RIMS2_HUMAN
ID RIMS2_HUMAN Reviewed; 1411 AA.
AC Q9UQ26; B3KX91; F8WD47; O43413; Q86XL9; Q8IWV9; Q8IWW1;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Regulating synaptic membrane exocytosis protein 2;
DE AltName: Full=Rab-3-interacting molecule 2;
DE Short=RIM 2;
DE AltName: Full=Rab-3-interacting protein 3;
GN Name=RIMS2; Synonyms=KIAA0751, RAB3IP3, RIM2;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hypothalamus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 689-1411 (ISOFORMS 4 AND 5).
RA Ho H.C.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP ALTERNATIVE SPLICING, AND GENOMIC ORGANIZATION.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-689, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND SER-1396, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
RA Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y.,
RA Yoon T.J.;
RT "SYT14L, especially its C2 domain, is involved in regulating melanocyte
RT differentiation.";
RL J. Dermatol. Sci. 72:246-251(2013).
RN [11]
RP INVOLVEMENT IN CRSDS, VARIANTS CRSDS 532-SER--SER-1411 DEL;
RP 962-GLN--SER-1411 DEL; 1042-GLU--SER-1411 DEL AND 1170-THR--SER-1411 DEL,
RP AND TISSUE SPECIFICITY.
RX PubMed=32470375; DOI=10.1016/j.ajhg.2020.04.018;
RA Mechaussier S., Almoallem B., Zeitz C., Van Schil K., Jeddawi L.,
RA Van Dorpe J., Duenas Rey A., Condroyer C., Pelle O., Polak M., Boddaert N.,
RA Bahi-Buisson N., Cavallin M., Bacquet J.L., Mouallem-Beziere A.,
RA Zambrowski O., Sahel J.A., Audo I., Kaplan J., Rozet J.M., De Baere E.,
RA Perrault I.;
RT "Loss of Function of RIMS2 Causes a Syndromic Congenital Cone-Rod Synaptic
RT Disease with Neurodevelopmental and Pancreatic Involvement.";
RL Am. J. Hum. Genet. 106:859-871(2020).
RN [12]
RP STRUCTURE BY NMR OF 637-934.
RG RIKEN structural genomics initiative (RSGI);
RT "PDZ domain and the first C2 domain of human RIM2B.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Rab effector involved in exocytosis. May act as scaffold
CC protein. Plays a role in dendrite formation by melanocytes
CC (PubMed:23999003). {ECO:0000269|PubMed:23999003}.
CC -!- SUBUNIT: Interacts with RAB3A and RAB3B that have been activated by
CC GTP-binding. Interacts with RAB3C, RAB3D and RAB26. Interacts with
CC TSPOAP1 and RIMBP2. Interacts with PPFIA3 and PPFIA4. Interacts via its
CC zinc finger with the first C2 domain of UNC13A. Forms a complex
CC consisting of UNC13A, RIMS2 and RAB3A. Heterodimer with PCLO. Part of a
CC ternary complex involving PCLO and EPAC2 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UQ26; P16333: NCK1; NbExp=2; IntAct=EBI-1756749, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Synapse {ECO:0000250}. Presynaptic cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=6; Synonyms=RIM2-alpha;
CC IsoId=Q9UQ26-6; Sequence=Displayed;
CC Name=1; Synonyms=RIM2-beta;
CC IsoId=Q9UQ26-1; Sequence=VSP_040865, VSP_040866;
CC Name=2;
CC IsoId=Q9UQ26-2; Sequence=VSP_040872, VSP_040873;
CC Name=3;
CC IsoId=Q9UQ26-3; Sequence=VSP_040865, VSP_040866, VSP_040867,
CC VSP_040874;
CC Name=4; Synonyms=RimL3a;
CC IsoId=Q9UQ26-4; Sequence=VSP_040868, VSP_040871;
CC Name=5; Synonyms=RimL3c;
CC IsoId=Q9UQ26-5; Sequence=VSP_040869, VSP_040870;
CC Name=7; Synonyms=RIM2-gamma;
CC IsoId=Q9UQ26-7; Sequence=VSP_040864, VSP_040875;
CC Name=8;
CC IsoId=Q9UQ26-8; Sequence=VSP_044661, VSP_040867, VSP_044662;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:32470375). Expressed in
CC melanocytes (PubMed:23999003). In fetal tissues, predominantly
CC expressed in the brain (PubMed:32470375). In the retina, expressed in
CC the outer plexiform layer (at protein level) (PubMed:32470375). In the
CC cerebellum, expressed in Purkinje cells (at protein level)
CC (PubMed:32470375). In the pancreas, expressed in Langerhans islets (at
CC protein level) (PubMed:32470375). {ECO:0000269|PubMed:23999003,
CC ECO:0000269|PubMed:32470375}.
