AJM1_MOUSE
ID AJM1_MOUSE Reviewed; 974 AA.
AC A2AJA9; Q6P0A3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Apical junction component 1 homolog {ECO:0000305};
GN Name=Ajm1; Synonyms=Gm996;
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 STRAIN=C57BL/6J; 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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-468; SER-509; SER-512
RP AND SER-593, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
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).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-322 AND ARG-749, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May be involved in the control of adherens junction
CC integrity. {ECO:0000250|UniProtKB:A0A1C3NSL9}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:A0A1C3NSL9}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:A0A1C3NSL9}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:A0A1C3NSL9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AJA9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AJA9-2; Sequence=VSP_038820;
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DR EMBL; AL732590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065698; AAH65698.1; -; mRNA.
DR CCDS; CCDS50532.1; -. [A2AJA9-1]
DR RefSeq; NP_001005424.2; NM_001005424.2. [A2AJA9-1]
DR AlphaFoldDB; A2AJA9; -.
DR BioGRID; 237896; 3.
DR IntAct; A2AJA9; 1.
DR MINT; A2AJA9; -.
DR STRING; 10090.ENSMUSP00000109855; -.
DR iPTMnet; A2AJA9; -.
DR PhosphoSitePlus; A2AJA9; -.
DR SwissPalm; A2AJA9; -.
DR jPOST; A2AJA9; -.
DR PaxDb; A2AJA9; -.
DR PeptideAtlas; A2AJA9; -.
DR PRIDE; A2AJA9; -.
DR ProteomicsDB; 296146; -. [A2AJA9-1]
DR ProteomicsDB; 296147; -. [A2AJA9-2]
DR Antibodypedia; 32260; 47 antibodies from 10 providers.
DR DNASU; 381353; -.
DR Ensembl; ENSMUST00000114217; ENSMUSP00000109855; ENSMUSG00000029419. [A2AJA9-1]
DR Ensembl; ENSMUST00000188161; ENSMUSP00000140763; ENSMUSG00000029419. [A2AJA9-1]
DR Ensembl; ENSMUST00000191602; ENSMUSP00000140109; ENSMUSG00000029419. [A2AJA9-1]
DR GeneID; 381353; -.
DR KEGG; mmu:381353; -.
DR UCSC; uc008isq.1; mouse. [A2AJA9-1]
DR CTD; 389813; -.
DR MGI; MGI:2685842; Ajm1.
DR VEuPathDB; HostDB:ENSMUSG00000029419; -.
DR eggNOG; ENOG502QQYV; Eukaryota.
DR GeneTree; ENSGT00390000016543; -.
DR HOGENOM; CLU_012765_0_0_1; -.
DR InParanoid; A2AJA9; -.
DR OMA; KEKTHDN; -.
DR OrthoDB; 71355at2759; -.
DR PhylomeDB; A2AJA9; -.
DR TreeFam; TF323946; -.
DR BioGRID-ORCS; 381353; 0 hits in 66 CRISPR screens.
DR PRO; PR:A2AJA9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AJA9; protein.
DR Bgee; ENSMUSG00000029419; Expressed in lumbar subsegment of spinal cord and 70 other tissues.
DR ExpressionAtlas; A2AJA9; baseline and differential.
DR Genevisible; A2AJA9; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045216; P:cell-cell junction organization; IBA:GO_Central.
DR InterPro; IPR038825; Apical_junction.
DR PANTHER; PTHR21517; PTHR21517; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Membrane; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..974
FT /note="Apical junction component 1 homolog"
FT /id="PRO_0000392545"
FT REGION 23..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 322
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 749
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 749
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 202..234
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038820"
SQ SEQUENCE 974 AA; 107186 MW; 9C1D6C006770E3CC CRC64;
MTRTDPPDLL VSTVYQDIKV VDPGLTSKRQ PCERSVARPA APTPFNKRHC RSFDFLEALD
EPTMETHPEP PPPEPAPPRA RPRDSEPRRR TRSKSAPRAS QGLATAPASP PVLQRRGREA
QRAVRVEGSP RREPSYPALR ALANELHPIK LQPQRGGPGR IAPLCATPGR CAPPEPPSGP
VPHVRCRLDI KPDEAVLQHA ARSSRSCAPR ETTSWARTAP QFHGLTVPGP RHVALSRTPT
PSDLYCTDPR TLYCDGPLPG PRDYLEHRSQ PFTTPPGPTQ FFYTEEPEGY AGSFTTSPGL
PFDGYCSRPY LSEEPPRPSP RRGGSYYAGE VRTFPIQEPP SRSYYGETTR AYGMPFVPRY
VPEEPRAHPG ARTFYTEDFG RYRERDVLAR TYPHPRSSPP WADWGPRPYR TLQVMPPPAP
GPLLASWHGG TGTSPPRLAT DSRHYSRSWD NILAPGPRRE DPLGRGRSYE NLLGREVRDT
RGSSPEGRRP PVVVNLSTSP RRYAALSLSE TSLTEKGRAG ESLGRNWYVT PEITITDNDL
RSVDRPTAKG WELPGGRPRQ PVSTVPEGPA SSRQRSLEQL DELITDLVID SRSPAQAPEP
AAEGLGRQLR RLLDSRAAGP GGATLLAPSR SPPASAGSTE EPTGSGEAAD ASPEPSADED
DLMTCSNARC RRTETMFNAC LYFKSCHSCY TYYCSRLCRR EDWDAHKARC VYGRVGSVCR
HVLQFCRDSS PVHRAFSRIA RVGFLSRGRG VLFLGFPSPG SADNFLRFGL EGLLLSPTYL
SLRELATHAA PLGSYARELA AAGRLYEPAE CFLLSVSVAV GPSAAPPGAA ARPAPRTPGP
TVRKFAKVAL AAGSPTRPPP ARGGEPDMET LILTPPPGTA GLDEEGEAGR RAREVAFIHI
QRELRMRGVF LRHEFPRVYE QLCEFVEANR RFTPTTIYPT DRRTGRPFMC MIMAASEPRA
LDWVASANLL DDIM
