ID   AJAP1_RAT               Reviewed;         411 AA.
AC   Q4W8E7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Adherens junction-associated protein 1;
DE   Flags: Precursor;
GN   Name=Ajap1; Synonyms=Neumo48;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Ishii S., Watanabe M., Kanbara K., Hayasaki H., Hayashi H., Kagamiyama H.;
RT   "Characterization of a novel gene from rat brain, Neumo48, that induces
RT   morphological changes when overexpressed.";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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 with isoform 2 of
CC       BSG/CD147 (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; AB179740; BAD98504.1; -; mRNA.
DR   RefSeq; NP_001094484.1; NM_001101014.1.
DR   AlphaFoldDB; Q4W8E7; -.
DR   STRING; 10116.ENSRNOP00000064502; -.
DR   iPTMnet; Q4W8E7; -.
DR   PhosphoSitePlus; Q4W8E7; -.
DR   PaxDb; Q4W8E7; -.
DR   PRIDE; Q4W8E7; -.
DR   Ensembl; ENSRNOT00000100046; ENSRNOP00000093386; ENSRNOG00000050137.
DR   GeneID; 687031; -.
DR   KEGG; rno:687031; -.
DR   CTD; 55966; -.
DR   RGD; 1590138; Ajap1.
DR   eggNOG; ENOG502QVMU; Eukaryota.
DR   GeneTree; ENSGT00510000048586; -.
DR   InParanoid; Q4W8E7; -.
DR   OrthoDB; 770398at2759; -.
DR   PhylomeDB; Q4W8E7; -.
DR   PRO; PR:Q4W8E7; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   GO; GO:0005912; C:adherens junction; ISO:RGD.
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:RGD.
DR   GO; GO:0044291; C:cell-cell contact zone; ISO:RGD.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR   GO; GO:0044214; C:spanning component of plasma membrane; ISO:RGD.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:RGD.
DR   GO; GO:0061045; P:negative regulation of wound healing; ISO:RGD.
DR   GO; GO:0030860; P:regulation of polarized epithelial cell differentiation; ISO:RGD.
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..411
FT                   /note="Adherens junction-associated protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000284803"
FT   TOPO_DOM        44..283
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..411
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          62..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..411
FT                   /note="Targeting signals"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        123..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   411 AA;  44755 MW;  28533B826DD95FE9 CRC64;
     MWIQQLLGLS SMPIRWPGRS LGSHLWILIA MLQLAVDFPS CDSLGPGPEF RLLSRPQRPQ
     RLWSLRTGPP TRLPTPAWSP RAARAERAHG PIQMQTPRAR RAHRPRDQVA TLGPKGGLTK
     PPAATRSSPS LTSASASSSM TAGAAEHQSL LKRGRRHTHD AEFNDFDFHG GRPTTETEFI
     AWGPTGDEEA LESNTFPGGF GPTTVSILQT RKTTMAATTT TTAASTATAM TLQTKGVTES
     LDPWKRTPVG VSTTEPSTSP SNNGKDIQPP RILGETSGLA VHQIITITVS LIMVIAALIT
     TLVLKNCCAP SGHTRRNSHQ RKMNQQEESC QNLTDFTPAR VPSSVDIFTA YNETLQCSHE
     CVRASVPVYA DETLHSTGEY KSTFNGNRSS SADRHLIPVA FVSEKWFEIS C