-cell adhesion."
FT /evidence="ECO:0000269|PubMed:25653389"
FT MUTAGEN 641..658
FT /note="SDFETEDFDVRSRTSVQT->EDFETEDFDVREREEVQE: No effect on
FT cell aggregation or E-cadherin/catenin complex assembly.
FT Increases strength of cell-cell adhesion."
FT /evidence="ECO:0000269|PubMed:25653389"
FT MUTAGEN 641
FT /note="S->A: No effect on cell aggregation or E-
FT cadherin/catenin complex assembly. Decreases strength of
FT cell-cell adhesion."
FT /evidence="ECO:0000269|PubMed:25653389"
FT MUTAGEN 641
FT /note="S->E: No effect on cell aggregation or E-
FT cadherin/catenin complex assembly. Increases strength of
FT cell-cell adhesion."
FT /evidence="ECO:0000269|PubMed:25653389"
FT HELIX 59..82
FT /evidence="ECO:0007829|PDB:1DOW"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1DOW"
FT HELIX 87..113
FT /evidence="ECO:0007829|PDB:1DOW"
FT HELIX 118..165
FT /evidence="ECO:0007829|PDB:1DOW"
FT HELIX 170..195
FT /evidence="ECO:0007829|PDB:1DOW"
FT HELIX 201..230
FT /evidence="ECO:0007829|PDB:1DOW"
FT HELIX 235..259
FT /evidence="ECO:0007829|PDB:1DOW"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:4E18"
FT HELIX 328..352
FT /evidence="ECO:0007829|PDB:4E17"
FT HELIX 360..368
FT /evidence="ECO:0007829|PDB:5Y04"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:5Y04"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:1L7C"
FT HELIX 399..409
FT /evidence="ECO:0007829|PDB:1L7C"
FT HELIX 413..440
FT /evidence="ECO:0007829|PDB:1L7C"
FT HELIX 444..473
FT /evidence="ECO:0007829|PDB:1L7C"
FT HELIX 478..506
FT /evidence="ECO:0007829|PDB:1L7C"
FT HELIX 508..531
FT /evidence="ECO:0007829|PDB:1L7C"
FT HELIX 535..560
FT /evidence="ECO:0007829|PDB:1L7C"
FT HELIX 567..581
FT /evidence="ECO:0007829|PDB:1L7C"
FT HELIX 583..598
FT /evidence="ECO:0007829|PDB:1L7C"
FT HELIX 608..629
FT /evidence="ECO:0007829|PDB:1L7C"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:6DV1"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:6DV1"
FT HELIX 669..675
FT /evidence="ECO:0007829|PDB:6DV1"
FT HELIX 678..702
FT /evidence="ECO:0007829|PDB:6DV1"
FT HELIX 711..730
FT /evidence="ECO:0007829|PDB:6DV1"
FT HELIX 739..765
FT /evidence="ECO:0007829|PDB:6DV1"
FT HELIX 770..793
FT /evidence="ECO:0007829|PDB:6DV1"
FT STRAND 799..803
FT /evidence="ECO:0007829|PDB:6DV1"
FT STRAND 806..810
FT /evidence="ECO:0007829|PDB:6DV1"
FT HELIX 812..840
FT /evidence="ECO:0007829|PDB:6DV1"
SQ SEQUENCE 906 AA; 100106 MW; 3ED1EC50925DBBB5 CRC64;
MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV
LAASVEQATE NFLEKGDKIA KESQFLKEEL VVAVEDVRKQ GDLMKSAAGE FADDPCSSVK
RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL
KPEVDKLNIM AAKRQQELKD VGNRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN
RDLIYKQLQQ AVTGISNAAQ ATASDDAAQH QGGSGGELAY ALNNFDKQII VDPLSFSEER
FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER
SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA
QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA
QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR
TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS
DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED
DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC
MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL
QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS
TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF
KAMDSI
