ID F7W5H9_SORMK Unreviewed; 3143 AA.
AC F7W5H9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Vacuolar protein sorting-associated protein {ECO:0000256|PIRNR:PIRNR037235};
GN ORFNames=SMAC_09548 {ECO:0000313|EMBL:CCC12767.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC12767.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC12767.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC12767.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC12767.1}.
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DR EMBL; CABT02000031; CCC12767.1; -; Genomic_DNA.
DR RefSeq; XP_003343651.1; XM_003343603.1.
DR STRING; 771870.F7W5H9; -.
DR GeneID; 10800906; -.
DR KEGG; smp:SMAC_09548; -.
DR VEuPathDB; FungiDB:SMAC_09548; -.
DR eggNOG; KOG1809; Eukaryota.
DR HOGENOM; CLU_000135_0_0_1; -.
DR InParanoid; F7W5H9; -.
DR OMA; SGWRPIR; -.
DR OrthoDB; 199953at2759; -.
DR Proteomes; UP000001881; 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; IPR015412; Atg2/VPS13_C.
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; PF09333; ATG2-VPS13_C; 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; 2.
DR PIRSF; PIRSF037235; VPS13_fungi; 2.
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:UP000001881};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR037235}.
FT DOMAIN 2..57
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12624"
FT DOMAIN 116..358
FT /note="Vacuolar protein sorting-associated protein 13
FT extended chorein"
FT /evidence="ECO:0000259|Pfam:PF16908"
FT DOMAIN 578..813
FT /note="VPS13 middle RBG modules"
FT /evidence="ECO:0000259|Pfam:PF16910"
FT DOMAIN 1962..2038
FT /note="Vacuolar protein sorting-associated protein 13 VPS13
FT adaptor binding"
FT /evidence="ECO:0000259|Pfam:PF06650"
FT DOMAIN 2039..2493
FT /note="Vacuolar protein sorting-associated protein 13 VPS13
FT adaptor binding"
FT /evidence="ECO:0000259|Pfam:PF06650"
FT DOMAIN 2739..2915
FT /note="Vacuolar protein sorting-associated protein 13 DH-
FT like"
FT /evidence="ECO:0000259|Pfam:PF16909"
FT DOMAIN 2921..3001
FT /note="Atg2/VPS13 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09333"
FT DOMAIN 3012..3115
FT /note="Intermembrane lipid transfer protein VPS13 C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF21679"
FT REGION 426..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3143 AA; 352531 MW; 2188BC703C42B77E CRC64;
MLEGLVAGLL NRFLGMYVKN FDPTQLKVGI WSGDVKLRNL ELRREALDQL KLPINVVYIQ
DVYLLASPKE EAEYNEEEEE RRKQRIKMEK LDSAELLKER NQEGLSPEEQ KRSQSFASSL
VTKIVDNLQV TVKNIHVRYE DAISAPGHPF ALGLTLEEFS AVSTDGEWQP TFIQDSTKTT
HKLATLGALA VYWDTDATLL GPGREAVTPG YQPKPHDEIL AGFRSMIAKT DGDLPENHQF
ILKPVSGQAK LELDKTGDST VPKFKANLLF DEIGVVLDDY QYRDALMMVD LFHYFIRHQE
YKKYQPKGVR PKEDPRAWLQ FAGNAVLSKI HDRNRRWSWD YFRERRDDRK RYIELFKKRK
QGQQLSPEEN DDLTKLEWKL DYEDLRFWRS LARNQLKREN AEALRNRPPP PAQPQQQGWI
AWALGSKPKQ QQQQEKQQED ENTQITEEQR KELYEVIDWD EKTALAAEVD VPRDTVQMQL
