VPS13_CHATD
ID VPS13_CHATD Reviewed; 3225 AA.
AC G0S3B8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Intermembrane lipid transfer protein VPS13 {ECO:0000305};
DE AltName: Full=Vacuolar protein sorting-associated protein 13 {ECO:0000305};
GN Name=VPS13 {ECO:0000303|PubMed:30093493};
GN ORFNames=CTHT_0020450 {ECO:0000312|EMBL:EGS22501.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272 {ECO:0000312|Proteomes:UP000008066};
RN [1] {ECO:0000312|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000312|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2] {ECO:0007744|PDB:6CBC}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-335, FUNCTION, AND REGION.
RX PubMed=30093493; DOI=10.1083/jcb.201807019;
RA Kumar N., Leonzino M., Hancock-Cerutti W., Horenkamp F.A., Li P.,
RA Lees J.A., Wheeler H., Reinisch K.M., De Camilli P.;
RT "VPS13A and VPS13C are lipid transport proteins differentially localized at
RT ER contact sites.";
RL J. Cell Biol. 217:3625-3639(2018).
CC -!- FUNCTION: Mediates the transfer of lipids between membranes at
CC organelle contact sites (By similarity). Binds phospholipids, including
CC phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic
CC acid (PA), and phosphatidylserine (PS) (PubMed:30093493). May play a
CC role in mitochondrial lipid homeostasis, Golgi vesicle transport,
CC reticulophagy, actin cytoskeleton organization and formation of the
CC prospore membrane (By similarity). {ECO:0000250|UniProtKB:Q07878,
CC ECO:0000269|PubMed:30093493}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the VPS13 family. {ECO:0000305}.
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DR EMBL; GL988040; EGS22501.1; -; Genomic_DNA.
DR RefSeq; XP_006692520.1; XM_006692457.1.
DR PDB; 6CBC; X-ray; 3.00 A; A/B=1-335.
DR PDB; 7U8T; X-ray; 3.00 A; A/B=1944-2635.
DR PDBsum; 6CBC; -.
DR PDBsum; 7U8T; -.
DR SMR; G0S3B8; -.
DR STRING; 759272.G0S3B8; -.
DR EnsemblFungi; EGS22501; EGS22501; CTHT_0020450.
DR GeneID; 18256083; -.
DR KEGG; cthr:CTHT_0020450; -.
DR eggNOG; KOG1809; Eukaryota.
DR HOGENOM; CLU_000135_0_0_1; -.
DR OrthoDB; 4159at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0120014; F:phospholipid transfer activity; ISS:UniProtKB.
DR GO; GO:0120009; P:intermembrane lipid transfer; ISS:UniProtKB.
DR InterPro; IPR026847; VPS13.
DR InterPro; IPR026854; VPS13-like_N.
DR InterPro; IPR031645; VPS13_C.
DR InterPro; IPR017148; VPS13_fungi.
DR InterPro; IPR031642; VPS13_mid_rpt.
DR InterPro; IPR031646; VPS13_N2.
DR InterPro; IPR009543; VPS13_VAB.
DR PANTHER; PTHR16166; PTHR16166; 1.
DR Pfam; PF12624; Chorein_N; 1.
DR Pfam; PF06650; SHR-BD; 1.
DR Pfam; PF16908; VPS13; 1.
DR Pfam; PF16909; VPS13_C; 1.
DR Pfam; PF16910; VPS13_mid_rpt; 1.
DR PIRSF; PIRSF037235; VPS13_fungi; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid transport; Lipid-binding; Membrane; Reference proteome;
KW Transport.
