ID A0A0D1YP75_9PEZI Unreviewed; 3209 AA.
AC A0A0D1YP75;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Vacuolar protein sorting-associated protein {ECO:0000256|PIRNR:PIRNR037235};
GN ORFNames=PV09_06270 {ECO:0000313|EMBL:KIW02462.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW02462.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW02462.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW02462.1,
RC ECO:0000313|Proteomes:UP000053259};
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 Ochroconis gallopava CBS43764.";
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; KN847549; KIW02462.1; -; Genomic_DNA.
DR RefSeq; XP_016212331.1; XM_016359883.1.
DR STRING; 253628.A0A0D1YP75; -.
DR GeneID; 27314243; -.
DR VEuPathDB; FungiDB:PV09_06270; -.
DR HOGENOM; CLU_000135_0_0_1; -.
DR InParanoid; A0A0D1YP75; -.
DR OrthoDB; 199953at2759; -.
DR Proteomes; UP000053259; 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:UP000053259};
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..377
FT /note="Vacuolar protein sorting-associated protein 13
FT extended chorein"
FT /evidence="ECO:0000259|Pfam:PF16908"
FT DOMAIN 602..836
FT /note="VPS13 middle RBG modules"
FT /evidence="ECO:0000259|Pfam:PF16910"
FT DOMAIN 1979..2555
FT /note="Vacuolar protein sorting-associated protein 13 VPS13
FT adaptor binding"
FT /evidence="ECO:0000259|Pfam:PF06650"
FT DOMAIN 2802..2981
FT /note="Vacuolar protein sorting-associated protein 13 DH-
FT like"
FT /evidence="ECO:0000259|Pfam:PF16909"
FT DOMAIN 3078..3181
FT /note="Intermembrane lipid transfer protein VPS13 C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF21679"
FT REGION 568..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1575..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3209 AA; 361000 MW; F74C50469B666511 CRC64;
MLESLVANLL NRFLGMYVQN FDPKQLNVGI WSGDVALRNL ELRREALDQL KLPLNVVEGH
LGLLTLSIPW SNLRGKPVKI NIEEVYLLAA PRTDAEVDPA EEERRAHAVK MEKLDSAELL
RERNTEGMSQ EDQKKNQSFT SSLVTAIVDN VQITVKNIHI RYEDALSNPD HPFALGITLE
GFDAVSTDEN WVPTFIQSTS ATTHKLASLK SLAVYWDTDA KLLGSGSGSQ QGIDHDEFLE
KFKALTVKDE EGKTTDQHQF ILKPVTGRAG LEMDKTGKLE RPKVKAKLLF DELGFVIDDD
QYRDALMLVD LFHYFIRHQE YKKYQPKSKP LEDPQAWLRF AGQAVLDKIH ERNRRWSWAY
FKERRDDRIR YIELFKKKKK DEKLTTDEAT EMDRLEHKLT YEDLRFWRSL ARNQLRKENV
GVKKQPQKQT WSQWIWGGGQ REEAADDGQM SDQQRKELYE AINFDEKQSI AEAVELPKEY
VKMQVDLSLR TGSFTLKKEP HGAKTEILRL LFDSFKTQFL QRPGSFLAKV SLEGMRLYDG
TTKGSLFPQM ITIKGAPEIP DDSRIEELQE DDEEATKDGV GEDDRLAEPE SDPEDPFFQL
EFENNPLDGS ADTALNLKLK GMEFIYNPAF VVGVVQFFKP PERHMESIGA LMESAGKTVE
GIRAQTRAGL EFALEEHKTI NANFDITAPL IIVPDSVTRK SNICLIIDAG HASVKSELVD
KETLQDIQSK QREKLSDQDF RRLESLMYDK FKLDLTSTQV LIGTTIEETR AKLSNKESNF
