ID   W6MVT1_9ASCO            Unreviewed;       648 AA.
AC   W6MVT1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Vacuolar protein sorting-associated protein 52 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=KUCA_T00002462001 {ECO:0000313|EMBL:CDK26490.1};
OS   Kuraishia capsulata CBS 1993.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX   NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK26490.1};
RN   [1] {ECO:0000313|EMBL:CDK26490.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26490.1};
RA   Genoscope - CEA;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDK26490.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26490.1};
RA   Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA   Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA   Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA   Gabaldon T., Wincker P., Dujon B.;
RT   "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT   features among budding yeasts (/Saccharomycotina/).";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the VPS52 family.
CC       {ECO:0000256|ARBA:ARBA00008180}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HG793127; CDK26490.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6MVT1; -.
DR   STRING; 1382522.W6MVT1; -.
DR   HOGENOM; CLU_010797_1_0_1; -.
DR   OrthoDB; 2723231at2759; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007258; Vps52.
DR   InterPro; IPR048361; Vps52_C.
DR   InterPro; IPR048319; Vps52_CC.
DR   PANTHER; PTHR14190; SUPPRESSOR OF ACTIN MUTATIONS 2/VACUOLAR PROTEIN SORTING 52; 1.
DR   PANTHER; PTHR14190:SF7; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 52 HOMOLOG; 1.
DR   Pfam; PF20655; Vps52_C; 1.
DR   Pfam; PF04129; Vps52_CC; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          115..279
FT                   /note="Vps52 coiled-coil"
FT                   /evidence="ECO:0000259|Pfam:PF04129"
FT   DOMAIN          371..638
FT                   /note="Vps52 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20655"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          135..169
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   648 AA;  75245 MW;  8140D61583888F30 CRC64;
     MSRSAYFPRN DQQEQATPHH HLQHRISRRS ISKHQNADIH RPPRMEILSQ ILNPEWEIGS
     SETEDVDMGP IKSYFADPDA ITDVSSLQEL LFLSTLNEDY AMTAEDYDAQ FAKFTHYHET
     IQQARVFLKP LFDYLLNFEK ELTKLSAEME FLQKRSNALN EQIEDKKQID LKLTPIVNDL
     AIPPEIVRSL VNDDITSKWI ENLRFISEKK ELYEKYANEY GEFKSLVELR KVLELMTLKA
     VERVRDFIIR KIKLLRVNGI SSQVVQKDLL DVREIYPFLQ QHNTNLAQEL RQAYVYTMRW
     YYHQSFVKYL YSLERLNTVH VDKIALLGSN DDEYVNNSGF GFLNIYSHSG TASTSSSLST
     SKGNGKHTLY QNDYLNLGKR GQIISLEDQT VIIGQIAETS QMTYWLETGF RNFNLALLDN
     VSVEYLFLSE FFQLSNFEQV NDLFKIVFQP TLSVGINYTR SLIAETYDVY GVLICIRLSQ
     ALEYELQHRR VPVLEDYFNL QMITLWPKFQ KIIDANCDSM RKVISKSSSF FSSAHSSMGS
     NSSMPLALTQ QFGKLLSGLL NLTTNTVFET EQNEPLSSSI IRLRNDFESV LTKISNNLGK
     DSRKKELFLY NNYFLILTIL NEIEGKLADP EREHFQTLVK AYEPRLPK
//