EASLSTGSFT LKQNPHGDSR DLISLHFDVF KAKGLKRPDS FLADVSLGGL RVNDGTTPNS
LFKEIVRVKD APDNQIAHRM SIAELEQNSD EAFFQFQVEQ NPLDGQGDIA VTAKLKPLEI
VWNPNVVVGV VDFFRPPERH MDSINALMET AGATVEGLRA QTRAGLEFAL EEHKTLNAKL
DLQAPLIIIP ESITSKMSTC LILDAGHISV NSELVDKDTM KEVQSKQKQT FTDEDLKTLE
SLMYDRFLVK LSSTQVLIGP SIEETKKQLV DKDDKMLHIV DKITVDFVVE TSILPKAPNL
TKLKVSGHLP VLHASVSDAK YKSLMRIIDV AIPKLAGADA PSQPTGQPGP RPRLASNAST
ASHRLLEHRP STQLLPFSTS HQQAIILDDD DLDEDEDAFE DAKDGSATDQ LKLQQRNFEF
KFAVDELKGS LYRSDPDGKA PDQLLVDLVA QRFDLQFYIR PFDMSAEVSL GSVTVDDFVD
NPPAEFKAIV SSGDVEESGE IQDLVRVKFV KVRKDSPEFM PVYDGVETNL DVAISTINLV
VTRKTLLTLL DFVLVTFTNT ANPNPPPQNA ITDDGSETSI EVEPPASPQQ TTDGAIRVKV
DLKSIRLILN NDGIRLATLS FNHADVGVFI LGKTMRVAAR LGDLNLVDDV NLGVSEDSSI
RQLVAIQGEE LADFRYETFD AGRPESYPGY DSSIFLRAGS VKINFLEEPF RKIVEFLVKF
GKMQAIYNAA RQAAANQANQ FQQSPSKVKF DVVVKTPIVV FPRDVRPDRP KRDLITAYLG
EIYAQNKFVP LDDSENADIA MKLTAGIRNI RLTSNFHYTD GQEEELELID KVDLGFQITY
AEHKEGIKRP DLEIEGNMSD FNLRLTQYQL NSLLEISRSV PAAFSGDSEQ NRLDAEREVD
DRTLSKARTM SGFDDNGGNE QLIDLGPELG PQAETWTKLD LIFTVNTIGL ELINAPEDQP
VGDLDTASLS KFSLDSSRLK TRMDSNGSLE AEFVIQSFTI YDTRQRETNK FRRIMTSGNK
DVQQLMASVT MSGGKERNII AMVAIDSPRV IFALDYLFAI GQFVTVGLKV PEPEVPEKSP
LDTPDDMSDA ESMAVSYTGR RSDSIDQRRE PPDPPTEPPK EESKMRIAYR VNVVDAQVIL
IANPLSSSSE AIVLGTKQVL LSQQHALTFQ ISECGMFLCR MDRFDDSRLR IIDDFSVQMS
MDTSKPFTTN IHVDIEPLIL RVSLRDILLV MQIVSKASEL SGNESTEPKG TASDQKAKQL
KSSGMKQRTA SGKGTSTVAN KSKRTGTKTV ATDPRSQKGG QQPHDITKTP PRYEQLTAAI
EGIRVVLIGD VHELPILDLS IKSFSTSAEN WSSNLKAEAA IEMYTNIYNF AKSAWEPLIE
PWQVGFGVAR DQSTGLMSVD VSSKKTFDVT LSTASIALLS KSMAFLTKDE DVLGKPRGVE
APYRIRNYTG FNIIMQAKRE STEETAPLRL DDGQETPWSF ENWEKVRESL SGESNSTSNV
AIQLEGSGFD AVKNIRINRE GEFLYALKPK TDEVLHKLMV DVKLGTDNVK YVTLRSPLPA
PVGAVYMKSL LIRPDPGFGY GWSTDTLWWR DLLKRPTKTL MCKGEHGDPF YFQLSARNYP
YMRLKLSAPV TIENLLPYDF KYRIYDKNTK KDWSNFLRKG GVSPVHVVEL SHLLLLSIDM
QETVFKPSEF AIINSGTSED FRKETNLVCK DDSGLALHLK LHYFRIPNSG GAFKVTVYCP
YIILNKTGLD VGIRSKGFMQ HAKAAAGQLL VDVDESPRKA QPLMFSFGSD DHRNRALLKI
ADSDWSRPQS FDAIGSTTEV VLNSPSRNTE IHLGVTVDSG HGKYKMVKTV TLAPRYVIQN
RLGEDINIRE PSSSSLLELQ TGALRPLHFL QRGAVKQLCL CYPGVDNQWT APFNISDLGT
THIKIARAGQ RQRLIRVETL MEESTIFLNL TMEKKNWPFS MRNESDTEFT FYQANPNIDE
DGIEDRSGWR PVRYRLPPRS IMPYAWDFPA AKNKEVCISA NGKDRHVKLA EIGNLIPMKF
VGANGQTKVI DINVTADGPT QTLILSNFKQ SKSLYKQKSN AGSTDRGMFE AKELDTGVTF
RAQLRLSGIG ISLINSQLKE LAYITFRDVQ LRYSDSHLYQ TISLAVKWIQ IDNQLYGGIF
PMILYPSVVP KRAQEIEAHP SLHAMVTRVK DDSYGVEYIK YATVLLQEMT VELDEDFIYA
VLDFSKVPGA SWSSSDEEDK LCDDNIDVPQ PKQLAAGRDI YFEVLNIQPM QLDLSFVRTE
RVNVEDKTSS KNPVMFFFNV MTMAIGNIND APVRFNALML ENMRVSVPVL IQNISNHYSQ
EALYQVHNIL GSADFLGNPV GLFNNISSGF ADIFYEPYQG LIMSDRPEDF GIGLARGAGS
FVKKSVFGFS DSFSKVTGSF AKGLAAATMD KQFQDRRRIT RARNHPKHAL FGVTSGANSL
FTSVASGVGG LARKPLEGAE QEGALGFFKG IGKGVVGLAT KPAIGVLDFA SNVSEGVRNT
TTVFDGSELD RVRLPRYIPA DGIVRPYSQR EALGQSWLKQ IDNGKYFDEQ YIAHLELPTE
DMVVMVTFAR ILLIRSRKLQ TEWDVPLKDV QTIAKERTGL SLTLRGGTNG PFIPIGMESG
RTFIYRQVAI AVEEFNRRFR GLE
//
