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Database: UniProt
Entry: A0A158PPR5_ANISI
LinkDB: A0A158PPR5_ANISI
Original site: A0A158PPR5_ANISI 
ID   A0A158PPR5_ANISI        Unreviewed;      1903 AA.
AC   A0A158PPR5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   08-NOV-2023, entry version 27.
DE   SubName: Full=Receptor-mediated endocytosis protein 6 (inferred by orthology to a C. elegans protein) {ECO:0000313|WBParaSite:ASIM_0001531801-mRNA-1};
GN   ORFNames=ASIM_LOCUS14728 {ECO:0000313|EMBL:VDK53186.1};
OS   Anisakis simplex (Herring worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC   Anisakis simplex complex.
OX   NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001531801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ASIM_0001531801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK53186.1, ECO:0000313|Proteomes:UP000267096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the GAPVD1 family.
CC       {ECO:0000256|ARBA:ARBA00008489}.
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DR   EMBL; UYRR01031898; VDK53186.1; -; Genomic_DNA.
DR   WBParaSite; ASIM_0001531801-mRNA-1; ASIM_0001531801-mRNA-1; ASIM_0001531801.
DR   Proteomes; UP000036680; Unplaced.
DR   Proteomes; UP000267096; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR   InterPro; IPR041545; DUF5601.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR003123; VPS9.
DR   InterPro; IPR045046; Vps9-like.
DR   InterPro; IPR037191; VPS9_dom_sf.
DR   PANTHER; PTHR23101:SF25; GTPASE-ACTIVATING PROTEIN AND VPS9 DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR23101; RAB GDP/GTP EXCHANGE FACTOR; 1.
DR   Pfam; PF18151; DUF5601; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   Pfam; PF02204; VPS9; 1.
DR   SMART; SM00167; VPS9; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF109993; VPS9 domain; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS51205; VPS9; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267096}.
FT   DOMAIN          155..301
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   DOMAIN          1533..1687
FT                   /note="VPS9"
FT                   /evidence="ECO:0000259|PROSITE:PS51205"
FT   REGION          389..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..968
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1062..1115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          19..53
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        395..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..913
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        951..968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1072..1090
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1091..1109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1903 AA;  212517 MW;  5FB9C45237674DF7 CRC64;
     MDMCNWQLNN SLSILCERLR SEKLLVASEL ENIQRLNEQI DEEQLLLAQL SWIVNRQQDI
     LNRLVNSHPS VLPENSCLLN AQLDSADFIE AYQRIDAHHY SSLTSILNTL YKSPKSVAEL
     LNASDQIVKE SEESNEGFVS CIFSFLYGCC VFPNDERYLL EVLSYLIDMQ LSSNSDPRRV
     LRKGNAAFCR LYRLFSEGLF IDIFLTAALH DPVMYVLSQD DIFLDIDPSK SAIRFPPEER
     RRRFGEDENS LSYLQRLSAH RKVIESKLIA ISTRFVQGIT EAMSCFPQSL SWLVKELYST
     LIDRNKLTTE QGSMAQIVHR VLESSGESLN ELFSKNTFDS HQCEQHLRRS FVANFSELNC
     FHAILRSSAI ERITDTNIRR DIRNLIRRMP SRFDAPNSPQ RNIDTKNESR MSPPISNKSD
     GNAQNSTLSP TSSRSNKLRT FADRVQTVAH KGQLRLRSQH SSQQDSNGSH PGAASNVEVL
     IFALGDNSEP LGLCSEEKFM ESLRQPLSIR KHKTSDGASE KRTRFLDSES IGMSDRVTDA
     GSEDEEEGAS LSSSIEGNAE DALEDDAEDV SSTLPDNFSD VGLISANVSG RGSPSISGPP
     SVSGRDTPQS SHTDAAVQQD TSNANANNTT RTRHHLHRSN MPNLPLSVRR ENSEGLEDKF
     GKFGLPQQDN KHRYRDDTHS LVSDSWSTDV QPSDTEGIMT DTRHEAISNL PANIQQLLQP
     PNNDTNNTHQ IPIVSEETAP SRPLSAVTNR MTNRLPTSTT ANNNAATANI ASNTTANQAG
     AASSSSLGIL MNSEDRSDTW SVDAMASDSE ADNMLVHNRN DDLLLINDDD STDQRIDTAS
     GTSGGDTPLL MSTQSETSLA SGVISAATQS KHLNPSKNVT TDSLNEQIHR GNIDSSTNDP
     ISNNSNRSHQ QQAKKKVPPV DVSVFDEIPS NSALPPNVPS IGEVAANGNS RERLRRQSSG
     SSFYSKSDID SEFSKDLNED ALSTLLAEYV PMSSSYNPTS NIMDLITTNA NSHTTSTSPA
     ASILARAGSF CNDDIDNQSI SQQRDHSLSP INNTFPFNVT KQRKDVSEMD RVGELSQSNA
     CCPHSSDVHN DTKLANSDEK SEDGDKSTSK NVDVNTNAIS GGIQTAATAN TSGFARKKIN
     IFQGLQKVGE SLKMRKGMAV SSLKQSLSQA TTMNELASVD ANSNPSMCVS NDKPNTFKRD
     TQQDITGRKR LTGSHSMGEL GCLREKNESN EHTANAILDK YKGKHAIVID YNNSPDNLER
     VSNQLHPAQQ CISVLSSSSS LSYLPYYDAN NVTQCRAFID AKRKLRLVLS SIGSSSLPDL
     SNMTISEHST VDYSLSSANQ INKRGECNDA QYLKNFLQIL LAESINGQEK TLSAQIREVL
     RCITVFSDKE IRKLLRTLKD EHRKRTAYVL YLQQSRLTLL QYRSYLEKLL NRVQREKSLT
     VECLVEVLVR FYLQQRDMYV RRFINDFQLL KAQDERTDAV ERALTMLYER MPNEAMWKDA
     DKEMLAYARK SVERSIMAQI HLIAFYPNGE ADQCRDSVFH KSLRKLAQII TPDHAELRIP
     QRFHGECPWP SAQAEISIIN AYKSPRDKIA CVVRCCETIQ NLIFLAPQRG TASADDITPL
     LVYILIQANP QALLSNIQYI NGFYGNRLEG AEAYWEFGVE NLEESSYVSC MNSALERNYQ
     CFADGTVNTS ILMSEMESDE SGSRNVLLGT IDEHLVRMRD HIKVVLGKQR SKVYFSYFKE
     WLRGHKSQEE FNGLGLAMMP TDQKFVHSDF FVTMKKLCDM QHKEDNAVRI FDDNRLTKQQ
     KDLNASAQGV SNDQAIKKPR LISDIEYVDT RQSTAIVPSI PTEYNAMMEG LSEVHPFSGW
     LPSKGQIKGR MLLAVWEHGI ESITDDCINP LLVVIRVSFI LSF
//
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