ID   HSV2_PICAN              Reviewed;         360 AA.
AC   Q5QA93;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=SVP1-like protein 2;
GN   Name=HSV2;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=15556634; DOI=10.1016/j.febslet.2004.10.055;
RA   Leao-Helder A.N., Krikken A.M., Gellissen G., van der Klei I.J.,
RA   Veenhuis M., Kiel J.A.K.W.;
RT   "Atg21p is essential for macropexophagy and microautophagy in the yeast
RT   Hansenula polymorpha.";
RL   FEBS Lett. 577:491-495(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=14613885; DOI=10.1016/s1567-1356(03)00125-9;
RA   Ramezani-Rad M., Hollenberg C.P., Lauber J., Wedler H., Griess E.,
RA   Wagner C., Albermann K., Hani J., Piontek M., Dahlems U., Gellissen G.;
RT   "The Hansenula polymorpha (strain CBS4732) genome sequencing and
RT   analysis.";
RL   FEMS Yeast Res. 4:207-215(2003).
CC   -!- FUNCTION: Involved in mitochondrial or peroxisomal functions and amino
CC       acid signaling pathways. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC       Note=Vesicular and vacuolar. {ECO:0000250}.
CC   -!- DOMAIN: May contain a beta-propeller domain involved in specific
CC       binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the
CC       association of the protein to the membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR   EMBL; AY756176; AAV74417.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5QA93; -.
DR   SMR; Q5QA93; -.
DR   PhylomeDB; Q5QA93; -.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Membrane; Protein transport; Repeat; Transport;
KW   Vacuole; WD repeat.
FT   CHAIN           1..360
FT                   /note="SVP1-like protein 2"
FT                   /id="PRO_0000051031"
FT   REPEAT          12..50
FT                   /note="WD 1"
FT   REPEAT          191..231
FT                   /note="WD 2"
FT   REPEAT          236..275
FT                   /note="WD 3"
SQ   SEQUENCE   360 AA;  40519 MW;  E9C5DB3E42229A7B CRC64;
     MNTHRPIESV RAHEPAVLNA AFNQDQTCFA VCHESGFQVY NTDPMELRMK RTFSTNGGVG
     LIAMLHRTNY VALVGGGRQP RFPVNKLCIW DDLKKKPSIM LEFMSPILNV LLSRILIVVV
     LKNKVLIHAF ESKPKLLAQH ETYDNEAGVA ELSVNEQTSF LAFPGRAIGQ IQLVDVSPAH
     RDRNLISIIK AHKSRIQCLA ISNSGLLIAS ASQTGTIIRI HDTAKCSLRF ELRRGLDRAT
     VTSIKFSPDD SKLAVLSDKN TLHVYNLTAA DPQPESAMAN RLHLLSAVPL MPTYFRSVWS
     FVSYHIDTKD DAVNDCGVLG WADNESIVVL WKKKGIWEKY VLVENDKWTL VREGWRRFEE