ID A0A428P339_9HYPO Unreviewed; 3213 AA.
AC A0A428P339;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Vacuolar protein sorting-associated protein {ECO:0000256|PIRNR:PIRNR037235};
GN ORFNames=CEP54_013404 {ECO:0000313|EMBL:RSL47425.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL47425.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL47425.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL47425.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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}.
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:RSL47425.1}.
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DR EMBL; NKCI01000217; RSL47425.1; -; Genomic_DNA.
DR STRING; 1325734.A0A428P339; -.
DR Proteomes; UP000288168; 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 Reference proteome {ECO:0000313|Proteomes:UP000288168};
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..380
FT /note="Vacuolar protein sorting-associated protein 13
FT extended chorein"
FT /evidence="ECO:0000259|Pfam:PF16908"
FT DOMAIN 595..831
FT /note="VPS13 middle RBG modules"
FT /evidence="ECO:0000259|Pfam:PF16910"
FT DOMAIN 1986..2561
FT /note="Vacuolar protein sorting-associated protein 13 VPS13
FT adaptor binding"
FT /evidence="ECO:0000259|Pfam:PF06650"
FT DOMAIN 2809..2985
FT /note="Vacuolar protein sorting-associated protein 13 DH-
FT like"
FT /evidence="ECO:0000259|Pfam:PF16909"
FT DOMAIN 3083..3186
FT /note="Intermembrane lipid transfer protein VPS13 C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF21679"
FT REGION 835..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1386..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1747..1816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 415..473
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 839..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3213 AA; 361460 MW; 0A1185EEC1345101 CRC64;
MLEGLVAGLL NRFLGMYVKN FDPAQLKVGI WSGDVKLRNL ELRREALDQL KLPINVMEGH
LGELTLIIPW SNLRGAPVKV FIEDVFLLAS PKEEAEYDEE EEERRKQRLK MEKLDSAELL
KERNQEGMSQ EEQKKSQSFT QSLVTKIVDN LQVTVKNIHI RYEDSISAPG HPFALGVTLE
EFSAVSTDGQ WKPTFIQDSS SVTHKLATLG ALAVYWNTDS TLLGTGREAA TPSSEMLPHD
EIVEKFREMI GKGAEKNTSH QFILKPVNGQ AKIELDKSGD IKVPKFKANL LFEEIGLVLD
DDQYRDALMM VDLFHYFIRH QEYKKLQPKG ARPKEDPHAW LQFAGNAVLS KIHERNRKWS
WDYFRERRDD RKKYIELFKK RKQGQQMSPE DIDAINSLEW KLGYEDLRFW RSLARNQLKK
ENAEALKKQP QQQEQQQQGW LSWVWGSKPQ ETIEQNEENT QMTEEQRQEL YEAIDWDEKN
ALADEVDVPR EAIKMCIETS LSTGSFTLKR NPHDNTSDLL SLHFDVFKAK ALQRKDSLLA
NVSLGGLRVN DGTTPDTLYP EIVRVKDAPD VKQRRRLSLA ELENAEEDPF FQFEVEQNPL
EREGDIAVVG KMKPLEVIWN PNFVVGIADF FRPPERHMES ITALMESAGA TVESIREQTR
AGLEFALEEH KTINAELDLQ APLIIVPVSI TTEDSTCLIV DAGHIHVNSQ LVDQDTMKEI
