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Database: UniProt
Entry: A0A0J9XDG4_GEOCN
LinkDB: A0A0J9XDG4_GEOCN
Original site: A0A0J9XDG4_GEOCN 
ID   A0A0J9XDG4_GEOCN        Unreviewed;      3152 AA.
AC   A0A0J9XDG4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Vacuolar protein sorting-associated protein {ECO:0000256|PIRNR:PIRNR037235};
GN   ORFNames=BN980_GECA10s03101g {ECO:0000313|EMBL:CDO55305.1};
OS   Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Geotrichum.
OX   NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO55305.1, ECO:0000313|Proteomes:UP000242525};
RN   [1] {ECO:0000313|EMBL:CDO55305.1, ECO:0000313|Proteomes:UP000242525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO55305.1,
RC   ECO:0000313|Proteomes:UP000242525};
RA   Casaregola S.;
RL   Submitted (MAR-2014) 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; CCBN010000010; CDO55305.1; -; Genomic_DNA.
DR   STRING; 1173061.A0A0J9XDG4; -.
DR   OrthoDB; 199953at2759; -.
DR   Proteomes; UP000242525; 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   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          140..368
FT                   /note="Vacuolar protein sorting-associated protein 13
FT                   extended chorein"
FT                   /evidence="ECO:0000259|Pfam:PF16908"
FT   DOMAIN          593..829
FT                   /note="VPS13 middle RBG modules"
FT                   /evidence="ECO:0000259|Pfam:PF16910"
FT   DOMAIN          1925..2496
FT                   /note="Vacuolar protein sorting-associated protein 13 VPS13
FT                   adaptor binding"
FT                   /evidence="ECO:0000259|Pfam:PF06650"
FT   DOMAIN          2749..2923
FT                   /note="Vacuolar protein sorting-associated protein 13 DH-
FT                   like"
FT                   /evidence="ECO:0000259|Pfam:PF16909"
FT   DOMAIN          3021..3126
FT                   /note="Intermembrane lipid transfer protein VPS13 C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21679"
FT   REGION          435..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1531..1562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1531..1548
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3152 AA;  357333 MW;  53A5CEEB368C9A44 CRC64;
     MLESLVASLL NRFLGSYVKN FDPKQLNIGI WGGDVKLRNL SLKREALDQL KLPIDVVEGH
     LGQLVLQIPW SNLKNKPVKV LIEDVFLLAV PKLDQDYDDD EQQRRNQAVK LSRLDDLELA
     DKMSTSINLS PEEIRKNQSF TDSLVTKIID NLQITIKNIH IRYEDHTSVP NHSFSLGISL
     EELSAVSTNS EWDPIFIQDT TNITHKLTTL SSLSIYWNTD SKLIKEDELP EILRFMSLVP
     GLKENITDSF QYILRPVSGL GRITINKTAV GGPKTKAQLM FDELGFVFDS DQYRDVLWVA
     EIFRIYNRTK EFQKFRPKTP VMKNPKAWLK YAANVVLAEV KQKRREWTWD YILERREDKL
     RYIHLYKKKT ISPPLSAEET EEFNQLEIKY SFEDLRFYRS LAKSELKKEK AQIKAAQVEK
     PAASGWSSWL WGSSAEPDKA DETASDTENP DSVTITDEQR QELYDAIEWD EKQVITDSID
     VPRDTVTLEV EATLKTGSFK LRRNPHNNPE DIVQILFTGL SSSFYNRPDS YLANVSLHKL
     RVDDGNSESL YKQVVTVKSL ASDSLPRPES EDESSESEIE EVSEKDAFFW MSFESNPLDD
     IADTNLFIKM KSITVFYNTL FFENVMRFFH PPKIHLETLG AILNAANATV EELRDQTRIG