CC -!- DISEASE: Cone-rod synaptic disorder syndrome, congenital non-
CC progressive (CRSDS) [MIM:618970]: An autosomal recessive disorder
CC characterized by reduced visual acuity, photophobia, nystagmus,
CC distinctive electroretinographic features, neurodevelopmental delay,
CC poor or absent language, autistic behaviors, and abnormal glucose
CC homeostasis. {ECO:0000269|PubMed:32470375}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34471.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018294; BAA34471.2; ALT_INIT; mRNA.
DR EMBL; AF007156; AAC19157.1; -; mRNA.
DR EMBL; AK126939; BAG54403.1; -; mRNA.
DR EMBL; AC007751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043144; AAH43144.1; -; mRNA.
DR EMBL; AY057119; AAL23679.1; -; mRNA.
DR EMBL; AY057121; AAL23681.1; -; mRNA.
DR CCDS; CCDS43761.1; -. [Q9UQ26-3]
DR CCDS; CCDS55269.1; -. [Q9UQ26-8]
DR CCDS; CCDS64948.1; -. [Q9UQ26-1]
DR CCDS; CCDS64949.1; -. [Q9UQ26-7]
DR RefSeq; NP_001093587.1; NM_001100117.2. [Q9UQ26-8]
DR RefSeq; NP_001269810.1; NM_001282881.1. [Q9UQ26-1]
DR RefSeq; NP_001269811.1; NM_001282882.1. [Q9UQ26-7]
DR RefSeq; NP_055492.3; NM_014677.4. [Q9UQ26-3]
DR PDB; 1V27; NMR; -; A=807-934.
DR PDB; 1WFG; NMR; -; A=637-754.
DR PDBsum; 1V27; -.
DR PDBsum; 1WFG; -.
DR AlphaFoldDB; Q9UQ26; -.
DR BMRB; Q9UQ26; -.
DR SMR; Q9UQ26; -.
DR BioGRID; 115051; 8.
DR IntAct; Q9UQ26; 10.
DR MINT; Q9UQ26; -.
DR STRING; 9606.ENSP00000262231; -.
DR GlyGen; Q9UQ26; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UQ26; -.
DR PhosphoSitePlus; Q9UQ26; -.
DR BioMuta; RIMS2; -.
DR DMDM; 41019522; -.
DR EPD; Q9UQ26; -.
DR MassIVE; Q9UQ26; -.
DR MaxQB; Q9UQ26; -.
DR PeptideAtlas; Q9UQ26; -.
DR PRIDE; Q9UQ26; -.
DR ProteomicsDB; 31373; -.
DR ProteomicsDB; 85496; -. [Q9UQ26-6]
DR ProteomicsDB; 85497; -. [Q9UQ26-1]
DR ProteomicsDB; 85498; -. [Q9UQ26-2]
DR ProteomicsDB; 85499; -. [Q9UQ26-3]
DR ProteomicsDB; 85500; -. [Q9UQ26-4]
DR ProteomicsDB; 85501; -. [Q9UQ26-5]
DR ProteomicsDB; 85502; -. [Q9UQ26-7]
DR Antibodypedia; 26403; 215 antibodies from 29 providers.
