ID   HSV2_NEUCR              Reviewed;         429 AA.
AC   Q7SG97; V5IQQ4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=SVP1-like protein 2;
DE   AltName: Full=Autophagy-related protein 14;
GN   Name=apg-14; Synonyms=hsv2; ORFNames=NCU02466;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(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}.
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; CM002236; ESA43889.1; -; Genomic_DNA.
DR   RefSeq; XP_011392953.1; XM_011394651.1.
DR   AlphaFoldDB; Q7SG97; -.
DR   SMR; Q7SG97; -.
DR   STRING; 5141.EFNCRP00000001933; -.
DR   PRIDE; Q7SG97; -.
DR   EnsemblFungi; ESA43889; ESA43889; NCU02466.
DR   GeneID; 3881242; -.
DR   KEGG; ncr:NCU02466; -.
DR   VEuPathDB; FungiDB:NCU02466; -.
DR   HOGENOM; CLU_025895_0_0_1; -.
DR   InParanoid; Q7SG97; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
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; Reference proteome;
KW   Repeat; Transport; Vacuole; WD repeat.
FT   CHAIN           1..429
FT                   /note="SVP1-like protein 2"
FT                   /id="PRO_0000051030"
FT   REPEAT          10..48
FT                   /note="WD 1"
FT   REPEAT          50..96
FT                   /note="WD 2"
FT   REPEAT          178..218
FT                   /note="WD 3"
FT   REPEAT          223..262
FT                   /note="WD 4"
FT   REGION          262..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  45740 MW;  E6FF81BE910D9902 CRC64;
     MDTRRILEHP VLAPVLSVTF NHDNSCFAVG LDHGFRIYES GSCVLRTSRD FGAGIGMVQM
     LGRTNILGLV GGGRQTKLSR NKLVLWDDKS KKQVGVISAS SLVRGAKMSS KRIVLVLMDR
     VQVYQTAKPH PLLSTYETTD NPLGLCCLSS DRIAFPGRAI GHVQLVEVET GNVSIITAHT
     SALRAMALSQ DGELLATASE MGTIIRVYAT SNCARLYELR RGIDKAIIFS IGFSPSGKYL
     ACTSDKSTLH VFDVTRPGGT RPITSNGGTA YAAGEPSVTG NNRPSSPYSV ASSSGGGGGV
     MVNSNNGGSD MAADDGQGRW GFLSKLPLMP RIFSDPYSFA SAKFEMADEP VSNGSREPLT
     RDGGLAIIGG PLKGNLGWIS ETEMVVIGAG RDPKWEKFAI QEGGQQDGYQ GGGRRLVRVG
     WKRYGGETP