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Database: UniProt
Entry: A0A2Y9PGR1_DELLE
LinkDB: A0A2Y9PGR1_DELLE
Original site: A0A2Y9PGR1_DELLE 
ID   A0A2Y9PGR1_DELLE        Unreviewed;      1481 AA.
AC   A0A2Y9PGR1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Regulating synaptic membrane exocytosis protein 1 isoform X17 {ECO:0000313|RefSeq:XP_022446124.1};
GN   Name=RIMS1 {ECO:0000313|RefSeq:XP_022446124.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022446124.1};
RN   [1] {ECO:0000313|RefSeq:XP_022446124.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022446124.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_022446124.1; XM_022590416.2.
DR   Proteomes; UP000248483; 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; 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:SF18; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 1; 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; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483};
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          59..119
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          553..639
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          690..813
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          1327..1445
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          131..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          871..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1123..1181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1234..1263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..412
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..678
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..858
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..913
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        927..948
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1007
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1009..1045
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1234..1249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1481 AA;  164678 MW;  2DCAE355629D24CD CRC64;
     MRPRCVVRDM VKPAACKTPR NVEHQPHQPS PRLHQQFESY KEQVRKIGEE ARRYQGEHKD
     DAPTCGICHK TKFADGCGHL CSYCSTKFCA RCGGRVSLRS NNEDKVVMWV CNLCRKQQEI
     LTKSGAWFFG SGPQQPSQDG TLSDTATGAG SEAPREKKSR LQERSRSQTP LSTATASPQD
     QVPHSVPPDR RKGAEPSQQA GRPEQKQASF RSRSEPPRDR KKTPGLAEQN GKGAPKGERK
     RAPRSSGQPT EGLTEERERK ERRESRRLEK GRSQDYPDVP EKRENGPAVE AEKQRKEEEY
     QTRYRSDPNL ARYPVKPPPE EQQMRMHARM SRARHERRHS DVALPRTEAA AGPEGRPGPR
     APNAARGSPP ASPRAYSAER TAEARAPGAP PLAEPSPPAP RPGPGPADAP EPRAPEPLRK
     QSRLDPGAAV LVRKAKREKV ETMLRNDSLS SDQSESVRPS PPKPHRAKRG GKRRQMSVSS
     SEEEGVSTPE YTSCEDVELE SESVSEKGDL DYYWLDPATW HSRETSPISS HPVTWQPSKE
     GDRLIGRVIL NKRTTMPKES GALLGLKVVG GKMTDVGRLG AFITKVKKGS LADVVGHLRA
     GDEVLEWNGK PLPGATNEEV YNIILESKSE PQVEIIVSRP IGDIPRIPES SHPPLESSSS
     SFESQKMERP SISVISPTSP GALKDAPQVL PGQLSVKLWY DKVGHQLIVN VLQATDLPPR
     VDGRPRNPYV KMYFLPDRSD KSKRRTKTVK KVLEPKWNQT FVYSHVHRRD FRERMLEITV
     WDQPRVQEEE SEFLGEILIE LETALLDDEP HWYKLQTHDE SSLPLPQPSP FMPRRHVHGE
     SASKKLQRSQ RISDSDISDY EVDDAIGVVP PVGYRSGARE SKPSTLTVPE QQRTTHHRSR
     SVSPHRGDDQ GRPRSRLPNV PLQRSLDEIH PTRRSRSPTR HHDVSCSPVG HRPGDVDSQC
     LSEQDSELLM LPRAKRGRSA ECLHTTSDLQ PSLDRARSAS TNCLRPDASL HSPERERHSR
     KSERSSTQKQ TRKGTASDAE RVHRQASPTR SPPADTAFGS PRGRQLPQVP GRSGSAEQAS
     LVVEERTRQM KMKVHRFKQT TGSGSSRELD REQYSKYNVH TDQYRSCDSV SARSSDSDVS
     DVSAISRTSS TSFLSEQSER PRGRTSSFTP KMQGRRMGTS GRAITKSTSV SGEMYTLEHN
     DGSQSDTAVG TVGTGGKKRR SSLSAKVVAI VTRRSRSTSQ LSQTESGHKK LKSTIQRSTE
     TGMAAEMRKM VRQPSRESTD GSINSYSSEG NLIFPGVRLG VDSQFSDFLD GLGPAQLVGR
     QTLATPAMGD IQIGMEDKKG QLEVEVIRAR SLTQKPGSKS TPAPYVKVYL LENGACIAKK
     KTRIARKTLD PLYQQSLVFD ESPQGKVLQV IVWGDYGRMD HKCFMGVAQI LLEELDLSSM
     VIGWYKLFPP SSLVEPTLTP LTRRASQSSL ESSTGPPCIR S
//
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