MCTP1_MOUSE
ID MCTP1_MOUSE Reviewed; 951 AA.
AC E9PV86;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Multiple C2 and transmembrane domain-containing protein 1 {ECO:0000305};
GN Name=Mctp1 {ECO:0000312|MGI:MGI:1926021};
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Calcium sensor which is essential for the stabilization of
CC normal baseline neurotransmitter release and for the induction and
CC long-term maintenance of presynaptic homeostatic plasticity.
CC {ECO:0000250|UniProtKB:A1ZBD6}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds Ca(2+) via the C2 domains in absence of phospholipids.
CC {ECO:0000250|UniProtKB:Q6DN14};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:D4ABL6}; Multi-pass membrane
CC protein {ECO:0000255}. Recycling endosome
CC {ECO:0000250|UniProtKB:D4ABL6}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A1ZBD6}.
CC -!- SIMILARITY: Belongs to the MCTP family. {ECO:0000305}.
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DR EMBL; AC112671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS26656.1; -.
DR RefSeq; XP_017171131.1; XM_017315642.1.
DR AlphaFoldDB; E9PV86; -.
DR SMR; E9PV86; -.
DR STRING; 10090.ENSMUSP00000118958; -.
DR iPTMnet; E9PV86; -.
DR PhosphoSitePlus; E9PV86; -.
DR MaxQB; E9PV86; -.
DR PaxDb; E9PV86; -.
DR PeptideAtlas; E9PV86; -.
DR PRIDE; E9PV86; -.
DR ProteomicsDB; 252753; -.
DR Antibodypedia; 2751; 62 antibodies from 13 providers.
DR DNASU; 78771; -.
DR Ensembl; ENSMUST00000125209; ENSMUSP00000118958; ENSMUSG00000021596.
DR GeneID; 78771; -.
DR CTD; 79772; -.
DR MGI; MGI:1926021; Mctp1.
DR VEuPathDB; HostDB:ENSMUSG00000021596; -.
DR eggNOG; KOG1030; Eukaryota.
DR GeneTree; ENSGT00940000156031; -.
DR InParanoid; E9PV86; -.
DR OrthoDB; 234298at2759; -.
DR PhylomeDB; E9PV86; -.
DR TreeFam; TF323373; -.
DR BioGRID-ORCS; 78771; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Mctp1; mouse.
DR PRO; PR:E9PV86; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; E9PV86; protein.
DR Bgee; ENSMUSG00000021596; Expressed in granulocyte and 102 other tissues.
DR ExpressionAtlas; E9PV86; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISO:MGI.
DR GO; GO:1902883; P:negative regulation of response to oxidative stress; ISO:MGI.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR Pfam; PF00168; C2; 3.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; SSF49562; 3.
DR PROSITE; PS50004; C2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Membrane;
KW Metal-binding; Reference proteome; Repeat; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..951
FT /note="Multiple C2 and transmembrane domain-containing
FT protein 1"
FT /id="PRO_0000441711"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 240..358
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 404..521
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 555..676
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 29..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 594
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 594
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 654
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 951 AA; 106795 MW; A8E942F4F2B49460 CRC64;
MEPRAATTGE LVRAASPSFQ ARLWKNLQLG VGKGKGGGGG RAGGPEHRTA ATPTPSPPPP
GTTQDALAGV GSTGSRWSGF KKRKQVLDRV FSSSQPNLCC SSPEPLEPGG AGRAEQGSTL
RRRLREHLLP VAKGSSTATG TGGVTPPGGR SPDSAPSSSS ASSSLSSSPQ PPPRGDRVRD
ESTRRGGPGV HLCHQKSSSL PGTACLEQLL EPAPPPAEPA RGPAEPQALQ KDIERDCSQK
ISTVGNSNAD VPLADPGMYQ LDITLRRGQS LAARDRGGTS DPYVKFKIGR KEVFRSKIIH
KNLNPVWEEK ACVLIDHLRE PLYIKVFDYD FGLQDDFMGS AFLDLTQLEL NRSTDVTLTL
KDPHYPDHDL GIILLSVILT PKEGEHRDVT MLMRKSWKRS SKFQTQSLRL SDQHRKSHLW
RGIVSITLIE GRDLKAMDSN GLSDPYVKFR LGHQKYKSKI MPKTLNPQWR EQFDFHLYEE
RGGIMDITAW DKDAGKRDDF IGRCQVDLSS LSREQTHKLE LHLEEGEGHL VLLVTLTASA
TVCISDLSVN SMEDQKEREE ILKRYSPLRI FNNLKDVGFL QVKVIRAEGL MAADVTGKSD
PFCVVELNND RLLTHTVYKN LNPEWNKVFT FNIKDIHSVL EVTVYDEDRD RSADFLGRVA
IPLLSIQNGE QKAYVLKNKQ LTGPTKGVIY LEIDVIFNAV KASLRTLIPK ERKYIEEENR
LSKQLLLRNF IRTKRCVIVL VNAAYYVNSC FDWDSPPRSL AAFVLFLLIV WNFELYMIPL
LLLLLLTWNY FLIISGKDNR QRDTVVEDML EDEEEEDDRD DKDGEKKGFI NKIYAIQEVC
VSVQNILDEV ASLGERIKNT FNWTVPFLSW LAIVALCVFT AILYFIPLRY IVLVWGINKF
TKKLRSPYAI DNNELLDFLS RVPSDVQVVQ YQELKPDHSH SPYKRKKNNL G