HLVDKINVDF LIETCIVPKG TSLTKFRVSG HLPVLHASIS DQKYKSLMKV IDFAIPKFHD
DSPPKQDEGK SKSRASLQPS KTEDRRESFT FAAQRHEIVV EEESVSGEHE EFTDANEGRA
QPQVQIDQKN FELKFTVDKL QGSLFKADPD GKRGDQLLVE LVAEGFLLDF YQRPFDMAAE
VRLRTLAVVD HVEDEPLPEF KNIIESEKVA GEDLFKLRFV KVNQDSPEFL PKYEGIATNL
DVQVSTINFI VTRRTLLTLL DFVLLTFTNP EQPEQQPKPI ESESESAAEE QVQTSGPQDA
DKIRVKVDLK RIAVILNNDG IRLATLGLNT ANVSVFLMGK KMRIGAHLGD LQLIDDVNQG
VSEKSNLRRL VTIQGDELAQ FSYETYDDTA ESYPGYDTSI FLRAGSLKVN FVTEPFRKIM
DFGVKFGKMQ AIFNAARQAA ANQANQLQQK ASKMHFDVIV RTPIVVFPRM VVTDEPERDT
LTAELGEIYA SNSFVALDDS EAADQANQIV AGIRNVRLLS LFHYDGGESE ELQMIDKLDL
KFKINMVEHK QGYMRPDMEI EGGLSDLNLK ITQEQMQFAL ELSKSVPAAF ATEPDEDVQG
EVEEELENET VIPAKKAMES KQEAKGKDKN EEKRFSTSSL GPELGSSEDT WTKLDLVFKV
GSIGLELIKG KENEPIRDVK AHSLSQFSLN HTHVKLRMIS DGALESELLI QSLSIRDTRS
KGTNKFRKIM SLINTDVKQQ FMASVSISGG EERSMVALLT IDSPRMIFSL DYIFALKGWL
DRGLAVEGPL DIEDHATDAD DSRSVSTQHS GDGAPSKGNV QQPEVPAVSK PQPDQNAMDV
SFRVNVVDAQ VVLIANPAIT TSEAIVLGTK QVLVAKQHAM TLQVDKVGMF LCRMDRFETN
RLRILDDFSV QTSLDMRNQG KDSSLTSVNV DIEPLVLRLS LRDILLAMQI FNRASAMSSD
EDAAMPHQDP KKLAPTKGGT SIQSRRRSSA KPASTSQGPG AKTIATTKSQ KSLPPSQTAG
PGSAIITREE MKVAMAGIRV VLIGDKHELP MLDWSVKKFN IDVRDWSSNL SADTRLDTFF
NVYNFSKSAW EPLIEPWSVG FHMSKDTNPD KLSMEFYSKK NLELTLTSAT IALASKSFDF
LSSDEDMLSK PRGMDAPYRI RNHTGFDVNI WAESKGDDEG SAAKLEDGQE IPWRFEDAMT
TRETLTSEDA SAGLGIKLEG SGFNSVDKIS VSREGEKMYN LYPKKDKIQH RLLVEVKLGT
DNIKYITFRS PLLVENNTQI PVEVGVFDPE AGNILKIERI APGDGRPAPV GAAYMHSLIV
RPDQGFGYTW CRERLFWRDL LKRRTRTLTC RHENDGEDSP PFYFQMHAAL DEKNPLTKSY
PYMRIRLHAP VTIQNLLPFD FQYRMFDQNT KKDWKNFLRK GGVSPVHVVE LTHLLMLSVD
MQDTPFRASE FTIINSSDRE NFKRERTMVV KDRNDLNLRL KLQYFTIPDS GGAFMVTVYA
PYIILNRTGL ELDIRSKTFL GGTRAAAGQG IFTAREGDEP RKPRPLMFNF PTDDKKNRAL
IKLGDSDWSR PQSFDAIGST YAVTLASSSG RREMDVGVSI AEGEGKYNLT KVVTIAPRYI
VKNKLGEEIN LREPGSSDII TMQDGDLLPL RFLRQAANHQ LSLCYPGINN AWSSPFDIAN
VGHVHVKLAK AKQRQKLIRV DILMENATLF LHLSVETKHW PFSMRNESSQ EFLFWQANPN
VDEDDEDQVA GWKPIRYRLP PRSIMPYAWD YPAAKRKEII LSANKREKAV KLAEIGNPPP
MRIPPSQEHP RGVIIDLNIV ADGPTQTLIL SNFRQSKSLY RQKTATQSNT SGFEVKDLDT
DITFSARLAF AGIGVSLINR QLKELVYLTL RDIELKYSDS PLYQTLKATI KWIQLDNQLY
GGIFPIIFYP SVVPKTGKEM EAHPILHAAV TRVKDDSYGV LYIKYFTVLL QQMTLEIDED
FIFALLDFAK IPGASWSEPK EGKLCDETLE LPEPTQQQSG QDIYFELLHL QPMQFDISFV
RTERINAEQE AQSTLGGNPL MFFVNVVTMS IGNVNDAPIR FNALLLENAR VSTATLYNNI
KTHYVQESLR QVHVVIGSAD FLGNPVGLFN NLSSGVQDIF YEPYQGLVMT DRPQDLGLGI
AKGAGSFVKK SIFGFSDSMA KFTGSVSKGL AAASMDKEFQ DRRRMARARN RPKHALYGIT
SGGNAFAESL ASGIGGLARH PLQGAEKEGA LGFAKGVAKG VIGLATKPAI GAFDLASNMA
EGVRNTTTVF DQEGLDRVRL TRFIGADGIV RPYSQREALG QFWLKTLDSG KYFNEDYIAH
LELSGRDLMV MVTYSNILLV KTKRLQSEWD VPLKDIQTIS KERTGISIFL KGGVSGPFLP
VGEEESRNWL YKMIAVAVNA FNERYGGAN
//
