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Database: UniProt
Entry: F1A2I8_DICPU
LinkDB: F1A2I8_DICPU
Original site: F1A2I8_DICPU 
ID   F1A2I8_DICPU            Unreviewed;      3845 AA.
AC   F1A2I8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGC29598.1};
GN   ORFNames=DICPUDRAFT_158801 {ECO:0000313|EMBL:EGC29598.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC29598.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
CC   -!- FUNCTION: Mediates the transfer of lipids between membranes at
CC       organelle contact sites. {ECO:0000256|ARBA:ARBA00033718}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the VPS13 family.
CC       {ECO:0000256|ARBA:ARBA00006545}.
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DR   EMBL; GL871413; EGC29598.1; -; Genomic_DNA.
DR   RefSeq; XP_003293882.1; XM_003293834.1.
DR   STRING; 5786.F1A2I8; -.
DR   EnsemblProtists; EGC29598; EGC29598; DICPUDRAFT_158801.
DR   GeneID; 10505197; -.
DR   KEGG; dpp:DICPUDRAFT_158801; -.
DR   eggNOG; KOG1809; Eukaryota.
DR   InParanoid; F1A2I8; -.
DR   OMA; GPTNILR; -.
DR   OrthoDB; 23713at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblProtists.
DR   GO; GO:0016045; P:detection of bacterium; IEA:EnsemblProtists.
DR   GO; GO:0045053; P:protein retention in Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR   GO; GO:0051593; P:response to folic acid; IEA:EnsemblProtists.
DR   InterPro; IPR015412; Atg2/VPS13_C.
DR   InterPro; IPR026847; VPS13.
DR   InterPro; IPR026854; VPS13-like_N.
DR   InterPro; IPR031645; VPS13_DH-like.
DR   InterPro; IPR031646; VPS13_extend_chorein.
DR   InterPro; IPR031642; VPS13_mid_RBG.
DR   PANTHER; PTHR16166:SF97; INTERMEMBRANE LIPID TRANSFER PROTEIN VPS13F; 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; PF16909; VPS13_DH-like; 1.
DR   Pfam; PF16908; VPS13_ext_chorein; 1.
DR   Pfam; PF16910; VPS13_mid_rpt; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          2..114
FT                   /note="Chorein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12624"
FT   DOMAIN          313..550
FT                   /note="Vacuolar protein sorting-associated protein 13
FT                   extended chorein"
FT                   /evidence="ECO:0000259|Pfam:PF16908"
FT   DOMAIN          901..1018
FT                   /note="VPS13 middle RBG modules"
FT                   /evidence="ECO:0000259|Pfam:PF16910"
FT   DOMAIN          1085..1180
FT                   /note="VPS13 middle RBG modules"
FT                   /evidence="ECO:0000259|Pfam:PF16910"
FT   DOMAIN          3477..3637
FT                   /note="Vacuolar protein sorting-associated protein 13 DH-
FT                   like"
FT                   /evidence="ECO:0000259|Pfam:PF16909"
FT   DOMAIN          3645..3728
FT                   /note="Atg2/VPS13 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09333"
