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Database: UniProt
Entry: A0A0D2F9E6_9EURO
LinkDB: A0A0D2F9E6_9EURO
Original site: A0A0D2F9E6_9EURO 
ID   A0A0D2F9E6_9EURO        Unreviewed;      3181 AA.
AC   A0A0D2F9E6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Vacuolar protein sorting-associated protein {ECO:0000256|PIRNR:PIRNR037235};
GN   ORFNames=PV04_10336 {ECO:0000313|EMBL:KIW63500.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW63500.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW63500.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW63500.1,
RC   ECO:0000313|Proteomes:UP000054266};
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 Capronia semiimmersa CBS27337.";
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; KN846962; KIW63500.1; -; Genomic_DNA.
DR   STRING; 5601.A0A0D2F9E6; -.
DR   HOGENOM; CLU_000135_0_0_1; -.
DR   OrthoDB; 199953at2759; -.
DR   Proteomes; UP000054266; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Golgi apparatus {ECO:0000256|PIRNR:PIRNR037235};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW   ECO:0000256|PIRNR:PIRNR037235};
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          597..833
FT                   /note="VPS13 middle RBG modules"
FT                   /evidence="ECO:0000259|Pfam:PF16910"
FT   DOMAIN          1950..2526
FT                   /note="Vacuolar protein sorting-associated protein 13 VPS13
FT                   adaptor binding"
FT                   /evidence="ECO:0000259|Pfam:PF06650"
FT   DOMAIN          2778..2953
FT                   /note="Vacuolar protein sorting-associated protein 13 DH-
FT                   like"
FT                   /evidence="ECO:0000259|Pfam:PF16909"
FT   DOMAIN          3050..3156
FT                   /note="Intermembrane lipid transfer protein VPS13 C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21679"
FT   REGION          417..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1048..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1368..1412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1558..1584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1711..1775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          97..134
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        438..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..584
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..860
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1383..1403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1737..1775
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3181 AA;  357058 MW;  3B98084CF029BEA4 CRC64;
     MLEGLVANLL NRFLGMYVKN FDPKQLNVGI WSGDVKLRNL ELRREALDQL RLPINVVEGR
     LGELTLSIPW SNLRGKPVRV NIEDVFLLAA PKEEDDYNAE EEEKRAVAVK LEKLESAELL
     KEQNTEAMSA EEQQKSQSFT QSFVTAIVDN LQVSIKNVHV RYEDSIATPG HAFAVGLTLK
     EMSAVSTDAD WQPTFIQSTS GTTHKLAVLN SLALYWNSDA ELFGTGKGGD VGAEAQEIDK
     DELVRRFRQG IEDTAGHQYL LKPVSGRAGI ELDKTGHVDK PKTKARLLFQ ELGFIIDEDQ
     YRDALMLVDL MHYFVRHHEY KKDSPKETPK ENPRAWVKFA GQAVLNKIHE RNRKWTWDYF
     KERRDTRRKY IELFKKKKKE QQFTEQETKD MAQLEHDLTY EDLRFWRSLA RSQLRRENVG
     VKKPPQKQTW SSWVWGSKPE EKQEDDDAGM TDEQRKELYQ AIDWDEKKAL ADAVDLPRET
