ID A0A452CB15_BALAS Unreviewed; 1245 AA.
AC A0A452CB15;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE SubName: Full=Regulating synaptic membrane exocytosis protein 2 isoform X4 {ECO:0000313|RefSeq:XP_028020094.1};
GN Name=RIMS2 {ECO:0000313|RefSeq:XP_028020094.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028020094.1};
RN [1] {ECO:0000313|RefSeq:XP_028020094.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028020094.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
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DR RefSeq; XP_028020094.1; XM_028164293.1.
DR AlphaFoldDB; A0A452CB15; -.
DR Proteomes; UP000261681; Unplaced.
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 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; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
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; PF17820; PDZ_6; 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; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
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 20..76
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 524..610
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 677..800
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1091..1209
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1245 AA; 141573 MW; 3B32D9502F7F93DE CRC64;
MYKEQVKKMG EESQQQQEQK GDAPTCGICH KTKFADGCGH NCSYCQTKFC ARCGGRVSLR
SNKVMWVCNL CRKQQEILTK SGAWFYNSGS NTPQQPDQKV LRGLRNEEAP QEKKAKLHEQ
AQFQGPSGDL SVPAVEKSRS HGLTRQDSIK NGSGVKHQIA SDVASDRKRS PSVSRDQNRR
YDQREEREEY SQYATSDSAM PRSPSDYADR RSQREPQFYE ESDHINYRDS NRRSHRHSKE
YIVDDEDAEG RDEYERQRRE EEYQARYRSD PNLARYPVKP QPYEEQMRIH AEVSRARHER
RHSDVSLANS ELEDSRISML RMERPSRQRS VSERRAAMEN QRSYSMERTR EAQGPSSYPQ
RTTNHSPPTP RRSPIPIDRP DMRRTDSLRK QQHLDPSSAV RKTKREKMET MLRNDSLSSD
QSESVRPPPP KPHKSKKGGK MRQVSLSSSE EELASTPEYT SCDDVEIESE SVSEKGDMDY
NWLDHTSWHS SEASPMSLHP VTWQPSKDGD RLIGRILLNK CLKDGSVPRD SGAMLGLKVV
GGKMTESGRL CAFITKVKKG SLADTVGHLR PGDEVLEWNG RLLQGATFEE VYNIILESKP
EPQVELVVSR PIGDIPRIPD STHAQLESSS SSFESQKMDR PSISVTSPMS PGMLRDVPQF
LSGQLSSQSL SRRTTPFVPR VQIKLWFDKV GHQLIVTILG AKDLPSREDG RPRNPYVKIY
FLPDRSDKNK RRTKTVKKTL EPKWNQTFIY SPVHRREFRE RMLEITLWDQ ARVREEESEF
LGEILIELET ALLDDEPHWY KLQTHDVSSL PLPHPSPYMP RRQLHGESPT RRLQRSKRIS
DSEVSDYDCD DGIGVVSDYR HNGRDLQSST LSVPEQVMSS NYCSPSGSPH RVDVIGRTRS
WSPSVPPPQS RNVEQGLRGT RSTTGHYNTI SRMDRHRVMD DHYSPDRDSH FLTLPRSRYS
QTIEHHHRDG RSHPRTGSVQ TNPSSTPVAG RRGRQLPQLP PKGTLERKAG GKKLRSTVQR
STETGLAVEM RNWMTRQASR ESTDGSVNSY SSEGNLIFPG VRLASDSQFS DFLDGLGPAQ
LVGRQTLATP AMGDIQVGMM DKKGQLEVEI IRARGLVVKP GSKTLPAPYV KVYLLDNGVC
IAKKKTKVAR KTLEPLYQQL LSFEESPQGK ILQIIVWGDY GRMDHKSFMG VAQILLDELE
LSNMVIGWFK LFPPSSLVDP TLAPLTRRAS QSSLESSTGP SYSRS
//
