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Database: UniProt
Entry: A0A0D2I3Z6_9EURO
LinkDB: A0A0D2I3Z6_9EURO
Original site: A0A0D2I3Z6_9EURO 
ID   A0A0D2I3Z6_9EURO        Unreviewed;      3183 AA.
AC   A0A0D2I3Z6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Vacuolar protein sorting-associated protein {ECO:0000256|PIRNR:PIRNR037235};
GN   ORFNames=Z520_12292 {ECO:0000313|EMBL:KIX92021.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX92021.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX92021.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX92021.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates the transfer of lipids between membranes at
CC       organelle contact sites. May play a role in mitochondrial lipid
CC       homeostasis. {ECO:0000256|PIRNR:PIRNR037235}.
CC   -!- SIMILARITY: Belongs to the VPS13 family.
CC       {ECO:0000256|ARBA:ARBA00006545, ECO:0000256|PIRNR:PIRNR037235}.
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DR   EMBL; KN848113; KIX92021.1; -; Genomic_DNA.
DR   RefSeq; XP_016626144.1; XM_016782778.1.
DR   STRING; 1442371.A0A0D2I3Z6; -.
DR   GeneID; 27718038; -.
DR   VEuPathDB; FungiDB:Z520_12292; -.
DR   OrthoDB; 199953at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-UniRule.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0045053; P:protein retention in Golgi apparatus; IEA:UniProtKB-UniRule.
DR   InterPro; IPR026847; VPS13.
DR   InterPro; IPR026854; VPS13-like_N.
DR   InterPro; IPR049424; VPS13_C.
DR   InterPro; IPR031645; VPS13_DH-like.
DR   InterPro; IPR031646; VPS13_extend_chorein.
DR   InterPro; IPR017148; VPS13_fungi.
DR   InterPro; IPR031642; VPS13_mid_RBG.
DR   InterPro; IPR009543; VPS13_VAB.
DR   PANTHER; PTHR16166:SF93; INTERMEMBRANE LIPID TRANSFER PROTEIN VPS13; 1.
DR   PANTHER; PTHR16166; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS13; 1.
DR   Pfam; PF12624; Chorein_N; 1.
DR   Pfam; PF21679; VPS13_C; 1.
DR   Pfam; PF16909; VPS13_DH-like; 1.
DR   Pfam; PF16908; VPS13_ext_chorein; 1.
DR   Pfam; PF16910; VPS13_mid_rpt; 1.
DR   Pfam; PF06650; VPS13_VAB; 1.
DR   PIRSF; PIRSF037235; VPS13_fungi; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|PIRNR:PIRNR037235};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW   ECO:0000256|PIRNR:PIRNR037235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037235}.
FT   DOMAIN          2..115
FT                   /note="Chorein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12624"
FT   DOMAIN          139..376
FT                   /note="Vacuolar protein sorting-associated protein 13
FT                   extended chorein"