DR DNASU; 9699; -.
DR Ensembl; ENST00000262231.14; ENSP00000262231.10; ENSG00000176406.23. [Q9UQ26-1]
DR Ensembl; ENST00000339750.3; ENSP00000342051.2; ENSG00000176406.23. [Q9UQ26-7]
DR Ensembl; ENST00000504942.6; ENSP00000427018.3; ENSG00000176406.23. [Q9UQ26-8]
DR Ensembl; ENST00000507740.5; ENSP00000423559.1; ENSG00000176406.23. [Q9UQ26-3]
DR GeneID; 9699; -.
DR KEGG; hsa:9699; -.
DR UCSC; uc003ylq.4; human. [Q9UQ26-6]
DR CTD; 9699; -.
DR DisGeNET; 9699; -.
DR GeneCards; RIMS2; -.
DR HGNC; HGNC:17283; RIMS2.
DR HPA; ENSG00000176406; Group enriched (adrenal gland, brain, retina).
DR MalaCards; RIMS2; -.
DR MIM; 606630; gene.
DR MIM; 618970; phenotype.
DR neXtProt; NX_Q9UQ26; -.
DR OpenTargets; ENSG00000176406; -.
DR PharmGKB; PA38445; -.
DR VEuPathDB; HostDB:ENSG00000176406; -.
DR eggNOG; KOG2060; Eukaryota.
DR GeneTree; ENSGT00940000155236; -.
DR InParanoid; Q9UQ26; -.
DR OrthoDB; 109268at2759; -.
DR PhylomeDB; Q9UQ26; -.
DR TreeFam; TF321703; -.
DR PathwayCommons; Q9UQ26; -.
DR SignaLink; Q9UQ26; -.
DR SIGNOR; Q9UQ26; -.
DR BioGRID-ORCS; 9699; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; RIMS2; human.
DR EvolutionaryTrace; Q9UQ26; -.
DR GeneWiki; RIMS2; -.
DR GenomeRNAi; 9699; -.
DR Pharos; Q9UQ26; Tbio.
DR PRO; PR:Q9UQ26; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9UQ26; protein.
DR Bgee; ENSG00000176406; Expressed in lateral nuclear group of thalamus and 145 other tissues.
DR ExpressionAtlas; Q9UQ26; baseline and differential.
DR Genevisible; Q9UQ26; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; TAS:ParkinsonsUK-UCL.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; ISS:ParkinsonsUK-UCL.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030073; P:insulin secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; ISS:ParkinsonsUK-UCL.
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:0061669; P:spontaneous neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR039032; Rim-like.
DR InterPro; IPR030631; RIM2.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12157; PTHR12157; 2.
