ID A0A3Q2Z9M1_KRYMA Unreviewed; 905 AA.
AC A0A3Q2Z9M1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Catenin alpha-2 {ECO:0000256|ARBA:ARBA00023806};
DE AltName: Full=Alpha N-catenin {ECO:0000256|ARBA:ARBA00029822};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000000123.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000000123.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004413}. Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000256|ARBA:ARBA00008376}.
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DR RefSeq; XP_017260975.1; XM_017405486.1.
DR AlphaFoldDB; A0A3Q2Z9M1; -.
DR STRING; 37003.ENSKMAP00000000123; -.
DR Ensembl; ENSKMAT00000000147.1; ENSKMAP00000000123.1; ENSKMAG00000000106.1.
DR GeneID; 108229805; -.
DR CTD; 1496; -.
DR GeneTree; ENSGT01030000234543; -.
DR OMA; QDELMNN; -.
DR OrthoDB; 2875365at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR Gene3D; 6.10.250.2510; -; 1.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 5.
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:SF23; CATENIN ALPHA-2; 1.
DR Pfam; PF01044; Vinculin; 1.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; alpha-catenin/vinculin-like; 4.
DR PROSITE; PS00663; VINCULIN_1; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT REGION 867..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 100610 MW; BEC677A462B71824 CRC64;
MTTATSPILL KWDPKNLEIR TLTVERLLEP LVTQVTTLVN TSNKGPSSKK KGRSKKAHVL
AVSVEQATQN FLEKGEQIAK DSQDLKEELI AAVEDVRKQG ETMRIASSEF ADDPCSSVKR
GTMVRAARAL LSAVTRLLIL ADMADVMRLL AHLKVVEEAL EGVKNATNEQ DLANRFKEFG
KEMVKLNYVA ARRQQELKDP QCRDEMAAAR GALKKNATML YTASQAFLRH PDVAATRANR
DYVFKQVQEA MGGISIAAQA TSPTEEKHGH AGIGELAAAL NEFDNKIILD PLTFSEARFR
PSLEERLESI ISGAALMADS SCTRDDRRER IVAECNAVRQ ALQDLLSEYM NNTGRKEKGD
PLNSAIDKMT KKTRDLRRQL RKAVMDHISD SFLETNVPLL VLIEAAKSGN EKEVKEYAQV
FREHANKLVE VANLACSISN NEEGVKLVRM AATQIDSLCP QVINAALTLA ARPQSKVAQD
NMDVFKDQWE KQVRILTEAV DDITSVDDFL SVSENHILED VNKCVIALQE GDVDTLDRTA
GAIRGRAARV VHIINAEMEN YEPGVYTERV LESIKLLSET VMPRFAEQVE VAIEALSTNP
PQAFEENEFI DASRLVYDGV RDIRKAVLMI RTPEELEDDS DFEQEDYDTR SRTSVQTEDD
QLIAGQSARA IMAQLPQEEK AKIAEQVESF RQEKCKLDAE VAKWDDNGND IIVLAKQMCM
IMMEMTDFTR GKGPLKNSSD VINAAKKIAE AGSRMDKLSR AVADQCPDSA CKQDLLAYLQ
RIALYCHQLN ICSKVKAEVQ NLGGELIVSG LDSATSLIQA AKNLMNAVVL TVKASYVAST
KYQKVYGTAA VNSPVVSWRM KAPEKKPLVK REKPEECQTR VRRGSQKKHI SPVQALSEFK
AMDSF
//