FT                   /evidence="ECO:0000259|Pfam:PF16908"
FT   DOMAIN          601..837
FT                   /note="VPS13 middle RBG modules"
FT                   /evidence="ECO:0000259|Pfam:PF16910"
FT   DOMAIN          1953..2528
FT                   /note="Vacuolar protein sorting-associated protein 13 VPS13
FT                   adaptor binding"
FT                   /evidence="ECO:0000259|Pfam:PF06650"
FT   DOMAIN          2780..2955
FT                   /note="Vacuolar protein sorting-associated protein 13 DH-
FT                   like"
FT                   /evidence="ECO:0000259|Pfam:PF16909"
FT   DOMAIN          3052..3157
FT                   /note="Intermembrane lipid transfer protein VPS13 C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21679"
FT   REGION          561..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1052..1079
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1368..1415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1556..1589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1715..1782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..901
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1383..1406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1574..1589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1723..1740
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1741..1782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3183 AA;  357624 MW;  4A82E86E77BEA0C8 CRC64;
     MLESLVANLL NRFLGMYVKN FDPKQLNVGI WSGDVKLRNL ALRREALDQL HLPINVVEGH
     LGELTLSIPW SNLRGKPVKV NIEDVFLLAA PKEEDDYDPV EEDKRAVAVK LEKLESAELL
     KERNTEAMSP EEQQKSQSFT QSFVTAIVDN LQVSIKNVHI RYEDSIATPD HPFAVGLTLK
     EMSAVSTDAD WQPTFIQSTS ETTHKLAVLN SLALYWNSDA DLFGTGKGGD VGAEAQEIDK
     DELLRRFREG IEDTSHSQYL LKPVSGRAGI EMDKTGKTDK AKTKARLLFQ ELGFIIDDEQ
     YRDALMLVDL MHYFVRHHEY KKDAPKESPK ENPRAWLKFA GNAVLTKIHD RNRKWTWEYF
     KERRDTRRRY IELFKKKKKE QKFTEQETKD LTQLEHDLSY EDLRFWRSLA RTQLRKENVG
     VKKPAQKQTW SSWIWGAKGQ AEQSSENDEE AGMTEQQRKE LYNAIDWDEK KAIAESVDMP
     RESVKLEVES SLRTGSFTLK RDPHGQETEV LKLVFDNFKA KALQRPDSFL AELALGGFRV
     YDGTTEGTLF PQIVKVKGVE NQPKDEVKQD GTEDLDDEAE SESAVAEKGE QEEDSLFHLV
     FENNPLDESA DTKVDLKLKS LEFIHNPKFV VEIVKFFKPP ERQMESIGAL LETAGATVEE
     IRQQTRAGLE FALEEHKTIN ANLDIHAPIF IIPESITEKS TLCMILDAGH VSLNSELVDK
     ETMRDIHGKQ KQKYTEEDYR QLEGLMYDKF HLKLESTQVL IGPGIEETRA QLEAEDDSQS
     MHIIDRINMA FLLENSIIPK APDITKVRIS GTLPVLHASI SDKKYKNIMR LIDVAIPKFD
     TAETEANGTA VESRPQKATE DQASKRKSVQ LLEAKDIPII DHDSDSEDAP TKKDSRNKPE
     TPANIHQRNF EINFTVEKLQ ASLYKADPDG KKPDQLLVEL VAERFYFDFY LRPYDMVAQV
     LLRSLSVDDH IEEEPLPEFK QIISSKGFNA EEGKDLLNVK FVKVNPESPE FQSTYESIAT