DR PANTHER; PTHR12157:SF15; PTHR12157:SF15; 2.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Differentiation; Disease variant; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..1411
FT /note="Regulating synaptic membrane exocytosis protein 2"
FT /id="PRO_0000190201"
FT DOMAIN 26..185
FT /note="RabBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT DOMAIN 668..754
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 805..928
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1257..1375
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 117..173
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 689
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ7"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ7"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS1"
FT MOD_RES 1396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQZ7"
FT VAR_SEQ 1..1126
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_040864"
FT VAR_SEQ 1..223
FT /note="Missing (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_040865"
FT VAR_SEQ 50..90
FT /note="KVKEEHKPQLTQWFPFSGITELVNNVLQPQQKQQNEKEPQT -> EEEKEQS
FT VLK (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044661"
FT VAR_SEQ 224..263
FT /note="SGDLSVPAVEKSRSHGLTRQHSIKNGSGVKHHIASDIASD -> MQFETLRQ
FT VCNSVLSHFHGVFSSPPNILQNELFGQTLNNA (in isoform 1 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_040866"
FT VAR_SEQ 575..642
FT /note="SQKGKRKTSEQAVLSDSNTRSERQKEMMYFGGHSLEEDLEWSEPQIKDSGVD
FT TCSSTTLNEEHSHSDK -> MDYNWLDHTSWHSSEASPMSL (in isoform 3 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_040867"
FT VAR_SEQ 774..801
FT /note="SSSFESQKMDRPSISVTSPMSPGMLRDV -> KFYLCWKKTLFIIAFIRDQM
FT KYLTSNVK (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_040868"
FT VAR_SEQ 802..1411
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_040871"
FT VAR_SEQ 810
FT /note="S -> SSQSLSRRTTPFVPRVQ (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044662"
FT VAR_SEQ 811..824
FT /note="IKLWFDKVGHQLIV -> VCSHYVYSSFWNIK (in isoform 5)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_040869"
FT VAR_SEQ 825..1411
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_040870"
FT VAR_SEQ 1038
FT /note="S -> R (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040872"
FT VAR_SEQ 1039..1411
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_040873"
FT VAR_SEQ 1076
FT /note="D -> DSHFLTLPRSRYSQTIDHHHRDG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040874"
FT VAR_SEQ 1127..1174
FT /note="RSAPPSPALSRSHPRTGSVQTSPSSTPVAGRRGRQLPQLPPKGTLDRK ->
FT MGRQGLGGASAAGRSMQRSQSRSSLSASFEALAGYFPCMNSLEEEEGE (in
FT isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_040875"
FT VARIANT 532..1411
FT /note="Missing (in CRSDS)"
FT /evidence="ECO:0000269|PubMed:32470375"
FT /id="VAR_084549"
FT VARIANT 962..1411
FT /note="Missing (in CRSDS)"
FT /evidence="ECO:0000269|PubMed:32470375"
FT /id="VAR_084550"
FT VARIANT 1042..1411
FT /note="Missing (in CRSDS)"
FT /evidence="ECO:0000269|PubMed:32470375"
FT /id="VAR_084551"
FT VARIANT 1170..1411
FT /note="Missing (in CRSDS)"
FT /evidence="ECO:0000269|PubMed:32470375"
