VP13A_MACFA
ID VP13A_MACFA Reviewed; 3093 AA.
AC Q9BGZ0; A0A2K5U8A0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Intermembrane lipid transfer protein VPS13A {ECO:0000250|UniProtKB:Q96RL7};
DE AltName: Full=Chorea-acanthocytosis protein homolog {ECO:0000305};
DE AltName: Full=Chorein {ECO:0000305};
DE AltName: Full=Vacuolar protein sorting-associated protein 13A {ECO:0000305};
GN Name=VPS13A; Synonyms=CHAC; ORFNames=QflA-11022;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000312|Ensembl:ENSMFAP00000008576}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2475-3093.
RC TISSUE=Frontal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the transfer of lipids between membranes at
CC organelle contact sites (By similarity). Required for the formation or
CC stabilization of ER-mitochondria contact sites which enable transfer of
CC lipids between the ER and mitochondria (By similarity). Negatively
CC regulates lipid droplet size and motility (By similarity). Required for
CC efficient lysosomal protein degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q07878, ECO:0000250|UniProtKB:Q96RL7}.
CC -!- SUBUNIT: Interacts (via FFAT motif) with VAPA and VAPB (By similarity).
CC Interacts with RAB7A (By similarity). Interacts with XK (By
CC similarity). {ECO:0000250|UniProtKB:Q96RL7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q96RL7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RL7}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96RL7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RL7}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q96RL7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RL7}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q96RL7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RL7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q96RL7}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q5H8C4}. Cytoplasmic vesicle, secretory vesicle,
CC neuronal dense core vesicle {ECO:0000250|UniProtKB:Q5H8C4}.
CC Note=Localizes at mitochondria-endosomes and mitochondria-endoplasmic
CC reticulum contact sites. {ECO:0000250|UniProtKB:Q96RL7}.
CC -!- DOMAIN: The FFAT motif is required for interaction with VAPA and VAPB
CC and its localization to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q96RL7}.
CC -!- SIMILARITY: Belongs to the VPS13 family. {ECO:0000305}.
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DR EMBL; AB055267; BAB21891.1; -; mRNA.
DR AlphaFoldDB; Q9BGZ0; -.
DR STRING; 9541.XP_005582028.1; -.
DR Ensembl; ENSMFAT00000021483; ENSMFAP00000008576; ENSMFAG00000001206.
DR VEuPathDB; HostDB:ENSMFAG00000001206; -.
DR eggNOG; KOG1809; Eukaryota.
DR GeneTree; ENSGT00950000183083; -.
DR OrthoDB; 4159at2759; -.
DR Proteomes; UP000233100; Chromosome 15.
DR Bgee; ENSMFAG00000001206; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0099013; C:neuronal dense core vesicle lumen; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:1905146; P:lysosomal protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR015412; Autophagy-rel_C.
DR InterPro; IPR026847; VPS13.
DR InterPro; IPR026854; VPS13-like_N.
DR InterPro; IPR031645; VPS13_C.
DR InterPro; IPR031642; VPS13_mid_rpt.
DR InterPro; IPR031646; VPS13_N2.
DR InterPro; IPR009543; VPS13_VAB.
DR PANTHER; PTHR16166; PTHR16166; 1.
DR Pfam; PF09333; ATG_C; 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; 2.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW Lipid droplet; Lipid transport; Lysosome; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Transport.