     NLDVAMSTIN VIVTRRTLLT LLDFVLTTFT SPGDQQATQE DTDEPEERAD DPRPAEPQAD
     KIRIKAQLTS IALILNNDGV RLATLSLNSG DVGVFLDAGT MQVKARLGSL SLVDDINEGA
     PEDSPLRRLI AIEGDDLADF KYQTFDSSRK DYPGYDSGIY LRSGSIKVNF LEEPFRKIME
     FGVKFGKMQA IFNAARQAAA NQATQVQESA QKMHFDVIIK TPIVVFPRAM VEDRPRDLLT
     AYLGEIYANN KFVGVQGQKG GPLVNKLAAG IRHIRLTSEF HYSDGSSQEL EMIDKVDLDF
     KIRYLEHQAG IERPDLEIDG SMSPINLRVS HTQFKFLMEL SKTIPAAFAT DDESEEDVAE
     ELPSSTTESA KAAEPETTTS ESLAKPSYQG PELGTGEETW TKLNLVFKAP MIALELMLAD
     EDRPIENLEA ASLSKFSINE TNIKLRMISD GAMEAELVIH SFTVRDSRTK ETNKFRKIMS
     LINNDVQQQF MASLSITGGE ERHMIVMLTI DSPRVIVALD YIFALQAFAN TALQSDEPPP
     IAEVDDLTER SDPSLENDQG QMESGAQEVE SAGQSSMTIS FRLNVVDAQV ILIANPTISN
     TEAIVLGTKE VLVSKQNAMT LQVSKVGMFL CRMDRFETSR LRILDDFSIQ MSMDNRSQGK
     ESSLTSIHIG IEPLVLRLSL RDILLAMQIV SKASSTTAQP KMQEDTEPKK LKDVKASSKA
     PSTKRKSIAA TSTAAQRSKR SKSVSKSTKS GSQQQSSKSV VMSREEMVAQ IEGIRVILIG
     DMHELPLLDW SVKKFDVDVR DWSSSLTADT KIDTFINVYN FSKSAWEPLI EPWNLGFHMS
     KQLHPEVLSM ELYSHKNMEL TITSATIALA SKSFDFLSTD EDILSKPRVA DAPYRIRNYT
     GFDLSVWADE KSESAAAAKL TDGEEYAWRF EDATSMRESL SPEGNAGLVG VKLEGSGFDS
     VVRIPVIREG ETLYNLKPRK DGVQHRMLVE VRLGSDNVKY ITFRSPLLVE NKTQIPIEVG
     VYSPDDGHLL KIEKIAPGEG KPAPVGAAFV HSLVLRPDQG FGYGWSNERL FWKDLLRRQT
     RALTCESEGR DESPPFFFQM HASYDDKDPI TKIYPFMRIQ VSAPVEIQNL LPYDFKYRIY
     DKNTKKDWTN FLRKGGVSPV HVVELSHLLL LSVEVEDAPF KQSDFAIINS DTQEGFRREK
     VLQLKDERGA QLRLKLHYTN IKDSGGAFRV SVYSPYVLLN KTGLDMSVQS KAFLGSSTKA
     SSPQGARTSA GEGTALPMLY SYGSDDRKNR SLIKIGDSTW SKPQSFDAIG SSYEVVLPSA
     SGKSEMHVGV SVAEGEGKYS LTKVVTMAPR FVLKNKIGED IELREPGSSE VWKMKNNDLL
     PMYFMRQSPE KQLCMCFPGV NNQWSSPFNM ANVGMTHVKL AKHGQRQKLV RVEIILEDAT
     LFLHFSIETK HWPFSMRNES DTEFLFFQAN PNLGEDEEED KGSGWKPIRY RLPPRSIMPY
     AWDYPASKNK ELVLTAGGRE RYVKLAEIGN LIPIKLPPDD RGGPMKVIDI NIVADGPTQT
     LVLSNYKPSR SMYRQKTGMT TASQTSLNQG FEVKQIESEV NFKAELRLAG IGISLVNSKL
     KELMYVTFRE MDLKYGDSKL YQTLNFTVKW IQIDNQLYGG IFPILLYPSV VPKTGKEMEA
     HPIFHTMVTR VKDDSYGVLY IKYATLLLQQ ITVELDEDFI FAMLDFAKVP GASWSEEKEG
     KLCDESLDVP EPTREEQGQD VYFELLHLQP IQLDLSFVRT ERVNAEDNFV NSPLMFIVNV
     MTMSIGNVND APIRFNALML ENARISVPAL IANIQNHYTQ EALRQVHIIL GSADFLGNPV
     GLFNNISSGV ADIFYEPYQG LVMTDRPQEL GIGIAKGASS FVKKSVFGFS DSMAKFSGSI
     SKGLAAATMD KEFQDQRRMS KSRNRPKHAL YGVTAGGNAF AASMASGIGG LARHPLEGAE
     KEGALGFVKG VGKGFLGLAT KPAIGAFDLA SNVAEGVRNT TTVFDSEGLD RVRLTRFIGM
     DGIVRPYSQR EALGQFWLKT CDDGRYFNEE YIAHLELEGG DMMVVITYER ILMIRTKKLR
     MEWDIKLTDV QTISKERTGM SIGLKGGANG PFIPVADEGS RNWLYKQIAI AVNAFNDKYN
     AKG
//
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