     VKLQVESSLR TGSFTLKRDP HGQSNDILKL VFDNFKLKAL QRPDSFLADV ALGGFRVYDG
     TTEGTLFPQI VKVKGAEEQP KEDVKQDDSQ TLDDEDDSEA GTTEKPEEDD SLFHLVFENN
     PLDESADTKV DLRLKSLEFI HNPKFVVEIV KFFKPPERQM ESIGALLETA GASIEEIRQQ
     TRAGLEFALE EHKTINANLD IHAPILIIPE SITEKSTLCM ILDAGHVSLN SELVDKDTMR
     DIHSKQKQKY TEEDHKQLEG LMYDKFHVKL ESTQVLIGPG IEATRAQLEA RVDSQDMHII
     DRINMAFLLE NSIIPKAPDV TKIRISGSLP VLHASISDKK YKNLMRLIDV AIPKFDSAEP
     EAPEDAVESR PPHAFEDQSA SKRKSVQLLE AKDLPIIEHD SDTEDSPSEE TNQTDTPANI
     HQRNFEIKFT VEKLQASLYK ADPDGKKPDQ LLVELVAEHF YFDFYLRPYD MVAEVLLRSL
     SVDDHIEKQP LPEFKQIISS KGFKADDGKD LLNVKFVKVN PASPEFISTY EGIATNLDVS
     VSTINVVVTR RTLLTLLDFV LTTFASPGGQ QQPIEGKHDE DEPEAIQEAP QQSAPADKIR
     IKAELTSIAL ILNNDGVRLA TLSLNSGDVG VFLDAGTIQI KARLGSLSLV DDINEGAPED
     SPLRRLIAIE GDDLADFKYQ TFDSTRRDYP GYDSGIYLRS GSIKINFMEE PFRKIMEFGV
     KFGRMQAIFN AARQAAADQA QQVQESAQRM HFDVVIKTPI VVFPSVMVDD RPRDVLTAYL
     GEIYASNKFV RVQGQKDGPL VNKLTAGIRH IRLTSEFHYD DGSAQELEMI DKVDLTFKIR
     YLEHQAGVER PDLEIEGNMS PINLRVSQTQ VKFLTDLSKT IPAAFAMEDE SEEDIAEELP
     VSTAESATVS DPNTTTSPAP ATPSYQAPEL GTGDETWTKV NLVFKAPMVS LELMLADEGE
     PIESLEAASL SKFAINETSV KMRIMSDGAM EAELVVHSFT IRDSRTKETN KFRKIMSLIN
     NDVQQQFMAN VSISGGADRH MIVMLTIDSP RVIVALDYVF ALQAFASTAL QSAEPPPVAE
     IEDLTESGEQ SPVEELAEAG DAAGEVESEA KSSMSVSFRV NVVDAQVIFI ANPTISNTEA
     IVLGTKEVLL SQQNATTLQI TKIGMFLCRM DRFETSRLRI LDDFSASMSM EKRGQGKDSG
     LTSIHIGVEP LVLRLSLRDI LLAMQIVSKA SSTTPQPKMQ EDTEPKKLKD VKASSKAPST
     IRKSIAGQST MAQRSKRSKS ISKTTKSSPQ HEQGRQWVVL SREEMIAQID GIRVILIGDM
     HELPMLDWSV KKFDVEVHDW SSSLTADTRI DTFINVYNFS KSAWEPLIEP WNLGFHMAKE
     LQPEVLSMEL YSHKNMELTV TTATIALASK SFNFLSTDED ILSKPRVADA PYRIRNYTGF
     DLSVWADEKS DSAAAAKLTD GEEYAWRFQD TTSMRESLSP EGNAGLVGVK LEGSGFDSVT
     RIPVIREGET LYNLKPKKDG VQHRMLVEVA LGTDNVKYIT FRSPLLVENK TQIPIEVGVF
     SPEEGHLLKI EKIAPGEARP APVGAAFVHS LVLRPDQGFG YGWSNERLFW KDLLRRPTRT
     ITCESEGKDE SPAFFFQMHA SYDEKDPITK VYPYMRIQIS APVEIQNLLP YDFKYRIYDK
     NTKKDWTNFL RKGGVSPVHV VELSHLLLLS VDVEDAPFKQ SDFAIINSNT QEEFRREKVV
     QLKDERGAQL RLKLHYTNIK NGGGAFRVSV FSPYVLLNKT GLDMSVQSKA FFGSSSKSSS
     PHGTRSSAGE GKALPMLYSY GTDDRKNRSL LRIGDSAWSK PQSFDAIGSS YEVVLPAASG
     KSELHAGVSV AEGEGKYSLT KVVTIAPRFV LKNKIGEDIE LREPGSSEVW KMQNNELRPV
     YFMRQSPEKQ LCLCFPGINN QWSSPFNMDN VGMTHVKLAK HGQRQRLVRV ETILEDATLF
     LHFSIETKHW PFSMRNESDT EFLFFQANPN VAEDEEEDKG SGWKPIRYRL PARSIMPYAW
     DYPASKNKEL VLIARGKERY VKLAEIGNLI PIKLPPDDRG GPAKAIDVNI VADGPTQTLV
     LSNYQPSKSL YRQKTGHTVA SQTSLNQGFE VKQIESEVNF KAELRLAGFG ISLVNSKLKE
     LMYITFREME LKYGDSKLYQ TVNFTVKWIQ IDNQLYGGIF PILLYPSVVP KTGKELETHP
     IFHAMVTRVK DDSYGVLYIK YATLLLQQIT VELDEDFIFA LLDFVKVPGA SWSEEKEGKL
     CDESVDVPEP TREQQGEDVY FELLHLQPIQ LDLSFVRTER VNAEDNFVNS PLMFFVNVMT
     MSIGNVNDAP IRFNALLLEN ARISVPALMT NIQNHYTQEA LRQVHIILGS ADFLGNPVGL
     FNNISSGVAD IFYEPYQGLV MTDRPQELGI GIAKGASSFV KKSVFGFSDS MAKFSGSISK
     GLAAATMDKE FQDQRRMAKN RNRPKHALYG VTAGGSAFAA SMASGIGGLA RHPLEGAEKE
     GAFGFVKGVG KGMLGLATKP AIGAFDLASN VAEGVRNTTT VFDAEGLDRV RLTRFIGMDG
     IVRPYSQREA LGQFWLKTCN DGQFFNEEYI AHLELEGRDM MVIITYDRIL MLRTKKLRME
     WDVKLTDIKT ISKERTGMSI GLKGGANGPF IPVTDEGSRN WLYRQIAIAV NAFNDRYNAK
     G
//
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