AJAP1_HUMAN
ID AJAP1_HUMAN Reviewed; 411 AA.
AC Q9UKB5; Q9Y229;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Adherens junction-associated protein 1;
DE AltName: Full=Membrane protein shrew-1;
DE Flags: Precursor;
GN Name=AJAP1; Synonyms=MOT8, SHREW1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND INTERACTION WITH CDH1 AND CTNNB1.
RC TISSUE=Brain;
RX PubMed=14595118; DOI=10.1091/mbc.e03-05-0281;
RA Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A.,
RA Baumann R., Starzinski-Powitz A.;
RT "Novel membrane protein shrew-1 targets to cadherin-mediated junctions in
RT polarized epithelial cells.";
RL Mol. Biol. Cell 15:397-406(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibrosarcoma;
RA Kudoh S., Chung I.M., Tsuiji M., Tsuji T., Irimura T.;
RT "Identification of genes differentially expressed in HT1080 human
RT fibrosarcoma cells selected for invasive capacity in vitro.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 179-411.
RA Rhodes S.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND VARIANT ARG-263.
RX PubMed=16410724; DOI=10.4161/cbt.5.3.2391;
RA McDonald J.M., Dunlap S., Cogdell D., Dunmire V., Wei Q.,
RA Starzinski-Powitz A., Sawaya R., Bruner J., Fuller G.N., Aldape K.,
RA Zhang W.;
RT "The SHREW1 gene, frequently deleted in oligodendrogliomas, functions to
RT inhibit cell adhesion and migration.";
RL Cancer Biol. Ther. 5:300-304(2006).
RN [6]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-303; LYS-304; TYR-350; GLU-359;
RP TYR-368; TYR-380; 396-LEU--ILE-397 AND LEU-396, AND INTERACTION WITH AP1M2.
RX PubMed=16707570; DOI=10.1091/mbc.e05-11-1034;
RA Jakob V., Schreiner A., Tikkanen R., Starzinski-Powitz A.;
RT "Targeting of transmembrane protein shrew-1 to adherens junctions is
RT controlled by cytoplasmic sorting motifs.";
RL Mol. Biol. Cell 17:3397-3408(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH BSG.
RX PubMed=17267690; DOI=10.1091/mbc.e06-07-0637;
RA Schreiner A., Ruonala M., Jakob V., Suthaus J., Boles E., Wouters F.,
RA Starzinski-Powitz A.;
RT "junction protein shrew-1 influences cell invasion and interacts with
RT invasion-promoting protein CD147.";
RL Mol. Biol. Cell 18:1272-1281(2007).
RN [8]
RP SIGNAL PEPTIDE.
RX PubMed=18648515; DOI=10.1371/journal.pone.0002767;
RA Hiss J.A., Resch E., Schreiner A., Meissner M., Starzinski-Powitz A.,
RA Schneider G.;
RT "Domain organization of long signal peptides of single-pass integral
RT membrane proteins reveals multiple functional capacity.";
RL PLoS ONE 3:e2767-e2767(2008).
RN [9]
RP SIGNAL PEPTIDE.
RX PubMed=18485053; DOI=10.1111/j.1600-0854.2008.00765.x;
RA Resch E., Quaiser S., Quaiser T., Schneider G., Starzinski-Powitz A.,
RA Schreiner A.;
RT "Synergism of shrew-1's signal peptide and transmembrane segment required
RT for plasma membrane localization.";
RL Traffic 9:1344-1353(2008).
CC -!- FUNCTION: Plays a role in cell adhesion and cell migration.
CC {ECO:0000269|PubMed:16410724, ECO:0000269|PubMed:17267690}.
CC -!- SUBUNIT: Forms a complex with CDH1 and CTNNB1; interacts directly with
CC CTNNB1. Interacts with AP1M2. Interacts with isoform 2 of BSG/CD147.
CC {ECO:0000269|PubMed:14595118, ECO:0000269|PubMed:16707570,
CC ECO:0000269|PubMed:17267690}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:16707570}; Single-pass type I membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:16707570};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction,
CC adherens junction {ECO:0000269|PubMed:14595118}. Note=Mainly
CC basolateral (PubMed:16707570). Localization is mediated by AP1M2
CC (PubMed:16707570). {ECO:0000269|PubMed:16707570}.
CC -!- TISSUE SPECIFICITY: Expressed in uterus and pancreas (at protein
CC level). {ECO:0000269|PubMed:14595118}.
CC -!- PTM: Thr-237 and Ser-239 may be phosphorylated; however as this
CC position is probably extracellular, the in vivo relevance is not
CC proven.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41245.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB41246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY282806; AAP35025.1; -; mRNA.
DR EMBL; AF175409; AAD53278.1; -; mRNA.
DR EMBL; AL391808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL023586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049672; CAB41245.1; ALT_INIT; mRNA.
DR EMBL; AL049673; CAB41246.1; ALT_INIT; mRNA.
DR CCDS; CCDS54.1; -.
DR RefSeq; NP_001035943.1; NM_001042478.1.
DR RefSeq; NP_061324.1; NM_018836.3.
DR RefSeq; XP_011540088.1; XM_011541786.2.
DR AlphaFoldDB; Q9UKB5; -.
DR BioGRID; 121012; 2.
DR IntAct; Q9UKB5; 2.
DR MINT; Q9UKB5; -.
DR STRING; 9606.ENSP00000367433; -.
DR iPTMnet; Q9UKB5; -.
DR PhosphoSitePlus; Q9UKB5; -.
DR BioMuta; AJAP1; -.