QSKQKQSYSD EDLKRLESVM YDKFIVKLTS TQVLIGPSIE ETKAQLVEKD DEARLHVVEQ
INVDFTVETS ILPKAPNLTK FKVSGHLPML HATVSDSKYK NLMRIIDVAI PKFGEPSLPE
SQSEGQKEQS RPRLTSTASN RSRRKSHRER RQSTPFPFMA QTAVVLDDMD EDDDNFEDAV
DGGGVEQLRI QQRIFEFKFK VDTLKGSLYR SDPDQRKPDA LLVELVAERF GLEFYTRPYD
MAAEVSLGSV TVDDFVDNPP DEFKSIISSG DSDDLKAGRS LVHVKFIKVN PMSPEFMPVY
EGVETNVTAK VSTINLIVTR KTLLTLLDFI LVTFTNNDSQ QAGQPGGPQS LLDNYDDDTA
SVDVSFNTTP PPNSGSIRVK VDFKSIRLIL NNDGIRLATL SFNKADAGIF LRQNTMRISA
RLGDLSLVDD VNLGVSEDSH LRQLVTIQGD DLADFRYETF DANNSKTYPG YDSSVFLRAG
SVKVNFVEEP FRKIIDFLVK FGKMQALYNA ARQAAMNQAN QMQQSPSRFK FDVVVNTPIV
VFPRVVKPGR PERDLITAYL GEIYAQNKFA PLDDSEDSEI AMKLSAGIRN IRLTSDFHYA
DDVSEELEMI DHVDLGFNIT YAEHKSGVKR PETEIEGTMS DFNLRLTQYQ VKFLMEISKS
VPAAFAGEGN DNEEEAAKAV DEGTLQRART LNTETDSGDD QTLVDLGPEL SSIDQAWTKL
DLVFRINTIG LELIMAEEDS PVHDIAKSSL SRFSLNETKV KTRMLSDGSL EAELLIRSFT
IYDSRPRETN KFRRIMSSMN KEVQQLMASV TMSGGKEKSL IAMATIDSPR VIFALDYLFA
IQKFAVEGLT VEEASPMDDE SILETTPEES DTDSLQVSFS GNTASRPRSQ LSRQQSTEVA
QIEEKKEEPS MSIAFRVNLV DAQVILIANP LTSSSEAIVL SIRQMLLSQQ HVLTFQVSQI
GMFLCRMDRF ETSRLRIIDD FSIQLSMDSS KPLSTSIHVD VEPLVLRLSL RDILLVLQIV
SKAGELSGNE PKQAKETPAE QKARELRNAG MKQRSASGRG QSTIAGRTKA TATSHAPSHA
VDSKAKQQTQ QAAQRRHEEL SATVEGIRVV LIGDVHELPI LDLGIKKFSA AAENWSSNLK
AETAMDLYSN VYNFSKSSWE PLLEPWQVGF GVAKDTVSGL LSVDVASKKV FDVTITTATI
ALASKSFDFL TTEQDVLDKP RGVEAPYRIR NYTGFDVVVH SKSPTSDEPI NLRLEDGKEA
PWSFEHWEKM RENLLTESNQ NYVNIQLEGS GFDPVKNVRL NREGEYLYSL RPKTDNVLHR
LCVEVELGTE DNIKYVTFRS PLHVENATQI PVELGIYDAQ EGHLLKIEKI APGDSRPAPV
GAVFEKRVLV RPDGGFGYQW SNDQLFWKDL LKRPTKQVVC KGENGDPFYF QVHARFDKAN
PLTKQYPYMK IKLSAPVTLE NLLPYDFKYR IYDKNTRKDW TNFLRKGGVS PVHVVELSHL
LLLSIDMQDT VFKASDFSII NPGNNEDFRK EGKLVVKDDQ GLPLNLSLHY FKIPNSGGAF
KVTVYSPYVV LNKTGVDVRV RAKGFLQQAK PAAGQFPLMD TSDQERPKAL PFMFSYGSDD
HRNRALLKVA DSEWSKPQSF DAIGSTSEVV LNSPNKNKEI HVGITVKSGE GKYKLTKVVT
LAPRFVLHNK LGEEILVRES SSSGYLTLGS GALQPLHFMQ KSKVKQLCLC YPGVNNHWTS
PFNIADIGTT HVKIAKAGQR QFLVRVEILM EDSTVFLNLS METKSWPFSM RNESDTEFMF
WQANPNVDEE GVEDRSGWRQ IRYRLPPRSI MPYAWDFPAA KFREIIISIN GKERHVKLAE
IGNQIPMKFT TSTGQQKIID INVAADGPKQ TMILSNFRAS KSMYKPKTLS RTNTGPEAFE
VKDQDTGATF RAQLKLAGIG VSLVNAQMKE LAYLTLRDVQ LRYSESPLIQ TVSMAIKWIQ
IDNQLYGGLF PMILYPSVVP KKAQEVEAHP SLHAMISRVK DDSYGVLYIK YATILLQQMT
VDLDEDFVFA LLDFTNVPGA SWTMVDDEGK LCDEDLDIPE PTQVQAGQDI YFEVLNIQPM
QLDLSFMRTE RVNAEDKGSS RNPIMFFLNV MTMAIGNVND APIRFNALIL DNVRVTTAVL
IQNCSSHYSQ EVMYQIHKIL GSADFLGNPV GLFNSISSGV TDVFYEPYQG LILSDKPEEF
GLGIAKGAAS FAKKTVFGFS DSFSKFTGSL SKGLAAASLD KQFQDRRRIT RARNRPKHAL
YGVAAGANSF ITSVASGVGG LARKPLEGAE QEGALGFFKG VGKGVIGLAT KPAVGVLDMA
SNVSEGIRNT TTVFDGQELD RTRFPRFIPQ DGIVRPYNPR EALGQYWLKQ VDNGRYFDEQ
YIGHLELPKE DMVVMVTYAR ILLIRSRRLT SEWDVPLKDI QTIAKERTGV SLALRGGANG
PFIPIGEGSE RGFLYKMVGV AVEEFNRRFR SGD
//
