ID A0A2K6BLC5_MACNE Unreviewed; 1349 AA.
AC A0A2K6BLC5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Regulating synaptic membrane exocytosis 2 {ECO:0000313|Ensembl:ENSMNEP00000012200.1};
GN Name=RIMS2 {ECO:0000313|Ensembl:ENSMNEP00000012200.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000012200.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000012200.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_011729926.1; XM_011731624.1.
DR Ensembl; ENSMNET00000036395.1; ENSMNEP00000012200.1; ENSMNEG00000030361.1.
DR GeneID; 105476014; -.
DR CTD; 9699; -.
DR GeneTree; ENSGT00940000155236; -.
DR OrthoDB; 2891597at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000030361; Expressed in cerebellum and 5 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd04031; C2A_RIM1alpha; 1.
DR CDD; cd04028; C2B_RIM1alpha; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR041282; FYVE_2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR010911; Rab_BD.
DR InterPro; IPR039032; Rim-like.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12157; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN; 1.
DR PANTHER; PTHR12157:SF15; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 2; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02318; FYVE_2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50916; RABBD; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 26..154
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 86..142
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 590..676
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 743..866
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1195..1313
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..85
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 226..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1349 AA; 153237 MW; FBD8AB39DB411158 CRC64;
MSAPVGPRGR PAATPAASQP PLQPEMPDLS HLTEEERKII LAVMDRQKKE EEKEQSVLKK
LHQQFEMYKE QVKKMGEESQ QQQEQKGDAP TCGICHKTKF ADGCGHNCSY CQTKFCARCG
GRVSLRSNKV MWVCNLCRKQ QEILTKSGAW FYNSGTNTPQ QPDQKVLRGL RNEEAPQEKK
PKLHEQTQFQ GPSGDLSVPA VEKSRSHGLT RQDSIKNGSG VKHHIASDIA SDRKRSPSVS
RDQNRRYDQR EEREEYSQYA TSDSAMPRSP SDYADRRSQH EPQFYEDSDH LSYRDSNRRS
HRHSKEYIVD DEDVESRDEY ERQRREEEYQ SRYRSDPNLA RYPVKPQPYE EQMRIHAEVS
RARHERRHSD VSLANADLED SRISMLRMDR PSRQRSISER RAAMENQRSY SMERTREAQG
PSSYAQRTTN HSPPTPRRSP LPIDRPDLRR TDSLRKQHHL DPSSAVRKTK REKMETMLRN
DSLSSDQSES VRPPPPKPHK SKKGGKMRQV SLSSSEEELA STPEYTSCDD VEIESESVSE
KGDMDYNWLD HTSWHSSEAS PMSLHPVTWQ PSKDGDRLIG RILLNKRLKD GSVPRDSGAM
LGLKVVGGKM TESGRLCAFI TKVKKGSLAD TVGHLRPGDE VLEWNGRLLQ GATFEEVYNI
ILESKPEPQV ELVVSRPIGD IPRIPDSTHA QLESSSSSFE SQKMDRPSIS VTSPMSPGML
RDVPQFLSGQ LSSQSLSRRT TPFVPRVQIK LWFDKVGHQL IVTILGAKDL PSREDGRPRN
PYVKIYFLPD RSDKNKRRTK TVKKTLEPKW NQTFIYSPVH RREFRERMLE ITLWDQARVR
EEESEFLGEI LIELETALLD DEPHWYKLQT HDVSSLPLPH PSPYMPRRQL HGESPTRRLQ
RSKRISDSEV SDYDCDDGIG VVSDYRHDGR DLQSSTLSVP EQVMSSNHCS PSGSPHRVDV
IGRTRSWSPS VPPPQSRNVE QGHRGTRTTT GHYNTISRMD RHRVMDDHYS PDRDRDCEAA
DRQPYHRSRS AEQRPLLERT TTRSRSTERP DTNLMRSMPS LMTGRSAPPS PALSRSHPRT
GSVQTSPSST PVAGRRGRQL PQLPPKGTLD RKAGGKKLRS TVQRSTETGL AVEMRNWMTR
QASRESTDGS MNSYSSEGNL IFPGVRLASD SQFSDFLDGL GPAQLVGRQT LATPAMGDIQ
VGMMDKKGQL EVEIIRARGL VVKPGSKTLP APYVKVYLLD NGVCIAKKKT KVARKTLEPL
YQQLLSFEES PQGKVLQIIV WGDYGRMDHK SFMGVAQILL DELELSNMVI GWFKLFPPSS
LVDPTLAPLT RRASQSSLES STGPSYSRS
//
