ID A0A1V6UZ95_9EURO Unreviewed; 3169 AA.
AC A0A1V6UZ95;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Vacuolar protein sorting-associated protein {ECO:0000256|PIRNR:PIRNR037235};
GN ORFNames=PENCOP_c003G08934 {ECO:0000313|EMBL:OQE43718.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE43718.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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}.
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:OQE43718.1}.
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DR EMBL; MDDG01000003; OQE43718.1; -; Genomic_DNA.
DR STRING; 36646.A0A1V6UZ95; -.
DR OrthoDB; 199953at2759; -.
DR Proteomes; UP000191500; 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:UP000191500};
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 591..826
FT /note="VPS13 middle RBG modules"
FT /evidence="ECO:0000259|Pfam:PF16910"
FT DOMAIN 1940..2516
FT /note="Vacuolar protein sorting-associated protein 13 VPS13
FT adaptor binding"
FT /evidence="ECO:0000259|Pfam:PF06650"
FT DOMAIN 2765..2940
FT /note="Vacuolar protein sorting-associated protein 13 DH-
FT like"
FT /evidence="ECO:0000259|Pfam:PF16909"
FT DOMAIN 3038..3144
FT /note="Intermembrane lipid transfer protein VPS13 C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF21679"
FT REGION 853..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1713..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1563
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3169 AA; 355938 MW; 768B07DFD7019D7D CRC64;
MLEGVVANLL NRFLGYYVKN FDATQLNIGI WSGDVKLRNL ELRREALDQL RLPLNVVEGH
LGQLTLSIPW SNLRGKPVKV EIEDVFLLAA PREDADYDPE EEEKRENALK MERIESAEIL
RERNAEGMSQ EEQRRNQSFT QSMITAVVDN LQISIKNVHF RYEDSISSPG HPFAVGVTLK
ELSAVSTDGD WNPTFIQSDS SVTHKLAVLG ALSVYWNTDA TLLGTGRGSD IGAEAQGISR
AELMEKLKTA IDADEGNQFM LRPVSGRAGL EMDKSGKYDR PAIKARLLFD ELGFVLDDKQ
YRDALMLVDL FHYFIRHQEY KKIQPKASPK EDPGAWMRFA GEAVLSKIQE RNRRWTWDYI
KERRDDRIAY IALFKKRKKE EAFTPEETKQ MQKLEAKLSY EDIRFWRSLA RNQLRKENVG
VKKPAEQQSW SAWLWGAKKE ESEETTMTEE QRQELYNAID WDEKKAIAES VDVPREWVKL
QVNWSLRAGS FTLIQDPHGS ANEVMKLVFD NFRAKALQRH DSYLLDLDLG GLKMYDGTTA
GTLYPQIVKV KDSPPEPKKI QELGDDDDDI ASQASADDLQ DEDSLFHLQL EKNPLDSDAD
TAVKVKLKSI EVIYNPRFLV GIVQFFEPPE RHMESIGALL DTAGATVEGL RQQTRAGLEF
ALQEHKKVDA QFDIHAPLII VPESITQPSS LCLIIDAGHA SVNSELVDRQ AMRDLQSKQK
QQYEEEDYKK LEHLLYDRFL IKLDSTQVLI GPGIEATKAQ LNTNVESRNF HIIDRINVDF
ALEMCIVPKV TQLTRTRISG HLPELHASIS DTKYKGLMKL IDIAIPQFDA GKSASDPVTA
AIAKEEAAIA TRARSSSFQP SAQRDLPVVD DDDEEEEEDV EAENEQAKKA VDTPTNIHRR