FT   REGION          136..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          856..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1047..1094
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1454..1502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1593..1621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2663..2699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3059..3103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3251..3271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2206..2240
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        146..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..286
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..879
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1454..1478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1593..1610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3059..3088
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3089..3103
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3845 AA;  442671 MW;  39CFD98353973BBC CRC64;
     MFETLVSNLL QRYLGEYIQS LNTENLNISI LKGNVSLENL QLKKRALEKF NLPFTIKEGF
     LGKLSLKIPW NNLKTEPVIV IIDNLYITAS PKSATSWDKE DEELLFQKKI KKLKIYEALK
     EEKRKKILEQ KEKREKRKKL LKEKRQQKQQ QKFEKKKQQQ RQLIKNRNLK NNDDNNNNNN
     NNNNNNNNDI NIFKDDNQNN EDNSINENNT VNDKDNNENN DSHSSPTTLE DGSTYSINRE
     ESEGGSNTDE TNLDEEEDDE DYDDDDDEDY EEYDEEEEEE EEEYDEQLIQ DEIYKGVLKD
     SFDENENQSS SSFADKLRNK IVDNLQIMIY NVHVRFEDSI TNPLSPYCFG ITLEHLLAQS
     SNEEWKPTFI HISQSLVHKL INLQNLSVYW DPHSSDPNLN YKNISDFKTI MTQLIPKKSI
     DQSKNPNHNY LLHPVCGSLK LLINKSLIPN KFIPLYTANF EFDEINLEIE SRQYSGILAL
     VEWFSMLKRG EKYRKFKPKE CGGILKTAKD RWSFALECIR NEVREKLLKW SPKYFEKRRK
     DRLDYIHLYK LKKRKKNITD SNNIRIDQLE RDYSFEDLVY FRSLADAQIK AEDSVRSNPN
     TPLLLSPKST SVYNNQLENK NDDNNSNNNI NNNNNNNNDN NNNSETTKKI EIIDSSSNSN
     NKINPSSKNV NIGNNSNGNN SNGGWFRWLW GGSKKNEEGT TDQESILSTL DLTEQQKREL
     YSTIEYDEHQ VSKNIVYPKD YVKTRINFTM NRGSVAFRLK PPTSPITHFP DSSKSKPKSA
     DLVIELVNMS ISLDKFVESL YVQTILETIF VRDYFTDNTQ FPILMKPILN SYSNNINNNN
     NKNYLSINSS PILKNNKIKN NSGNNNSDNS CYKDNNENNE SGELSSDEEA TKQPLFSMTL
     QQNPLTSESD FSVFIEALPL EIIYNKSMMD SILEFFGNAP SDTLKDIEEA ARNQIKIFKD
     KTTLRIQYEL QNHKSVDLDI NINAPHVLIP ENFTNPSSPI LVLDLGSFSL QRVITHKTSD
     TMPEEIEASS ILRNDLSLYN SNINNENNID YNDNNNNNNN NNNNNNNNYQ ESSASSPSFS
     QSQPIKNSHG SSDGNVYDDE NVTKYLYDLF ELKLGNIQFY LVSGGELIQL VEKFDINFKI
     FKCIIKSQTL LSKLKLFGDL PSLNILLSQK SIEIMIRIIG TLQNDPPEIS NHLISSENLM
     DNQQINDQNN INKNEENEDL IIDIDNRSNS TSSVSNTATL LEGTDENSNI INSSTLIDSM
     ELENPQDQLP ILMIFHTIFE VTFSIPTVSL EVREDLHNKP FVKLILSDIS AQVLKRTFDT
     TVHLSLKKLY IEDLYQDFKN ENFRYLAKSL NEYIPHQDQD LSCSEIAEEE HLINISILSV
     QRNSPQYIGV SQKIDVFFNT LFVNLNKKLV IKIINMIELV EKTIIDTVIQ RREKRNLKKQ
     QHDHENDIII EHQQEQEQEQ QQHNEEQEFK KENIEQKEQN NQQSKQKFKT NSKRKKKEED