FT CHAIN 1..3225
FT /note="Intermembrane lipid transfer protein VPS13"
FT /id="PRO_0000455702"
FT DOMAIN 2..115
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 2290..2570
FT /note="SHR-BD"
FT /evidence="ECO:0000255"
FT REGION 1..1390
FT /note="Involved in phospholipid binding"
FT /evidence="ECO:0000269|PubMed:30093493"
FT REGION 1568..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3225 AA; 363788 MW; B14C181A9DBC3961 CRC64;
MLEGLVAGLL NRFLGMYVKN FDPKQLKWEV WNGKVRLDNL ELQREALDQL KLPINVIKGH
LGHLVLHIPW KTLASEQVKI NIEDVFLLAS PKEEAEYDED EEARRRHRLK MEKLDSAELL
KERSQEGLSE EEQKRTQTFA QALVTKIVDN LQITIRNIHI RYEDAISAPG HPFALGITLE
EFSAVSTDSD WTPAFITSIQ SAHKLATLES LAIYWDTDAK LIGPGREPHE HSDQIPHDEM
LKFFREMIAK GEADLSSEHQ FILKPVSGQA KIEIDKTGSH TVPRYKANLL FDEIGVVLDD
QQYRDALMMV DLFHYFIRHQ EYKKFQPKGV TPKEDPRAWF RFAGNAVLSK IHERNRRWSW
DYFRERRDDR RRYIELFKKT KQNIQLTPEE REDLDKLEWK LSYEDLRFWR SLARNQLKKE
NAEALKNKPP PQPQQQQGWL SWVWGSKPVQ PQQEEQQGDE NTRITEAQRK ELYEVIQWDE
KAALAAEIDV PRDSVRLLIE TSLSTGSFTL RQNPHGDARD LISLHFDLFR AKGLTRPDSF
LIDISLGGFR VNDNTTPDSL YKEIVRVKDA PNTEGQKRYS IADLELTVDE EAFFELQVEQ
HPLDGQGDVA VTMKLKPLEI IWNPNVVVGI ADFFRPPERH MESINALLET ANATVEGLRA
QTRAGLQFAL EEHKTVNAKL DLQAPLIILP ESITTPNSTC LIVDAGHISV NSELVDKETM
KQVQSTQDRP CTEEDLRRLE ELMYDRFLVK LTSTQVLIGP SVEITKQQLV QRDEKRQLHI
VDQINLDFVV AMSILPKAPN LTKLKISGHL PVLQVNASDS KYKHLMRIIE VAIPKLYDVE
PVLAPSGSHP TIRPRLASDA STRSRRASFR KASTQFLQFV SQQQEIVLDE SDSDDDSEKF
EDAKDTSVDE QLRIQQRIFD FKFTVDQLRG SLYRSDPEGK HPDQLLVELV AENFGVEYHL
RPYDMSAMVS LGSVTMDDFV ENPPAEFKSI VSSGDIEDRK QARDLVRVKF VRVKKESPEF
MSVYDGIETN VDVAISTINL VVTRKTLLTL LDFILVTFSN PQPAAPVATR MAVTDQESET
NIIVQPPPIE SGPIRVKVDL KSIRMILNND GIRLATLSFN HADVGVYILG RYMRVSAKLG
DLSLVDDVNL GVSEDSSLRQ LVTIQGNELA DFRYEYFDPD KPEKNPGYDS SIYLRAGSVK
VNFIEEPFRK IVDFLVKFGK MQAIYNAARM AAANQAQQLQ QSQSRIKFDI VVKTPIVVFP
RVVMSPKPKR DVITAYLGEI YAQNAFVPLD DSEKADMAMK LTTGIRNIRL TSHFHYSEGR
DEVLELIDHV DLGFTIIYAE HKEGIKRPDL EIEGSMSDFN LRITPYQLSA LLAISQSVPT
VFAADVEQHT ADAERDVDVA TLERARTMPS YSGASEEKVI DMAPELGTHG EAWTKLDLVF
