RIMS3_HUMAN
ID RIMS3_HUMAN Reviewed; 308 AA.
AC Q9UJD0; D3DPV8; Q92511; X5D7U7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Regulating synaptic membrane exocytosis protein 3;
DE Short=Nim3;
DE AltName: Full=RIM3 gamma;
DE AltName: Full=Rab-3-interacting molecule 3;
DE Short=RIM 3;
GN Name=RIMS3; Synonyms=KIAA0237;
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] (ISOFORM 1).
RX PubMed=12620390; DOI=10.1016/s0888-7543(02)00024-1;
RA Wang Y., Suedhof T.C.;
RT "Genomic definition of RIM proteins: evolutionary amplification of a family
RT of synaptic regulatory proteins.";
RL Genomics 81:126-137(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC TISSUE=Fetal brain;
RX PubMed=24722188; DOI=10.1038/ncomms4650;
RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M.,
RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I.,
RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A.,
RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D.,
RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.;
RT "Protein interaction network of alternatively spliced isoforms from brain
RT links genetic risk factors for autism.";
RL Nat. Commun. 5:3650-3650(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
CC -!- FUNCTION: Regulates synaptic membrane exocytosis. {ECO:0000250}.
CC -!- SUBUNIT: Binds PPFIA3 (By similarity). Does not bind RAB3.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UJD0; P21964-2: COMT; NbExp=3; IntAct=EBI-3909436, EBI-10200977;
CC Q9UJD0; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-3909436, EBI-8561769;
CC Q9UJD0; Q92993: KAT5; NbExp=3; IntAct=EBI-3909436, EBI-399080;
CC Q9UJD0; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-3909436, EBI-11742507;
CC Q9UJD0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-3909436, EBI-16439278;
CC Q9UJD0; P16284: PECAM1; NbExp=3; IntAct=EBI-3909436, EBI-716404;
CC Q9UJD0; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3909436, EBI-79165;
CC Q9UJD0; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-3909436, EBI-9090795;
CC Q9UJD0; P08670: VIM; NbExp=3; IntAct=EBI-3909436, EBI-353844;
CC Q9UJD0; P61981: YWHAG; NbExp=4; IntAct=EBI-3909436, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UJD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJD0-2; Sequence=VSP_055836, VSP_055837;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13243.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY326956; AAQ01683.1; -; mRNA.
DR EMBL; KJ535026; AHW56665.1; -; mRNA.
DR EMBL; D87074; BAA13243.2; ALT_INIT; mRNA.
DR EMBL; AL031289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07206.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07207.1; -; Genomic_DNA.
DR EMBL; BC003103; AAH03103.1; -; mRNA.
DR CCDS; CCDS30687.1; -. [Q9UJD0-1]
DR RefSeq; NP_055562.2; NM_014747.2. [Q9UJD0-1]
DR AlphaFoldDB; Q9UJD0; -.
DR SMR; Q9UJD0; -.
DR BioGRID; 115127; 13.
DR IntAct; Q9UJD0; 16.
DR MINT; Q9UJD0; -.
DR STRING; 9606.ENSP00000361769; -.
DR iPTMnet; Q9UJD0; -.
DR PhosphoSitePlus; Q9UJD0; -.
DR BioMuta; RIMS3; -.
DR DMDM; 41017811; -.
DR EPD; Q9UJD0; -.
DR jPOST; Q9UJD0; -.
DR MassIVE; Q9UJD0; -.
DR MaxQB; Q9UJD0; -.
DR PaxDb; Q9UJD0; -.
DR PeptideAtlas; Q9UJD0; -.
DR PRIDE; Q9UJD0; -.
DR ProteomicsDB; 84619; -. [Q9UJD0-1]
DR Antibodypedia; 18011; 101 antibodies from 29 providers.
DR DNASU; 9783; -.
DR Ensembl; ENST00000372683.1; ENSP00000361768.1; ENSG00000117016.10. [Q9UJD0-1]
DR Ensembl; ENST00000372684.8; ENSP00000361769.3; ENSG00000117016.10. [Q9UJD0-1]
DR GeneID; 9783; -.
DR KEGG; hsa:9783; -.
DR MANE-Select; ENST00000372684.8; ENSP00000361769.3; NM_014747.3; NP_055562.2.
DR UCSC; uc001cfu.2; human. [Q9UJD0-1]
DR CTD; 9783; -.
DR DisGeNET; 9783; -.
DR GeneCards; RIMS3; -.
DR HGNC; HGNC:21292; RIMS3.
DR HPA; ENSG00000117016; Tissue enriched (brain).
DR MIM; 611600; gene.
DR neXtProt; NX_Q9UJD0; -.
DR OpenTargets; ENSG00000117016; -.
DR PharmGKB; PA134980870; -.
DR VEuPathDB; HostDB:ENSG00000117016; -.
DR eggNOG; KOG2060; Eukaryota.
DR GeneTree; ENSGT00940000159332; -.
DR HOGENOM; CLU_071205_0_0_1; -.
DR InParanoid; Q9UJD0; -.
DR OMA; HIAMMDR; -.
DR OrthoDB; 109268at2759; -.
DR PhylomeDB; Q9UJD0; -.
DR TreeFam; TF315600; -.
DR PathwayCommons; Q9UJD0; -.
DR SignaLink; Q9UJD0; -.
DR SIGNOR; Q9UJD0; -.
DR BioGRID-ORCS; 9783; 8 hits in 1020 CRISPR screens.
DR ChiTaRS; RIMS3; human.
DR GenomeRNAi; 9783; -.
DR Pharos; Q9UJD0; Tbio.
DR PRO; PR:Q9UJD0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UJD0; protein.
DR Bgee; ENSG00000117016; Expressed in middle temporal gyrus and 156 other tissues.
DR Genevisible; Q9UJD0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0048786; C:presynaptic active zone; TAS:ParkinsonsUK-UCL.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISS:ParkinsonsUK-UCL.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039032; Rim-like.
DR PANTHER; PTHR12157; PTHR12157; 1.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Exocytosis; Neurotransmitter transport;
KW Phosphoprotein; Reference proteome; Synapse; Transport.
FT CHAIN 1..308
FT /note="Regulating synaptic membrane exocytosis protein 3"
FT /id="PRO_0000190204"
FT DOMAIN 156..274
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 86..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U57"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U57"
FT VAR_SEQ 121..153
FT /note="FIFPTTRLGAESQFSDFLDGLGPAQIVGRQTLA -> CVQPRAVVPSLLLGP
FT PVTEPLGRVHLPHYPARG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:24722188"
FT /id="VSP_055836"
FT VAR_SEQ 154..308
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:24722188"
FT /id="VSP_055837"
FT CONFLICT 24
FT /note="S -> G (in Ref. 3; BAA13243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 32796 MW; EDB57162FC75DF5F CRC64;
MFNGEPGPAS SGASRNVVRS SSISGEICGS QQAGGGAGTT TAKKRRSSLG AKMVAIVGLT
QWSKSTLQLP QPEGATKKLR SNIRRSTETG IAVEMRSRVT RQGSRESTDG STNSNSSDGT
FIFPTTRLGA ESQFSDFLDG LGPAQIVGRQ TLATPPMGDV HIAIMDRSGQ LEVEVIEARG
LTPKPGSKSL PATYIKVYLL ENGACLAKKK TKMTKKTCDP LYQQALLFDE GPQGKVLQVI
VWGDYGRMDH KCFMGMAQIM LDELDLSAAV TGWYKLFPTS SVADSTLGSL TRRLSQSSLE
SATSPSCS