DR DMDM; 74761984; -.
DR jPOST; Q9UKB5; -.
DR MassIVE; Q9UKB5; -.
DR MaxQB; Q9UKB5; -.
DR PaxDb; Q9UKB5; -.
DR PeptideAtlas; Q9UKB5; -.
DR PRIDE; Q9UKB5; -.
DR ProteomicsDB; 84765; -.
DR Antibodypedia; 2726; 55 antibodies from 17 providers.
DR DNASU; 55966; -.
DR Ensembl; ENST00000378190.7; ENSP00000367432.3; ENSG00000196581.11.
DR Ensembl; ENST00000378191.5; ENSP00000367433.3; ENSG00000196581.11.
DR GeneID; 55966; -.
DR KEGG; hsa:55966; -.
DR MANE-Select; ENST00000378191.5; ENSP00000367433.3; NM_018836.4; NP_061324.1.
DR UCSC; uc001alm.2; human.
DR CTD; 55966; -.
DR DisGeNET; 55966; -.
DR GeneCards; AJAP1; -.
DR HGNC; HGNC:30801; AJAP1.
DR HPA; ENSG00000196581; Tissue enhanced (brain, ovary).
DR MIM; 610972; gene.
DR neXtProt; NX_Q9UKB5; -.
DR OpenTargets; ENSG00000196581; -.
DR PharmGKB; PA142672629; -.
DR VEuPathDB; HostDB:ENSG00000196581; -.
DR eggNOG; ENOG502QVMU; Eukaryota.
DR GeneTree; ENSGT00510000048586; -.
DR HOGENOM; CLU_055642_1_0_1; -.
DR InParanoid; Q9UKB5; -.
DR OMA; HWRTVSP; -.
DR OrthoDB; 770398at2759; -.
DR PhylomeDB; Q9UKB5; -.
DR TreeFam; TF336539; -.
DR PathwayCommons; Q9UKB5; -.
DR SignaLink; Q9UKB5; -.
DR BioGRID-ORCS; 55966; 8 hits in 1066 CRISPR screens.
DR ChiTaRS; AJAP1; human.
DR GenomeRNAi; 55966; -.
DR Pharos; Q9UKB5; Tbio.
DR PRO; PR:Q9UKB5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UKB5; protein.
DR Bgee; ENSG00000196581; Expressed in orbitofrontal cortex and 114 other tissues.
DR Genevisible; Q9UKB5; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:UniProtKB.
DR GO; GO:0061045; P:negative regulation of wound healing; IDA:UniProtKB.
DR GO; GO:0030860; P:regulation of polarized epithelial cell differentiation; IDA:UniProtKB.
DR InterPro; IPR039239; AJAP1.
DR InterPro; IPR029198; AJAP1_PANP_C.
DR PANTHER; PTHR32422; PTHR32422; 1.
DR Pfam; PF15298; AJAP1_PANP_C; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; 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_0000284801"
FT TOPO_DOM 44..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..411
FT /note="Targeting signals"
FT REGION 311..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 263
FT /note="G -> R (in dbSNP:rs242056)"
FT /evidence="ECO:0000269|PubMed:16410724"
FT /id="VAR_031821"
FT MUTAGEN 303
FT /note="L->A: Predominantly localized to the apical
FT membrane."
FT /evidence="ECO:0000269|PubMed:16707570"
FT MUTAGEN 304
FT /note="K->A: No effect on membrane localization."
FT /evidence="ECO:0000269|PubMed:16707570"
FT MUTAGEN 350
FT /note="Y->A: Predominantly localized to the apical
FT membrane."
FT /evidence="ECO:0000269|PubMed:16707570"
FT MUTAGEN 359
FT /note="E->A: No effect on membrane localization."
FT /evidence="ECO:0000269|PubMed:16707570"
FT MUTAGEN 368
FT /note="Y->A: Predominantly localized to the apical
FT membrane."
FT /evidence="ECO:0000269|PubMed:16707570"
FT MUTAGEN 380
FT /note="Y->A: Predominantly localized to the apical
FT membrane."
FT /evidence="ECO:0000269|PubMed:16707570"
FT MUTAGEN 396..397
FT /note="LI->HV: Predominantly localized to the apical
FT membrane."
FT /evidence="ECO:0000269|PubMed:16707570"
FT MUTAGEN 396
FT /note="L->A: Predominantly localized to the apical
FT membrane."
FT /evidence="ECO:0000269|PubMed:16707570"
SQ SEQUENCE 411 AA; 44536 MW; 42C1C5F56B9FC975 CRC64;
MWIQQLLGLS SMSIRWPGRP LGSHAWILIA MFQLAVDLPA CEALGPGPEF WLLPRSPPRP
PRLWSFRSGQ PARVPAPVWS PRPPRVERIH GQMQMPRARR AHRPRDQAAA LVPKAGLAKP
PAAAKSSPSL ASSSSSSSSA VAGGAPEQQA LLRRGKRHLQ GDGLSSFDSR GSRPTTETEF
IAWGPTGDEE ALESNTFPGV YGPTTVSILQ TRKTTVAATT TTTTTATPMT LQTKGFTESL
DPRRRIPGGV STTEPSTSPS NNGEVTQPPR ILGEASGLAV HQIITITVSL IMVIAALITT
LVLKNCCAQS GNTRRNSHQR KTNQQEESCQ NLTDFPSARV PSSLDIFTAY NETLQCSHEC
VRASVPVYTD ETLHSTTGEY KSTFNGNRPS SSDRHLIPVA FVSEKWFEIS C