TVNTIGLELI NAEEDYPVGD LEAASLSRFS LNSSRLKTRM DSNGSLEAEF VIQAFTIYDT
RHRETNKFRR IMTSGNSNVD QLMASITMTG GKDRNIIAMV AIDSPRFIFA LDYLFAIQKF
ITIGTTLPEA PIPEKSPMET PEETSDADSV RVGSSGRHSE SSAGSGQQLV PVGSQQQQPV
LAASEQATTS IAFRVNIVDA QVILIANPLS SSSEAMVLGT KQVVLSQQHS LTFQISECGM
FLCRMDRFDD SRLRIIDDFS VKVAVDMSKP NITQVHADIE PLILRLSLRD ILLVMQTIAK
ASELSGGTPS ETASKTVAER KAQQLRAAGL KHRTASGKGT STLATRTRHA SQSAASHSGK
TTTLVMQEVA KQTQRFEELI LTVEGTRMVL LGDVHELPII DMSVKTFTIH AENWTSNLKA
ETAFDMYMNV YNFAKSAWEP LIEPWQVGFG ITREAKTGVL SVDVTSKKTF DVTITAATIA
LLSQSFAFFS KEQDVLTKPR GVEAPYRIRN YTGFDVIIST KRQIPGASPT TEQQLPTMTL
RLEDGQEAPW SFEEWEKMRE SLMTESSTAN SISVQLVGSG FQEVKSIRLT REGEFLFGLK
PKTQQVLHKL LVEIKLGKDN IKYVTLRSPL LVENDTGIVV ELGVYDAHEG HLLKIERINP
GESKPAPVGA AYFKSLLVRP DPGFKYGWSS DTLWWRDLLK RPTKTLVCKS EQYGGEVFYF
RLHARWDQAN PLTRNYPYMR LKLTAPLTIE NLLPYDFKYK IYDRVNKQEW NNFLRKGGSI
PVHMVDLSHT FLLGIEMQDT PFQASEFVVI NTGNADDFKK DSHLVVKDNA GMPLNLRLHY
FRIPDGGGSF KVTVYSPYVI LNKTGLDVSV RSKGFMQSAR AAAGQTLIDV GGDGQKKARP
LMFSFHNDDH RNRALLKAGD SEWSKPQSFD AIGSTTEVVL QTANRNAEIH LGVTVDSGQG
KYKMVKVVTL APRYVIHNKL GEDINIREPS SSFWIPLKHG AHRPLHWLQR GAVKQLCLCY
PGVDNQWTAP FNISDLGITH LKIARAGQRQ RLIRVEILME DATIFLNLSM EQRNWPFSMR
NESDTEFTFY QVNPTIEEDA SEDRSGWRPV RYRLPPRSIM PYAWDFPAAK HKEICICAYN
KERHVKLQEI GNLMPMKLAL PNGESKTIDI NVTADGPTQT LILSNYRQSK SLYRQRSNAG
SISGREGFEA KEFDTGTTFR ATLRLSGIGV SIINTQLKEL AYITLRDVQL RYSDSALYQT
FSLAVKWIQI DNQLYGGIFP MILYPSVVPK RAQEIDAHPS LHAMVTRVKD ESYGVEYIKY
ATVLLQEMTV ELDEDFIYAV LEFSKIPGAS WESTQEEDRL CDDSVDVPQP KQQQAGRDIY
FEVLNIQPMQ LDLSFVRTER VNVEDKTSSR NPVMFFFNVM TMAIGNINDA PVRFNALMLE
NVRVSIPVLI QNISNHYSQE ALYQIHKILG SADFLGNPVG LFNNISSGFA DIFYEPYQGL
IMSDRPEDFG LGLARGAGSF FKKSVYGFTD SFSKVTGSFA KGLAAATMDK QFQDRRRITR
ARNRPKHALF GVTAGANSLI SSVASGVGGL ARKPLEGAEQ EGALGFFKGI GKGVVGLATK
PAIGVLDFAS NISEGVRNTT TVFSSSEASE LDRVRLPRHI AADGIVRPYS QREALGQSWL
KQVDNGKYFD EAYIGHLELP TEDMVVMVTY ARILLIRSRR LQTEWDVPLK DVQTIAKERT
GLSLTLRGGT NGPFIPVAQE SGRAFLYRMV AVAVEEFNRR FRGLE