FT CHAIN 1..3093
FT /note="Intermembrane lipid transfer protein VPS13A"
FT /id="PRO_0000106278"
FT DOMAIN 3..116
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REPEAT 373..406
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT DOMAIN 2209..2454
FT /note="SHR-BD"
FT /evidence="ECO:0000255"
FT REPEAT 2860..2898
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REGION 2953..3027
FT /note="Required for lipid droplet localization"
FT /evidence="ECO:0000250|UniProtKB:Q96RL7"
FT MOTIF 842..848
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:Q96RL7"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5H8C4"
FT MOD_RES 1416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RL7"
SQ SEQUENCE 3093 AA; 350686 MW; E5F1A336C37242D2 CRC64;
MVFESVVVDV LNRFLGDYVV DLDTSQLSLG IWKGAVALKN LQIKENALSQ LDVPFKVKVG
HIGNLKLIIP WKNLYSQPVE AVLEEIYLLI VPSSRIKYDP IKEEKQLMEA KQQELKRIEE
AKQKVVDQEQ HLLEKQDTFA EKLVTQIIKN LQVKISSIHI RYEDDITNRD KPLSFGISLQ
NLSMQTTDQY WVPCLHDETE KLVRKLIRLD NLFAYWNVKS QMFYLNDYDD SLDDLRNGIV
NENIVPEGYD FVFRPISANA KLVMNRRSDF DFSAPKINLD VELHNIAIEF NKPQYFSIME
LLESVDMMTQ NMPYRKFRPD VPLHHHAREW WAYAIHGVLE VNVCPRLRMW SWKHIRKHRG
KMKQYKELYK KKLTSKKPPG ELLVSLEELE KTLDVLNITI ARQQAEVEVK KAGYKIYKEG
VKDPEDNKGW FSWLWSWSEQ NTNEQQPDVK PGILEEMLTP EEKALLYEAI GYSETAVDPT
LPKTFEALKF FVHLKSMSVV LRENHQKPEL IDIVIEEFST LIVQRPGAQA VKFETKIDSF
HITGLPDNSE KPRLLSSLDD AMSLFQITFE INPLDETVTQ RCIIEAEPLE IIYDARTVNS
IVEFFRPPKE VHLAQLTSAT LTKLEEFRNK TATGLLYIIE TQKVLDLRIN LKASYIIVPQ
DGIFSPTSNL LLLDLGHLKV TSKSRSELPD VKQGEANLKE IMDIAYDSFD IQLTSIQLLY
SRVGDNWREA RKLNVSTQHI LVPMHFNLEL SKAMVFMDVR MPKFKIFGKL PLISLRISDK
KLQGIMELVE SIPKPEPVTE VSAPVKSFQI QTSTSLGTSQ ISQKIIPLLE LPSVSEDDSE
EEFFDAPCSP LDEPLQFPTG VKSIRTRKLQ KQDCSVNMTT FKIRFEVPKV LIEFYHLVGD
CELSVVEIHV LGLGTEIEIR TYDLKANAFL KEFCLKCPEY LDENRKPVYL VTTLDNTMED
LLTLEYVKAE KNVPNLKSTY NNVLQLIKVN FSSLDIHLHT EALLNTINYL HNILPQSEEK
SAPVSTTETE DKGDVIKKLA LKLSTNEDII TLQILAELSC LQIFIQDQKR NISEIKIEGL
DSEMIMRPSE TEINAKLRNI IVLDSDITAI YKKAVYITGK EVFSFKMVSY MDATAGSAYT
DMNVVDIQVN LVVGCIEVVF VTKFLCSILA FIDNFQAAKQ ALAEATVQAA GMAATGVKEL
