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Database: UniProt
Entry: A0A2T7PE60_POMCA
LinkDB: A0A2T7PE60_POMCA
Original site: A0A2T7PE60_POMCA 
ID   A0A2T7PE60_POMCA        Unreviewed;       606 AA.
AC   A0A2T7PE60;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Rabphilin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C0Q70_07131 {ECO:0000313|EMBL:PVD31713.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD31713.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD31713.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD31713.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD31713.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PVD31713.1}.
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DR   EMBL; PZQS01000004; PVD31713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7PE60; -.
DR   STRING; 400727.A0A2T7PE60; -.
DR   EnsemblMetazoa; XM_025236366.1; XP_025092151.1; LOC112562831.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg4.
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:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd04035; C2A_Rabphilin_Doc2; 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; IPR010911; Rab_BD.
DR   InterPro; IPR043566; Rabphilin/DOC2/Noc2.
DR   InterPro; IPR047022; Rabphilin_Doc2_C2A.
DR   InterPro; IPR001565; Synaptotagmin.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45729; RABPHILIN, ISOFORM A; 1.
DR   PANTHER; PTHR45729:SF6; RABPHILIN-1; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF02318; FYVE_2; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50004; C2; 2.
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:UP000245119};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          41..158
FT                   /note="RabBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50916"
FT   DOMAIN          89..146
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          361..482
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          499..606
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          170..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  68104 MW;  51D17E14F5EEF864 CRC64;
     MGEFGSSGSL DRWVCPNDRQ LALRAKLGTG WSVHTNRLAS FQRGENLSLE EQEQIMRVIN
     RAEYIDHVEQ ERIGRLVEKL DNMKKNAIGN GSTQCILCGD EFGLLGASPT YCDDCKKAVC
     SKCGVDTFSS ARQPLWLCKI CAETREVWKR SGAWFFKGLP KYTLPEKKLE GGKHSTRMKP
     QLRGSVRGRP GSIRDSNYTW HRARGSSSTG TASYGESSEQ ESSDSSEDEI SISRHKSRKN
     HESESDNISI GSARSSHYDH YTRTERKASV TSTSYGGGHV SATESSRGDD LHDETDSERS
     STYQFSRDGS HMSQEHFTPA VGEEHAEDID RAVNRYVKST KPANDECDEA QVSSPESDGT
     SLGSLEFSLL YDSANNALHC TIARAKNLKA MDSNGLSDPY VKLHLLPGAN KSTKLRTKTI
     HKTLNPEWNE SLTYYGITED DVLKKTLRLS VLDEDAFGFD FIGETRVPLK RLKPHQTKHF
     NVHLEKQLPL EKDDDLIAIR GKILLSLKYA TAKQSLLVRI IRCAELAAMD SNGYSDPYVK
     VYLKPDKDKK SKFKTTVKKR TLNPEYNEEF TYDIKHNELA KKTLEITVWD KDIGKANDFI
     GVTRSH
//
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