ID A0A2Y9DVW4_TRIMA Unreviewed; 1692 AA.
AC A0A2Y9DVW4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Regulating synaptic membrane exocytosis protein 1 isoform X1 {ECO:0000313|RefSeq:XP_004381422.1};
GN Name=LOC101359991 {ECO:0000313|RefSeq:XP_004381422.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004381422.1};
RN [1] {ECO:0000313|RefSeq:XP_004381422.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_004381422.1; XM_004381365.1.
DR STRING; 127582.A0A2Y9DVW4; -.
DR GeneID; 101359991; -.
DR KEGG; tmu:101359991; -.
DR InParanoid; A0A2Y9DVW4; -.
DR OrthoDB; 2891597at2759; -.
DR Proteomes; UP000248480; 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 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; 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:SF18; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN 1; 1.
DR Pfam; PF00168; C2; 2.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
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 22..182
FT /note="RabBD"
FT /evidence="ECO:0000259|PROSITE:PS50916"
FT DOMAIN 110..170
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 605..691
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 742..865
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1538..1656
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1692 AA; 189259 MW; AEA2691D7949729E CRC64;
MSSAVGPRGP RPPTVPPPMQ ELPDLSHLTE EERNIIMAVM DRQKEEEEKE EAMLKCVVRD
MAKPAACKTP RNAENQPHQP SPRLHQQFES YKEQVRKIGE EARRYQGEHK DDAPTCGICH
KTKFADGCGH LCSYCRTKFC ARCGGRVSLR SNNEDKVVMW VCNLCRKQQE ILTKSGAWFF
GSGPQQPSQD GTLSDTASGA GSEVPREKKA RLQERSRSQT PLSTAAASCQ DTAAPSAQPD
RSKGAEPSQQ ALEPEQKQAS SRSRSEPPRE RKKTSGLSEQ NGKGALKSER KRVPKSSVQP
REGVVEERER KERRENRRLE KGRSQDYPDV PEKREEGKAP DDEKQRKEEE YQTRYRSDPN
LARYPVKPPP EEQQMRMHAR VSRARHERRH SDVALPHTEV GAALPESKPS KRAPAAARAS
PPDSPRAYSA ERTAEPRAPG AKQLTNHSPP APRHGPVPAE APEPKAQEPL RKQSRLDPSS
AVLIRKAKRE KVETMLRNDS LSSDQSESVR PSPPKPHRSK RGGKKRQMSV SSSEEEGVST
PEYTSCEDVE LESESVSEKG DLDYYWLDPA TWHSRETSPI SSHPVTWQPS KEGDRLIGRV
ILNKRTTMPK ESGALLGLKV VGGKMTDLGR LGAFITKVKK GSLADVVGHL RAGDEVLEWN
GKPLPGATNE EVYNIILESK SEPQVEIIVS RPIGDIPRIP ESSHPPLESS SSSFESQKME
RPSISVISPT SPGALKDAPQ VLPGQLSVKL WYDKVGHQLI VNVLQATDLP PRVDGRPRNP
YVKMYFLPDR SDKSKRRTKT VKKVLEPKWN QTFVYSHVHR RDFRERMLEI TVWDQPRVQE
EESEFLGEIL IELETALLDD EPHWYKLQTH DESSLPLPQP SPFMPRRHAH GESSSKKLQR
SQRISDSDIS DYEVDDGIGV VPPVGYRSSA RESKSTTLTV PEQQRTTHHR SRSVSPHRGD
DQGRPRSRLP NVPLQRSLDE IHPTRRSRSP TRHHDASRSP VDHRSRDVDS QYLSEQDSEL
LMLPRAKRGR SAECLHTTRH LVRHYKTLPL KMPLLENGSH SNIYSSILCV RTKAKLVTRQ
NMSLHPECFN SRILRNTDEL LVSELQPSLD RARSASTNCL RPDTSLRSPE RERGRWSPSL
DRRRPPSPRI QIQHASPEND RHSRKSERSS IQKQTRKGTA SDAERVLPPC LSRRGHAAPR
ATDQPVIRGK HPTRSRSSEH SSVRTLCSMH HLAPGGSAPP SPLLTRMHRQ GSPTQSPPAD
TSFSNRRGRQ LPQVPVRSGS IEQASLVVEE RTRQMKMKMH RFKQTTGSGS SQELDREQYS
KYNIHKDQYR SCDNVSAKSS DSDVSDVSAI SRTSSASRLS STSFMSEQSE RPRGRISSFT
PKMQGRRMGT SGRAITKSTS VSGEMYTLEH NDGSQSDTAV GTVGVGGKKR RSSLSAKVVA
IVSRRSRSTS QLSHTESGHK KLKSTIQRST ETGMAAEMRK MVRQPSREST DGSINSYSSE
GNLIFPGVRL GADSQFSDFL DGLGPAQLVG RQTLATPAMG DIQIGMEDKK GQLEVEVIRA
RSLTQKPGSK STPAPYVKVY LLENGACIAK KKTRIARKTL DPLYQQSLVF DESPQGKVLQ
VIVWGDYGRM DHKCFMGVAQ ILLEELDLSS MVIGWYKLFP PSSLVDPTLT PLTRRASQSS
LESSTGPPCI RS
//
