ID A0A2Y9T7U2_PHYMC Unreviewed; 1519 AA.
AC A0A2Y9T7U2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Regulating synaptic membrane exocytosis protein 2 isoform X11 {ECO:0000313|RefSeq:XP_023985697.1};
GN Name=RIMS2 {ECO:0000313|RefSeq:XP_023985697.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023985697.1};
RN [1] {ECO:0000313|RefSeq:XP_023985697.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023985697.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_023985697.1; XM_024129929.3.
DR Proteomes; UP000248484; Chromosome 15.
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:UP000248484};
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..158
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 86..146
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 593..679
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 730..853
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1365..1483
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..85
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..22
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1519 AA; 171790 MW; 35AA1A22907E3E20 CRC64;
MSAPVGPRGR PAPTPAASQP PLQPEMPDLS HLTEEERKII LAVMDRQKKE EEKEQSVLKK
LHQQFEVYKE QVKKMGEESQ QQQEQKGDAP TCGICHKTKF ADGCGHNCSY CQTKFCARCG
GRVSLRSNKE DKVVMWVCNL CRKQQEILTK SGAWFYNSGS NTPQQPDQKV LRGLRNEEAP
QEKKAKLHEQ APFQGPSGDL SVPAVEKSRS HGLTRQDSIK NGSGVKHQIA SDVASDRKRS
PSVSRDQNRR YDQREEREYP QYATSDSAMP RSPSDYADRR SQREPQFYEE SDHINYRDSN
RRSHRHSKEY IVDNEDAESR DEYERQRREE EYQARYRSDP NLARYPVKPQ PYEEQMRIHA
EVSRARHERR HSDVSLANAE LEDSRISMLR MERPSRQRSV SERRAAMENQ RSYSMERTRE
AQGPSSYPQR TTNHSPPTPR RSPIPIDRPD MRRTDSLRKQ QHLDPSSAVR KTKREKMETM
LRNDSLSSDQ SESVRPPPPK PHKSKKGGKM RQVSLSSSEE ELASTPEYTS CDDVEIESES
VSEKGDMDYN WLDHTSWHSS EASPMSLHPV TWQPSKDGDR LIGRILLNKR LKDGSVPRDS
GAMLGLKVVG GKMTESGRLC AFITKVKKGS LADTVGHLRP GDEVLEWNGR LLQGATFEEV
YNIILESKPE PQVELVVSRP IGDIPRIPDS THAQLESSSS SFESQKMDRP SISVTSPMSP
GMLRDVPQFL SGQLSIKLWF DKVGHQLIVT ILGAKDLPSR EDGRPRNPYV KIYFLPDRSD
KNKRRTKTVK KTLEPKWNQT FIYSPVHRRE FRERMLEITL WDQARVREEE SEFLGEILIE
LETALLDDEP HWYKLQTHDV SSLPLPHPSP YMPRRQLHGE SPTRRLQRSK RISDSEVSDY
DCDDGIGVVS DYRHNGRDLQ SSTLSVPEQV MSSNYCSPSG SPHRVDVIGR TRSWSPSVPP
PQSRNVEQGL RGTRSTTGHY NTISRMDRHR VMDDHYSPDR DRDCEAADRQ PYHRSRSTEQ
RPLLERTTTR SRSTERPDTN LMRSMPSLMT GRSAPPSPAL SRSHPRTGSV QTSPSSTPVA
GRRGRQLPQL PPKGTLERKE VDSTRRRHAG AMDIEERNRQ MKINKYKQVA GSDPRLEQDY
QSKYRSGWDP HRGADNISTK SSDSDVSDIS AVSRTSSASR FSSTSYMSVQ SERPRGNKKI
SVFTSKMQSR QMGISGKNMT KSTSISGDMC SLEKNDGSQS DTAVCALGTS SKKRRSSIGA
KMVAIVGLSR KSRSASQLSQ TEASGKKLRS TVQRSTETGL AVEMRNWMTR QASRESTDGS
MNSYSSEGNL IFPGVRLASD SQFSDFLDGL GPAQLVGRQT LATPAMGDIQ VGMMDKKGQL
EVEIIRARGL VVKPGSKTLP APYVKVYLLD NGVCIAKKKT KVARKTLEPL YQQLLSFEES
PQGKVLQIIV WGDYGRMDHK SFMGVAQILL DELELSNMVI GWFKLFPPSS LVDPTLAPLT
RRASQSSLES STGPSYSRS
//