FT /id="VAR_084552"
FT CONFLICT 309
FT /note="S -> F (in Ref. 5; AAH43144)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="Q -> R (in Ref. 5; AAH43144)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="M -> V (in Ref. 3; BAG54403)"
FT /evidence="ECO:0000305"
FT STRAND 646..649
FT /evidence="ECO:0007829|PDB:1WFG"
FT STRAND 651..663
FT /evidence="ECO:0007829|PDB:1WFG"
FT TURN 677..680
FT /evidence="ECO:0007829|PDB:1WFG"
FT STRAND 681..688
FT /evidence="ECO:0007829|PDB:1WFG"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:1WFG"
FT STRAND 694..701
FT /evidence="ECO:0007829|PDB:1WFG"
FT HELIX 706..710
FT /evidence="ECO:0007829|PDB:1WFG"
FT STRAND 718..722
FT /evidence="ECO:0007829|PDB:1WFG"
FT HELIX 732..741
FT /evidence="ECO:0007829|PDB:1WFG"
FT STRAND 743..754
FT /evidence="ECO:0007829|PDB:1WFG"
FT STRAND 808..816
FT /evidence="ECO:0007829|PDB:1V27"
FT TURN 817..820
FT /evidence="ECO:0007829|PDB:1V27"
FT STRAND 821..831
FT /evidence="ECO:0007829|PDB:1V27"
FT STRAND 836..838
FT /evidence="ECO:0007829|PDB:1V27"
FT STRAND 843..846
FT /evidence="ECO:0007829|PDB:1V27"
FT STRAND 854..857
FT /evidence="ECO:0007829|PDB:1V27"
FT HELIX 885..887
FT /evidence="ECO:0007829|PDB:1V27"
FT STRAND 890..898
FT /evidence="ECO:0007829|PDB:1V27"
FT STRAND 900..903
FT /evidence="ECO:0007829|PDB:1V27"
FT STRAND 910..915
FT /evidence="ECO:0007829|PDB:1V27"
FT HELIX 916..918
FT /evidence="ECO:0007829|PDB:1V27"
FT STRAND 925..929
FT /evidence="ECO:0007829|PDB:1V27"
SQ SEQUENCE 1411 AA; 160403 MW; 9D4E83F4CBE4A864 CRC64;
MSAPVGPRGR LAPIPAASQP PLQPEMPDLS HLTEEERKII LAVMDRQKKK VKEEHKPQLT
QWFPFSGITE LVNNVLQPQQ KQQNEKEPQT KLHQQFEMYK EQVKKMGEES QQQQEQKGDA
PTCGICHKTK FADGCGHNCS YCQTKFCARC GGRVSLRSNK VMWVCNLCRK QQEILTKSGA
WFYNSGSNTP QQPDQKVLRG LRNEEAPQEK KPKLHEQTQF QGPSGDLSVP AVEKSRSHGL
TRQHSIKNGS GVKHHIASDI ASDRKRSPSV SRDQNRRYDQ REEREEYSQY ATSDTAMPRS
PSDYADRRSQ HEPQFYEDSD HLSYRDSNRR SHRHSKEYIV DDEDVESRDE YERQRREEEY
QSRYRSDPNL ARYPVKPQPY EEQMRIHAEV SRARHERRHS DVSLANADLE DSRISMLRMD
RPSRQRSISE RRAAMENQRS YSMERTREAQ GPSSYAQRTT NHSPPTPRRS PLPIDRPDLR
RTDSLRKQHH LDPSSAVRKT KREKMETMLR NDSLSSDQSE SVRPPPPKPH KSKKGGKMRQ
ISLSSSEEEL ASTPEYTSCD DVEIESESVS EKGDSQKGKR KTSEQAVLSD SNTRSERQKE
MMYFGGHSLE EDLEWSEPQI KDSGVDTCSS TTLNEEHSHS DKHPVTWQPS KDGDRLIGRI
LLNKRLKDGS VPRDSGAMLG LKVVGGKMTE SGRLCAFITK VKKGSLADTV GHLRPGDEVL
EWNGRLLQGA TFEEVYNIIL ESKPEPQVEL VVSRPIGDIP RIPDSTHAQL ESSSSSFESQ
KMDRPSISVT SPMSPGMLRD VPQFLSGQLS IKLWFDKVGH QLIVTILGAK DLPSREDGRP
RNPYVKIYFL PDRSDKNKRR TKTVKKTLEP KWNQTFIYSP VHRREFRERM LEITLWDQAR
VREEESEFLG EILIELETAL LDDEPHWYKL QTHDVSSLPL PHPSPYMPRR QLHGESPTRR
LQRSKRISDS EVSDYDCDDG IGVVSDYRHD GRDLQSSTLS VPEQVMSSNH CSPSGSPHRV
DVIGRTRSWS PSVPPPQSRN VEQGLRGTRT MTGHYNTISR MDRHRVMDDH YSPDRDRDCE
AADRQPYHRS RSTEQRPLLE RTTTRSRSTE RPDTNLMRSM PSLMTGRSAP PSPALSRSHP
RTGSVQTSPS STPVAGRRGR QLPQLPPKGT LDRKAGGKKL RSTVQRSTET GLAVEMRNWM
TRQASRESTD GSMNSYSSEG NLIFPGVRLA SDSQFSDFLD GLGPAQLVGR QTLATPAMGD
IQVGMMDKKG QLEVEIIRAR GLVVKPGSKT LPAPYVKVYL LDNGVCIAKK KTKVARKTLE
PLYQQLLSFE ESPQGKVLQI IVWGDYGRMD HKSFMGVAQI LLDELELSNM VIGWFKLFPP
SSLVDPTLAP LTRRASQSSL ESSTGPSYSR S
