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Database: UniProt
Entry: A0A0V0YC01_TRIPS
LinkDB: A0A0V0YC01_TRIPS
Original site: A0A0V0YC01_TRIPS 
ID   A0A0V0YC01_TRIPS        Unreviewed;       710 AA.
AC   A0A0V0YC01;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Double C2-like domain-containing protein beta {ECO:0000313|EMBL:KRX97273.1};
DE   Flags: Fragment;
GN   Name=Doc2b {ECO:0000313|EMBL:KRX97273.1};
GN   ORFNames=T4E_3145 {ECO:0000313|EMBL:KRX97273.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX97273.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX97273.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX97273.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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:KRX97273.1}.
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DR   EMBL; JYDU01000033; KRX97273.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0YC01; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
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; cd04035; C2A_Rabphilin_Doc2; 1.
DR   CDD; cd15746; FYVE_RP3A_like; 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; IPR030541; FYVE_RBF-1.
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:SF4; RAB EFFECTOR NOC2; 1.
DR   PANTHER; PTHR45729; RABPHILIN, ISOFORM A; 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   Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
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          43..163
FT                   /note="RabBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50916"
FT   DOMAIN          91..151
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          437..559
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          575..704
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          203..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..274
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..289
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX97273.1"
SQ   SEQUENCE   710 AA;  80830 MW;  CF9598D74A95DF02 CRC64;
     LKYIRKSTKM PGKQNSWICP SDRFLILRSQ LSAGWSVWSD TQRADKSTIS DNEMQQIKDV
     LARAEHIEEN EQRRIGKLVE RLDRMKKMAA GNGINQCMLC GAKFGMIGTR SFASFCHDCN
     KYVCQKNCGL ETLDSNGQTI YLCKLCSETR EMWKKSGAWF YRGIPNFIKD TGLRSKSNDV
     SLSNTDDRGG FDTVSLTSMD SRCSKESLPS WSGKAKHAKR LLPTPPSESH IRPSQPRWAI
     ISQSIQSFDK CVDSSSEEEE EDSKDGQETE EDIEQNNENL NRRLFLDDSD TPYSRQSSCL
     SELDNSKPLS ELESPELKRL SEEEKRTARD VKEEETEIYD SKSSTSEVAV HSDSPVQSCT
     NSSSRYTMEI AEDSDASMAL STSVHDQATS EVNRITDQLA ECSMSKPYAT KNLQHSDSAK
     SFDSSLYDSS PDNDITNFGS LEYSLLYDET EEMLIVTIFQ ASNLPAMDSN GFSDPYVKLH
     LLPLANKSTK LRTSTKWKTL NPRWNERLIY YGMSKDDLRK KTLRLMVLDQ DRIGSDFLGE
     TRAPLKRLQS GKEKYFNVYL EKQMPVEKCD EFTEERGKIL LALCYDLQNK LLAVEVVRCV
     ELVGMDSTGY SDPTLKPGTL KSYHVKTEVK KKTLNPEYNR VFQFPVSYDE LAKKSLDVEV
     WDKDVGKLDD FIGSVTLSAN AKSDRLKHWI ECIQNPNKRI KKWHKLTGKV
//
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