ARRSSRMALD INIKAPVVVI PQSPVSENVF VADFGLITMT NTFHMITESQ SSPPPVIDLI
TIKLSEMRLY RSQFINDAYQ EVLDLLLPLN LEVVVERNLC WEWYQEVPCF NVNAQLKPME
FILSQEDITT IFKTLHGNIW YEKDGSASPA VTKDQYSATS GVTTNASHHS GGATVVTAAV
VEVHSRASLV KTTLNVSFKT DYLTMVLYSP GPKQASFTDV RDPSLKLAEF KLENIISTLK
MYTDDSTFSS FSLKNCILDD KRPHVKKATP RMIGLTVGFD KKDMMDIKYR KVRDGCVTDA
VFQEMYICAS VEFLQTVANV FLEAYTTGTA VETSVQTWTA KEEVPTQELE KWEINVIIKN
PEIVFVADMT KNDAPALVIT TQCEICYKGN LENSTMTAAI KDLQVRACPF LPIKRKGKVT
TVLQPCDLFY QTTQAGTDPQ VIDMSVKSLT LKVSPVIINT MITITSALYT TKETIPEETA
SSTAQLWEKK DTKTLKMWFL EESNETEKIA PTTELIPKGE MIKMNIDSIF IVLEAGIGHR
TVPMLLAKSR FSGEGKNWSS LINLHCQLEL EVHYYNEMFG VWEPLLEPLE IDQTEDFRPW
NLGIKMKKKA KKAIVESDPE EENYKVPEYK TVISFHSKDQ LNITLSKCGL VMLNNLAKAF
TEAATGSSAD FVKDLAPFII LNSLGLTISV SPSDSFSVLN IPMAKSYVLK NEESLSMDYV
RTKDNDHFNA MTSLSSKLFF ILLTPVNHST ADKIPLTKVG RRLYTVRHRE SGVERSIVCQ
IDTVEGSKKV TIRSPVQIRN HFSVPLSVYE GDTLLGTASP ENEFNIPLGS YRSFLFLKPE
DEDYQRCEGI DFEEIVKNDG ALLKKKCRSQ NPSKKSFLIN IVPEKDNLTS LSVYSEDGWD
LPYIMHLWPP ILLRNLLPYK IAYYIEGIEN SVFTLSEGHS AQICTVQLDK ARLRLKLLDY
LNHDWKSEYH IKPNQQDISF VNFTCITEME KTDLDIAVHM TYNTGQTVVA FHSPYWMVNK
TGRMLQYKAD GIHRKHPPNY KKPVLFSFQP NHFFNNNKVQ LMVTDSELSD QFSIDTVGSH
GAVKCKGLKM DYQVGVTIDL SSFNITRIVT FTPFYMIKNK SKYRISVAEE GTDKWLSLDL
EQCIPFWPED ASSKLLIQVE GSEDPPKRIY FNKQENCILL RLDNELGGII AEVNLAEHST
VITFLDYHDG AATFLLINHT KNELVQYNQS SLSEIEDSLP PGKAVFYTWA DPVGSRRLKW
RCRKSHGEVT QKDDMMMPID LGKKTIYLVS FFEGLQRIIL FTEDPKVFKV TYESEKAELA
EQEIAVALQD VGISLVNNYT KQEVAYIGIT SSDVVWETKP KKKARWKPMS VKHTEKLERE
FKEYTESSPS EDKVIELDTN IPVRLTPTGH NMKILQPRVI ALRRNYLPAL KVEYNTSAHQ
SSFRIQIYRI QIQNQIHGAV FPFVFYPVKP PKSVTMDSAP KPFTDVSIVM RSAGHSQISR
IKYFKVLIQE MDLRLDLGFI YALTDLMTEA EVTENTEVEL FHKDIEAFKE EYKTASLVDQ
SQVSLYEYFH ISPLKLHLSV SLSSGGEEAK DSKQNGGLIP VHSLNLLLKS IGATLTDVQD
VVFKLAFFEL NYQFHTTSDL QSEVIRHYSK QAIKQMYVLI LGLDVLGNPF GLIREFSEGV
EAFFYEPYQG AIQGPEEFVE GMALGLKALV GGAVGGLAGA ASKITGAMAK GVAAMTMDED
YQQKRREAMN KQPAGFREGI TRGGKGLVSG FVSGITGIVT KPIKGAQKEG AAGFFKGVGK
GLVGAVARPT GGIIDMASST FQGIKRATET SEVESLRPPR FFNEDGVIRP YRLRDGTGNQ
MLQKIQFCRE WIMTHSSSSD DDDGDDDESD LNR