DFEFKFTVGR LRGSLFRADP HDPQRDQLLV ELVAEGFELD FYMRPYDMVA EVVLKSLSVD
DYIEENPVPE FKRIISSKGF DADEDKDLFQ LKMVRVKPES PEFDSTYEGV AMNLDISVST
INLVVTRKTL LTLLDFILLT FTDPQQPSEP NPETDKAIEG SPNVDQKPEQ AGKLRIRANL
KSIALILNND GVRLATLSLN TADVGIFLVG SSMLIQSRIG SLTLVDDVNL GAAEDSDIRR
LLTIEGDNFA DFKYETFDPQ SDTYPGYDSE VYLRSGSIKI NFLEEPYRKI INFLVKFGKM
QAIFNAARQA AASQANQLQE NASRVRLDII VKTPIVVFPR VMKDGRPRDT ITAHLGEIYA
KNEFVPMDEG KDSPAVNVIS TGVRNIRLTS KFHFEDGTTE ELEMIQKVNL EFSICYLEHQ
ANNPRPDMEI EGSLSPINLR ISQSQLKFLL ELSNSIPGAF ATDAEQQELE AMESLPPSVT
EPTREATSKA VQAQNGPGGA PADDIENKET WVRLDMIFKV DSVGLELILA NDDQPVGRLE
DSSLSKFSLN DTRVKLRMLT DGSLESELLI HSFSIRDSRK QDSNKFRNIM SLINNDVQQQ
FMASVSMSGG PEKHLVAMLT IDSPRIIFAL DYLSALQSFS QSAFASEEPV EVVEDESDSP
EESESGSDAA ATPDKTITEA SSGDATGAAM TVSFRVNLVD AQVIMVANPA IPHSEAIVLG
TKEVLISHQN VSTLQIQKVG MFLCRMDKFE TSRLRILDDF TLEMSIDSRA QEKASVLTSI
EVHLEPLVLR LSLRDILMAI QIVNKASEMR AQTSQPVEGG DAKKITDAKT TRGRSASKAS
STIAKRARRL SQGVANLDKA ITPQSSVLLK REEISAKIDG VRVILIGDLH DLPLLDWSVK
KFNVDVRDWS STLNADTNFE TFLNVYNFSK SAWEPLIEPW QLGFHLAKEV NPDVFSFDVY
SHKTMELTVT SATIALASKS FQFLSTHEDV LSKPRGADAP YRIRNYTGFE LRVWADVSAG
EEGPAAKLND GEESPWRFED STAVRETLTP EGHGGVVGVK LEGSGFDSIS RIPVVREGET
IYALKPKQEN ILHRLLVEVK LGPDNVKYIT FRSPLLIENN TQIPVEIGIF NPGEGHLLKI
EKILPGDARP APVGSAYLHS IVVRPDQGFG YDWSGERLFW KDLIRRPTRT VKCVSESGGQ
SPPFYFQVNA TYDSKDSLTS VYPYMRIRIF APVEIQNLLP YDFKYRIYDK NTKKDWTNFL
RKGGVSPVHV VELSHLLLLS IDLQDTVFRQ SEFAIVNGNA QDYRREHTLS LKDERGLQLK
LQLHYFNIPN SGGAFKVSVY SPYLILNKTG LPMDIQSKAF LQSARNAAGQ GLRADPRDEG
RALPYMYSYA NEDQRNRSIL KVSDSAWSKP QSFEAIGSTF EVIFPDRQGR SEFHSGVSVA
EGEGKYKLTK VVTLAPRFIL KSKLNEDLLV REPGSSNVLQ VQNGQLVPLH FLRQVQEKQL
CLCFPGVNNQ WSSPFNIADV GTVHVKLAKA NQRQKLIKVD IILEGATLFL HFSVESRNWP
FSMRNESDME FIFYQANPNV EDDDEDDQTS GWRPIRYRIP PRSIMPYAWD YPATKNKSLV
LTCQGKERHI KLAEIGNLIP MRIPPSQPGG YQKIIDISIA ADGPTQTLVL SNFKPSKSMY
KQQRGQPSQT GTNTGFEVKE MNSDVNFKAQ LRLGGIGISL INQNLKELLY LTFREIEIKF
RESRLYQTLN TTIKWIQIDN QLYGGIFPIL LYPSVVPKTG KEMEAHPIFH AMVTRVKDDS
YGVLYIKYAT LLLQQMTLEL DEDFVFAMLD FVKIPGASWT EEQEGKLCDE DLNIPEPQQA
DNGQDVYFEL LHLQPMQVDI SFMRTEHVNV EDAMQPSNPL MFFVNVMTMS MGNVNDAPVR
LNALMLENAR VSFPSLVGNI RAHYTQEFLR QIHIILGSAD FLGNPVGLFN NVSSGVAAIF
YEPYQGLVMT DRPQELGMGI AKGATSFVKK SVFGFSDSMA KLTGSMSKGL AAATLDKEFQ
TQRRMSKVRN RPKHALYGIT AGGNAFATSL ASGIGGLARH PLQGAEKEGI QGFFKGVGKG
VLGLATKPAI GAFDLASNLA EGVRNTTTVF DAEGLDRVRL TRFIGTDGIV RPYSQREALG
QFWLKTTDDG KYFNEDYIAH LELPGRDMLV LLTYARIMLV RTKKLYTEWD IRLTDIQTIS
KERTGMSITL KGGANGPFIP VQDESSRNWL YRQIAVAVNA FNEKYNARG
//