     NPMVNITIKM KSLIVNLNED DQSYFMFQVS DLSIYFDIDL ESSMMRFKLG NLEISDISKD
     ASKDLNPLFG TDGEHIIEFY VLTYKNIKLP QFKENNEEKE NDNEEKESDN EEKGKEEEEN
     DFQYDKNGEV INFNSKISVR MTSVKLIVIV SLIEKIIDYF DEIITSQIDH IITESAKGAV
     EIMSNRRIAQ QKRILFEIDV DTPRIIFPKN HISPYVIIAD LGHISIFNQY NINALSPSEQ
     IFIYASSINF HSCKFLNGKV LDSTIEAISN KINIHVNIES FIKVSEQSES KQKVDGEISP
     IHLKISDQQY TLIIAIIKSL IEPNIKQKKR KKRNHRRMES QIKLDNLYQS FINVAQSNQT
     HGIDMNHSNL ISSLPIPTPL PVNTPLSAPL SNNGSTTDIK DQISFHLPHV SLEFFRKNKE
     SVVSLEVIEF ACSIIEYENG NEYSNFSVGS IDLTDTRKSI VNHFRKLIHH QNSPNKNDNS
     GTKKELQVYV CDKRNGDTEV KVLLDSFRGI IVPESLVSMI DFIMPGIKAL SSLSEISPIS
     SPVLDSDAIN NNPLFNQDPT KSIPVKNILE QKNKRSMGQT TLVHIETTNV ELSLVDNPAS
     HESRLLTLKG SVLGKINIQV CEPLTYKDFQ ISVENLELYK CRANNFEQTA ESIIDPFTIT
     ASISLVEGKE YLPIDILIGV NPIHLSISYQ DFLLFLSISN HLNILINNLN RLLNNQQINN
     KNNQQQNNNN NNNNNKEKKE ILRINFQSPS IELTIINDDD NKYFGVLNFK FNNISVEVSQ
     NRIMVGLFLS SNYFNISKSV WEPVIEEWGC KLAIETSNTP VSEIGNIVLT TNQNLNLNIT
     KSLFDTIISS YPVFISALTN SNQENLDSTV ILGYNNNLSQ HYKSQNYHPF LLKNHTGLEI
     QYSVIKLSNE LYKNKNNNNN NNNNNNEKNN FKVLNNLILE NGNEVYLDLR DISLSSKNEK
     DRFKTINNTQ KHRDTTSISL FRVNITVKGF ETITNLPIHK TGIYICNLIP KQNHNNHSNT
     NISSTTSNYE LITPEKQYQQ LVFEIKVSKS SKILIVRSNV LIVNDTDHAI EFLDRPSHTF
     KSSPYILEPN QSKPMSLCKD QSSPSMILSF RPLLDSHQNH QQRWTSPLDC SDSFLHPGTL
     LFDCPPNKFY FLKIDQHLSN YQFEEPTNSS QQQQQQQQQQ QQQQQQQQQQ QQNQHQQYHH
     INKRQYYEYK VENSFEERRS NHIIKIVAPL VIINYFIVPI DVSFYDQESN NIVGKEKIES
     GKRKDIYCAN IEKVIMIKVH MEGYGWSEYI QINQSSPNNI NRQPRKILST SNGKPFYLNV
     HQNEFFGSIQ VSLYSSFSII NNTGLSIQYK LNNINVVGNN KLSTTTTSTT TTKTSFSKTP
     IISDNNEKNE KNLETISIYT DPRNWYSNNN VVCSMFSPIS AHSITTQQLL LQVDNSNWSS
     PISIQLNKFE PITIVKEHRH SEKLFLQFLL YTQIESGSLT KTITISPQFI LINNISNNLY
     YSQKDSSLYK KFFIKPKETL PFHFLEEQLP KKITFRLSEK IEWSGSFNIN KTISFNIQLE
     KPQDDNDQSS SSSDSDSDLS SSSSNSNSSD NEDDDDDDDI TADNDEDFYL PMIQILQEKG
     IYYVIINPET KDYPPYIIQN LISLPISIHQ VDTNDQPIFV YSNHSKRYTW SNPMGTKRLS
     ITIPNTNYKK IVSLDKLQYH QPFPVKYQSS SSKIKDLNIK LEILANGPTN ILRMIDLNDI
     KSINRKEKLT NNNQTQQQEQ QEQQEQQQEE KEQKIIYNNQ TQKQQQQQQE QKNLSNKIKL
     NNFEFYIGGI SVSVIDSIPK ELLFITLKGL QVRFKEINTE QNINISIHSF KVDNQLYHTP
     YPVMISSFNS NTTSPTSHSL IVNFIRSSQY QPKELHQIGI EYIKELRFDI QPFEVQIDEA
     LLFHLVSFIN NVKCSFNNSS IPLTKQEKKD DQNLIIDKIK LPYSNIPLPI TINSKRLYIE
     FLYLPQVDIK LSYRSSPHNR PMIGPWASSA FSALANIDNA SLHLESWKLE HQFVTANGLG
     LSLFYHYKWK VSKILLYSGF LGAPLSLAEN ITRGINDLIN ESSAGFTNPE DFTKGVYKGT
     KSLVSNSLFG IFNSASKFTN TIGTAIAPFS MDENYLQQRD NSYRHSQQPK HVLDGVSNGI
     EKFSEGIAHG LSGLVNQPVK EFQDQGFTGL VKGLGKGLLG TFVKPTVGAI DMINSASQGL
     RNVYSDPSAC KSRSRPPRFI GSDGVIKSFS FEKSFWQELI KVSIKPSLLS SKEFYITHFK
     VYDDKKVPSY LVISTINFYL FNSKFNLSLM IKLWDSNGKS ISYSLLNSIQ NTISSIKMDQ
     TYFIS
//
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