     LEYALQEHKT VNLKLDMQAP LIVMPLDVFS WSSPCAIIDA GHISVVSHLV GKEVIEEVKK
     KKTLQYTDSD WKRLESLMYD KFNLKLHNTQ LLIGSNVRDT MKQLHNGVSD ATASVLDRIN
     LDFLIEVSIL PDAQSLTKFK MSGTLPLFQA SMSDAKYKIM MQLIDKGIPN FSFDDLIEPD
     ESETPESNDK AVLIGNRINQ ELPEYVHDDS ASEDSVGAEP LSASSRVSTQ KIFEFNFKVE
     KMNMALHRCT SIETLAQEPV VDMNLDSFEI CYYYKEKEMM ADVVVQNIDI EDYTQKDVPV
     ELTKLATSIP TDTSPSDFFN VKYKRIKTDH VDRFDQQISD QDIVVTMSAM KYVVSPKTFL
     TILDFIITTF TNPQPQQLPP ASNHLDGTLT PTGEVEPVAK IDVKVNLSSI TILLNDDGIK
     LATLQLDSAL VNVFLVPEKM KVEARVGKLS LHDEVNEGSA RNSILRQLIS IEGNDLADFK
     YETYDPSSSD FHYNSSVYLR AASMRFNVVE EPFARIVKFM SKFVQMKALY DSARQATVAQ
     ANQIQIEDAN KIHFDILVST PIVVIPKLVE FSDDSLCDMV VAHLGEIYAK NEYIHFPEDP
     NGPLANHMSV GIRDIKLSSN FNFPNGTNQY LEMIDKLDLT LDMSFVQPYE TMTRPVTVIS
     GNLSDTSMKF TEMQYKFLMQ TSSILSTIFS GEPGIQEQEL DQLEEELRAQ KNLQPVAVIR
     VPELPPVPAS VNKLDLSFYA KKIQLCLYNK TEEVMTDKLE KCSLTRFSLN DAGIKLRMKQ
     NSDMESDIHI KSFTVHDTRS VKENMFTEII PGIKHDEYQF LCNLTMTGQE KRKLKAILTV
     DSPSMILALD YLFALREFLF YGLATSPESI PELDDEEYEE ESEYESSEDE TSQLPARPGS
     APQSNLTIEY HINIVDASVI LLANPKLEDS EAIVFKAEHF ILSQQATMVL SANKVGMFLC
     RMDNFERNRL RLLDDFSLTT TMDNRGSSPN SEICKINISC EPLVLRLALR DVMLALDIVK
     RASALFTQTE SQTETPSKFK EPIKYSRFSK LQKSRSSAVS KSYATSFGGR SRNSLRGRRD
     SGSTSRVIVP IIRGQTLLAE FEGLRFVLIG NIHELPMLDM CTKPFKVKVR NWSSDLTIDS
     GIETFVNIFN YEKSAWEPLI EPWDLGLHVA RSIEDNNTAI NLYSRKMAEI TVTSQTISIV
     DNMMKFLSED AEEFLAKSIG HIAPYRIVNQ TGYDLEVWID HSDRDDIKNT TVIKDNEEIP
     WRFYDWNTVR ENLSTDTQKV NLGVALKNSP FDPIRNMSVT SVGEHIHTLY PKTDKVSHRL
     MCEVVMDESV KRIVLRSALT FENKTQIPID IAIGPSNNES FMCRIKPGQS RAIPIEHAYD
     KAVSIRPDPS FKFGWSREPM YWKNMLTGPK SISCLPLNEN SSTKFYFQAT AIYDKSIPLT
     RIYPHMKIVL SPPVEITNLL PFDFTYRIYD KKTGQDWGNT LKQGATGAVH VVELSHLLLL
     NVHPKEAGYN CTDFAIINTP KKDFSLEHRL LTRSTDGQRL VLKLHYIDDK ANGGGCKVQV
     YTPYLILNKT GLDIKVQTKF NTATSRVHSI AQLHNGKETF MKIASPQMWS FDSDDRGNRA
     TIRVGDSKWS EPLSFDTLGK DSDVTIPSST RQSEIHVGLH ISEGPGKYQM TKIVTLTPRF
     IINNKLSYDL QIKDSGSTLI VVGAKSLQPL HFLRRAEQQQ LSASFQGSSS VWSAPFNIEN
     IGCTFLRMYQ HDVGYVLLKI DILLENATLF LHIDKADKNW PFSIRNFTNH TFQFYQANPY
     VDDRGIELAQ HPKFTPVLYQ IPPKSVMPYA WDYPAAPLKE LVLNANGKER RIQLAEIGNL
     QPMKVPSTSD RPGGIVDLNV VADGPTQTLV MSDYDPSISL YKMNTQLTSS KSSVVPTEQF
     SVQDDEGEIQ SSITVRFEGI GVSLINRRMQ ELCYMTLRGI EFQYKCSEIY ETFSMKMKWM
     QIDNQLYGAI YPILLFPSVV PQTGKEMDTH PTFSGSITKV RDDSHGVFYL KYATILLQQL
     TVEMDEDLLF SLIEFFNSYK PTNDDDKVVL CDPQLEIPEP LTDTSGLDFY FEVLHIQPAQ
     MDLSFVRTER LNSEERASSD NPFMFFFNAL TMALGNINDA PVRLNALVIE NVRTPLPLLM
     QSISTHYRQE FFYQIHKILG SADFLGNPVG LFNNLSSGFM DMFYEPYQGY IMNDRPQEFG
     IGLAKGGLSF MKKSIFGISD SFSKFTGSIS KGLSAATMDR AFQDKRRMKR ARNRPKHALY
     GITSGANSFV DGITSGVSGL ALAPVQGATE GGALGFFKGL GKGIVGLPTK TALGFFDLAQ
     SVSEGVRNTT TVFDGNAIDS VRPPRFISLE GIVRPYSQRE AQGQAWLKVA NNGEFFRDNY
     LAHLSLADDE MIIIITYLRI MLLSTATMAT EWEVRFRDLQ TIAMERTGLA LILRGGVQGP
     FIPIPDTPSR KFLYKEIGVA VTEFNRKYQT LS
//
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