LOCUS       NP_055804               1692 aa            linear   PRI 03-MAY-2024
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_055804
VERSION     NP_055804.2
DBSOURCE    REFSEQ: accession NM_014989.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1692)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1692)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   3  (residues 1 to 1692)
  AUTHORS   Warwick,A.N., Shawkat,F. and Lotery,A.J.
  TITLE     Retinitis pigmentosa and bilateral cystoid macular oedema in a
            patient heterozygous for the RIM1 mutation previously associated
            with cone-rod dystrophy 7
  JOURNAL   Ophthalmic Genet 38 (2), 178-182 (2017)
   PUBMED   27176872
  REMARK    GeneRIF: This is the first reported case of bilateral cystoid
            macular edema in association with the RIM1 mutation. Overall, our
            findings were more consistent with a phenotype of retinitis
            pigmentosa.
REFERENCE   4  (residues 1 to 1692)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   5  (residues 1 to 1692)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   6  (residues 1 to 1692)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 1692)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 1692)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 1692)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 1692)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390056.7, AL034373.13,
            AL590011.5, AL445256.18 and AL035633.18.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 21, 2004 this sequence version replaced NP_055804.1.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY190519.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000521978.6/ ENSP00000428417.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1692
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..1692
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 1"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=188942
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          114..146
                     /region_name="BRcat_Rcat_RBR"
                     /note="BRcat (benign-catalytic) and Rcat
                     (required-for-catalysis) domains, part of the RBR
                     (RING1-BRcat-Rcat) domain; cl45895"
                     /db_xref="CDD:459240"
     Site            order(116,132,135,140,143)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:438995"
     Region          <131..186
                     /region_name="FYVE_like_SF"
                     /note="FYVE domain like superfamily; cl28890"
                     /db_xref="CDD:333710"
     Region          183..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          191..>284
                     /region_name="DUF601"
                     /note="Protein of unknown function, DUF601; pfam04642"
                     /db_xref="CDD:282493"
     Region          <257..536
                     /region_name="PLN03237"
                     /note="DNA topoisomerase 2; Provisional"
                     /db_xref="CDD:215641"
     Site            500
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIR4; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIR4; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          594..690
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(615..621,636,639,669,673,676..677)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          698..732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NE5; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            731
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NE5; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          742..868
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(773,779,834,836,844)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          870..1013
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NE5; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            977
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIR4; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1031
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NE5; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          1118..1222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          1235..1278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NE5; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1254
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIR4; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NE5; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1308
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIR4; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIR4; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIR4; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          1332..1394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NE5; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NE5; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NE5; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          1408..1428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIR4; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          1445..1495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     Region          1523..1668
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(1580,1584..1585,1587,1590,1618,1620,1622,1666..1667)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     Site            1677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1680
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1683
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     Site            1692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86UR5.1)"
     CDS             1..1692
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_014989.7:475..5553"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47449.1"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mssavgprgp rpptvpppmq elpdlshlte eerniimavm drqkeeeeke eamlkcvvrd
       61 makpaacktp rnaenqphqp sprlhqqfes ykeqvrkige earryqgehk ddaptcgich
      121 ktkfadgcgh lcsycrtkfc arcggrvslr snnedkvvmw vcnlcrkqqe iltksgawff
      181 gsgpqqtsqd gtlsdtatga gsevprekka rlqersrsqt plstaaassq daappsappd
      241 rskgaepsqq algpeqkqas srsrseppre rkktpglseq ngkgalkser krvpktsaqp
      301 vegaveerer kerresrrle kgrsqdypdt pekrdegkaa deekqrkeed yqtryrsdpn
      361 larypvkppp eeqqmrmhar vsrarherrh sdvalprtea gaalpegkag krapaaaras
      421 ppdspraysa ertaetrapg akqltnhspp aprhgpvpae apelkaqepl rkqsrldpss
      481 avlmrkakre kvetmlrnds lssdqsesvr psppkphrsk rggkkrqmsv ssseeegvst
      541 peytscedve lesesvsekg dldyywldpa twhsretspi sshpvtwqps kegdrligrv
      601 ilnkrttmpk dsgallglkv vggkmtdlgr lgafitkvkk gsladvvghl ragdevlewn
      661 gkplpgatne evyniilesk sepqveiivs rpigdiprip esshppless sssfesqkme
      721 rpsisvispt spgalkdapq vlpgqlsvkl wydkvghqli vnvlqatdlp arvdgrprnp
      781 yvkmyflpdr sdkskrrtkt vkkilepkwn qtfvyshvhr rdfrermlei tvwdqprvqe
      841 eeseflgeil ieletalldd ephwyklqth desslplpqp spfmprrhih gessskklqr
      901 sqrisdsdis dyevddgigv vppvgyrssa resksttltv peqqrtthhr srsvsphrgn
      961 dqgkprsrlp nvplqrslde ihptrrsrsp trhhdasrsp vdhrtrdvds qylseqdsel
     1021 lmlprakrgr saeclhttrh lvrhyktlpp kmpllqsssh wniyssilpa htktksvtrq
     1081 dislhhecfn stvlrftdei lvselqpfld rarsastncl rpdtslhspe rergrwspsl
     1141 drrrppspri qiqhaspend rhsrkserss iqkqtrkgta sdaervlptc lsrrghaapr
     1201 atdqpvirgk hparsrsseh ssirtlcsmh hlvpggsapp splltrmhrq rsptqsppad
     1261 tsfssrrgrq lpqvpvrsgs ieqaslvvee rtrqmkmkvh rfkqttgsgs sqeldreqys
     1321 kynihkdqyr scdnvsakss dsdvsdvsai srtssasrls stsfmseqse rprgrissft
     1381 pkmqgrrmgt sgrsimksts vsgemytleh ndgsqsdtav gtvgaggkkr rsslsakvva
     1441 ivsrrsrsts qlsqtesghk klkstiqrst etgmaaemrk mvrqpsrest dgsinsysse
     1501 gnlifpgvrl gadsqfsdfl dglgpaqlvg rqtlatpamg diqigmedkk gqlevevira
     1561 rsltqkpgsk stpapyvkvy llengaciak kktriarktl dplyqqslvf despqgkvlq
     1621 vivwgdygrm dhkcfmgvaq illeeldlss mvigwyklfp psslvdptlt pltrrasqss
     1681 lesstgppci rs
//
