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   24-JAN-2024, entry version 214.
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   INTERACTION WITH TJP1 AND TJP2.
RX   PubMed=10026224; DOI=10.1074/jbc.274.9.5981;
RA   Itoh M., Morita K., Tsukita S.;
RT   "Characterization of ZO-2 as a MAGUK family member associated with tight as
RT   well as adherens junctions with a binding affinity to occludin and alpha
RT   catenin.";
RL   J. Biol. Chem. 274:5981-5986(1999).
RN   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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,
RC   Pancreas, 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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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). Interacts with TJP2/ZO2 (via N-terminus)
CC       (PubMed:10026224). Interacts with TJP1/ZO1 (via N-terminus)
CC       (PubMed:10026224). {ECO:0000250|UniProtKB:P35221,
CC       ECO:0000269|PubMed:10026224, ECO:0000269|PubMed:10882138,
CC       ECO:0000269|PubMed:11907041, ECO:0000269|PubMed:16325582,
CC       ECO:0000269|PubMed:16325583, ECO:0000269|PubMed:18093941,
CC       ECO:0000269|PubMed:25653389, 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   EMDB; EMD-21925; -.
DR   SMR; P26231; -.
DR   BioGRID; 198510; 31.
DR   DIP; DIP-35299N; -.
DR   IntAct; P26231; 19.
DR   MINT; P26231; -.
DR   STRING; 10090.ENSMUSP00000049007; -.
DR   ChEMBL; CHEMBL4879433; -.
DR   GlyGen; P26231; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P26231; -.
DR   PhosphoSitePlus; P26231; -.
DR   SwissPalm; P26231; -.
DR   EPD; P26231; -.
DR   jPOST; P26231; -.
DR   PaxDb; 10090-ENSMUSP00000049007; -.
DR   PeptideAtlas; P26231; -.
DR   ProteomicsDB; 277921; -.
DR   Pumba; P26231; -.
DR   Antibodypedia; 3431; 872 antibodies from 44 providers.
DR   DNASU; 12385; -.
DR   Ensembl; ENSMUST00000042345.8; ENSMUSP00000049007.7; ENSMUSG00000037815.8.
DR   GeneID; 12385; -.
DR   KEGG; mmu:12385; -.
DR   UCSC; uc008ely.1; mouse.
DR   AGR; MGI:88274; -.
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; VHMSASQ; -.
DR   OrthoDB; 2875365at2759; -.
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 79 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 285 other cell types or tissues.
DR   ExpressionAtlas; P26231; baseline and differential.
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: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: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   Gene3D; 6.10.250.2510; -; 1.
DR   Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 5.
DR   IDEAL; IID50072; -.
DR   InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR   InterPro; IPR001033; Alpha_catenin.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   InterPro; IPR000633; Vinculin_CS.
DR   PANTHER; PTHR18914; ALPHA CATENIN; 1.
DR   PANTHER; PTHR18914:SF24; CATENIN ALPHA-1; 1.
DR   Pfam; PF01044; Vinculin; 1.
DR   PRINTS; PR00805; ALPHACATENIN.
DR   SUPFAM; SSF47220; alpha-catenin/vinculin-like; 4.
DR   PROSITE; PS00663; VINCULIN_1; 1.
DR   Genevisible; P26231; MM.
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
FT                   E-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
FT                   E-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
//