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AJAP1_MOUSE
ID   AJAP1_MOUSE             Reviewed;         412 AA.
AC   A2ALI5; B2RVK0;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Adherens junction-associated protein 1;
DE   Flags: Precursor;
GN   Name=Ajap1; Synonyms=Gm573;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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).
CC   -!- FUNCTION: Plays a role in cell adhesion and cell migration.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with CDH1 and CTNNB1; interacts directly with
CC       CTNNB1 (By similarity). Interacts with AP1M2 and isoform 2 of BSG/CD147
CC       (By similarity). {ECO:0000250|UniProtKB:Q9UKB5}.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q9UKB5}; Single-pass type I membrane protein
CC       {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9UKB5};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell junction,
CC       adherens junction {ECO:0000250|UniProtKB:Q9UKB5}. Note=Mainly
CC       basolateral. Localization is mediated by AP1M2.
CC       {ECO:0000250|UniProtKB:Q9UKB5}.
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DR   EMBL; AL805910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL954390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC147229; AAI47230.1; -; mRNA.
DR   EMBL; BC147230; AAI47231.1; -; mRNA.
DR   EMBL; BC147654; AAI47655.1; -; mRNA.
DR   EMBL; BC147658; AAI47659.1; -; mRNA.
DR   CCDS; CCDS38987.1; -.
DR   RefSeq; NP_001092769.1; NM_001099299.1.
DR   AlphaFoldDB; A2ALI5; -.
DR   STRING; 10090.ENSMUSP00000101271; -.
DR   iPTMnet; A2ALI5; -.
DR   PhosphoSitePlus; A2ALI5; -.
DR   MaxQB; A2ALI5; -.
DR   PaxDb; A2ALI5; -.
DR   PeptideAtlas; A2ALI5; -.
DR   PRIDE; A2ALI5; -.
DR   ProteomicsDB; 296145; -.
DR   Antibodypedia; 2726; 55 antibodies from 17 providers.
DR   Ensembl; ENSMUST00000105646; ENSMUSP00000101271; ENSMUSG00000039546.
DR   GeneID; 230959; -.
DR   KEGG; mmu:230959; -.
DR   UCSC; uc008was.1; mouse.
DR   CTD; 55966; -.
DR   MGI; MGI:2685419; Ajap1.
DR   VEuPathDB; HostDB:ENSMUSG00000039546; -.
DR   eggNOG; ENOG502QVMU; Eukaryota.
DR   GeneTree; ENSGT00510000048586; -.
DR   HOGENOM; CLU_055642_1_0_1; -.
DR   InParanoid; A2ALI5; -.
DR   OMA; HWRTVSP; -.
DR   OrthoDB; 770398at2759; -.
DR   TreeFam; TF336539; -.
DR   BioGRID-ORCS; 230959; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Ajap1; mouse.
DR   PRO; PR:A2ALI5; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; A2ALI5; protein.
DR   Bgee; ENSMUSG00000039546; Expressed in lumbar subsegment of spinal cord and 84 other tissues.
DR   ExpressionAtlas; A2ALI5; baseline and differential.
DR   Genevisible; A2ALI5; MM.
DR   GO; GO:0005912; C:adherens junction; ISO:MGI.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR   GO; GO:0044214; C:spanning component of plasma membrane; ISO:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0061045; P:negative regulation of wound healing; ISO:MGI.
DR   GO; GO:0030860; P:regulation of polarized epithelial cell differentiation; ISO:MGI.
DR   InterPro; IPR039239; AJAP1.
DR   InterPro; IPR029198; AJAP1_PANP_C.
DR   PANTHER; PTHR32422; PTHR32422; 1.
DR   Pfam; PF15298; AJAP1_PANP_C; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Cell membrane; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..412
FT                   /note="Adherens junction-associated protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000284802"
FT   TOPO_DOM        44..284
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..412
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          62..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..412
FT                   /note="Targeting signals"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        123..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  44772 MW;  FA54456D22247447 CRC64;
     MWIQQLLGLS SMSIRWPGRS LGSHAWILIA MLQLAVDFPS CDSLGPGPEF RLLSRPQRPQ
     RLWSLRSGPP TRLPTPAWSP RAARAERAHG PIQMQTPRAR RAHRPRDQVA TLGPKGGLTK
     PPAATRSSPS LASATASSSI VTAGAAEHQG LLRRGRRHTH DTEFNDFDFR GGRPTTETEF
     IAWGPTGDED ALESNTFPGG FGPTTVSILQ TRKTTVATTT TTTAASTATA MTLQTKGVTE
     SLDPWKRTPV GVSTTEPSTS PSSNGKDIQP PRILGETSGL AVHQIITITV SLIMVIAALI
     TTLVLKNCCA PSGHTRRNSH QRKMNQQEES CQNLTDFTPA RVPSSVDIFT AYNETLQCSH
     ECVRASVPVY ADETLHSTGE YKSTFNGNRT SSADRHLIPV AFVSEKWFEI SC
 
 
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