CTNL1_MOUSE
ID CTNL1_MOUSE Reviewed; 731 AA.
AC O88327; Q810J3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Alpha-catulin;
DE AltName: Full=Alpha-catenin-related protein;
DE Short=ACRP;
DE AltName: Full=Catenin alpha-like protein 1;
GN Name=Ctnnal1; Synonyms=Catnal1;
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].
RA Kishi M., Nagafuchi A., Tsukita S.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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 modulate the Rho pathway signaling by providing a
CC scaffold for the Lbc Rho guanine nucleotide exchange factor (ARHGEF1).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARHGEF1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; AF006071; AAC26012.1; -; mRNA.
DR EMBL; BC050070; AAH50070.1; -; mRNA.
DR CCDS; CCDS18200.1; -.
DR RefSeq; NP_061231.3; NM_018761.3.
DR AlphaFoldDB; O88327; -.
DR SMR; O88327; -.
DR IntAct; O88327; 1.
DR STRING; 10090.ENSMUSP00000036487; -.
DR iPTMnet; O88327; -.
DR PhosphoSitePlus; O88327; -.
DR MaxQB; O88327; -.
DR PaxDb; O88327; -.
DR PeptideAtlas; O88327; -.
DR PRIDE; O88327; -.
DR ProteomicsDB; 279288; -.
DR Antibodypedia; 14981; 144 antibodies from 27 providers.
DR DNASU; 54366; -.
DR Ensembl; ENSMUST00000045142; ENSMUSP00000036487; ENSMUSG00000038816.
DR GeneID; 54366; -.
DR KEGG; mmu:54366; -.
DR UCSC; uc008sxu.2; mouse.
DR CTD; 8727; -.
DR MGI; MGI:1859649; Ctnnal1.
DR VEuPathDB; HostDB:ENSMUSG00000038816; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_015314_4_0_1; -.
DR InParanoid; O88327; -.
DR OMA; DQQKMAK; -.
DR OrthoDB; 237299at2759; -.
DR PhylomeDB; O88327; -.
DR TreeFam; TF313686; -.
DR BioGRID-ORCS; 54366; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ctnnal1; mouse.
DR PRO; PR:O88327; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O88327; protein.
DR Bgee; ENSMUSG00000038816; Expressed in urinary bladder urothelium and 242 other tissues.
DR ExpressionAtlas; O88327; baseline and differential.
DR Genevisible; O88327; MM.
DR GO; GO:0005911; C:cell-cell junction; IEA:UniProt.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR001033; Alpha_catenin.
DR InterPro; IPR030045; CTNNAL1.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR46342; PTHR46342; 1.
DR Pfam; PF01044; Vinculin; 1.
DR PRINTS; PR00805; ALPHACATENIN.
DR SUPFAM; SSF47220; SSF47220; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..731
FT /note="Alpha-catulin"
FT /id="PRO_0000064269"
FT REGION 535..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBT7"
FT CONFLICT 62
FT /note="K -> R (in Ref. 2; AAH50070)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="T -> S (in Ref. 2; AAH50070)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="D -> N (in Ref. 2; AAH50070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 731 AA; 81462 MW; 36CF25115E3EF1F3 CRC64;
MAASPVPGGG GAGAVHSSNA AGFTFDSGLE IRTRSVEQTL LPLVSQITTL INHKDNTKKS
DKTLQAIQRV GQAVNLAVGR FVKVGEAIAN ENWDLKEEIN IACIEAKQAG ETIASLTDVT
KRSHLESDGQ VTILTDKTGV VQAARLLLSS VTKVLLLADR VVIKQIVTSR NKILATMERL
EKVNSFQEFV QIFSQFGNEM VEFAHLTGDR QNDLKDEKKK ARMAVARAVL EKGTMMLLTA
SKTCLRHPSC ESAHTNKEGV FDRMRVALEK VTEIVTDCRL SGETDSSSVS IFTGIKELKV
NIEALRENVC FESKENLSAA LEAVLEHVED FTDSAYTSHE HRERILELSS QARTELQQLL
SVWMQTQSRK TKSAAEELEL TVLKISHSLD ELRRELHCTA MQLAADLLKF HADHVVLKAL
KVTGVEGNLE ALAEYACKLS EQKEQLVETC RLLRHISGTE PLEITCIHAE ETFQVTGQQI
ISAAETLTLH PSSKIAKENL DVFCEAWESQ MSDMATLLRE ISDVFEGRRG ERCDHLSLPK
PTKNSANLKS LKPDKPDSEE QAKIAKLGLK LGLLSSDADC EIEKWEDEEN EIVRHGRNMS
RMAYSLYLFT RGEGPLKTSQ DLIHFLEVFA AEGLKLTSSV QSFSKQLKDD DKLMLLLEIN
KLIPLCHQLQ TITKTSLQSK VFLKVDKCIT KIRSMMTLVV QLLSLCYKLL KKMENNRWGS
ATNKDTMDGQ N
