PEP7_SCHPO
ID PEP7_SCHPO Reviewed; 536 AA.
AC O13786;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Vacuolar segregation protein pep7;
GN Name=pep7; Synonyms=vac1; ORFNames=SPAC17G6.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Required for vacuole segregation and vacuole protein sorting.
CC Possibly part of a complex which tethers the vacuole membrane to
CC microtubules, either directly or via kinesin or dynein-like motor
CC proteins. Probably functions in several interorganelle traffic pathways
CC (By similarity). {ECO:0000250}.
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DR EMBL; CU329670; CAB16219.1; -; Genomic_DNA.
DR PIR; T37840; T37840.
DR RefSeq; NP_594255.1; NM_001019678.2.
DR AlphaFoldDB; O13786; -.
DR SMR; O13786; -.
DR BioGRID; 278885; 8.
DR STRING; 4896.SPAC17G6.08.1; -.
DR iPTMnet; O13786; -.
DR MaxQB; O13786; -.
DR PaxDb; O13786; -.
DR PRIDE; O13786; -.
DR EnsemblFungi; SPAC17G6.08.1; SPAC17G6.08.1:pep; SPAC17G6.08.
DR GeneID; 2542423; -.
DR KEGG; spo:SPAC17G6.08; -.
DR PomBase; SPAC17G6.08; pep7.
DR VEuPathDB; FungiDB:SPAC17G6.08; -.
DR eggNOG; KOG1842; Eukaryota.
DR HOGENOM; CLU_026440_1_0_1; -.
DR InParanoid; O13786; -.
DR OMA; GLWCRVC; -.
DR PhylomeDB; O13786; -.
DR Reactome; R-SPO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:O13786; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0010009; C:cytoplasmic side of endosome membrane; ISO:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:PomBase.
DR GO; GO:0006896; P:Golgi to vacuole transport; ISO:PomBase.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISO:PomBase.
DR GO; GO:0006906; P:vesicle fusion; ISO:PomBase.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR021565; Rbsn_Rab-bd.
DR InterPro; IPR036531; Rbsn_Rab-bd_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 2.
DR Pfam; PF11464; Rbsn; 1.
DR SMART; SM00064; FYVE; 2.
DR SUPFAM; SSF140125; SSF140125; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS50178; ZF_FYVE; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..536
FT /note="Vacuolar segregation protein pep7"
FT /id="PRO_0000046857"
FT ZN_FING 39..62
FT /note="C2H2-type"
FT ZN_FING 136..201
FT /note="FYVE-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT ZN_FING 275..332
FT /note="FYVE-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 536 AA; 62434 MW; 952A483E1AFDF11A CRC64;
MQNGKRRIGV RISSNLSNHS GTNLSTSAQS DSSNIVKATE CPICGLELPN LSALNDHLDV
THFNDNEKIH KRQDSINSWL TRTLNGASAL QMKAAQRLWR MEPYEQNGDS SGAVGLEATK
LTDSLVVKNH WQPEVPDMVC HDPMCDKLLN FINGHIHCRK CGYIFCNFHS MYQIKLSIHA
TYDSENGFWC RVCRECYEGR PGYNDSNGLI RSRFQTFETF RKPLADKRRI EFLRLSKRMK
KLEELWTSEN VSMLDALLLN KAKRLEQSIV HWQDDSVVQI CPECNNSFTL TRRRRHCRLC
GRVICRFCVL EISLPQHPQP LLICMSCNQN YFRNVLYQTE RSKSLGYIRH IEHLQVFRQA
MVNYYRLYED SLSELLSGEI ITEATLKIVK DRRKKFLELC VKYDGTMKKI ANHPSSNDAE
EQFKQNVVNE AKRYLQETIL RLQAIPYHLQ VGQAWTSESE RELEKKKEQV EKKQEELMQT
RIVLEEQVFL VENMIEDAKA KRKFSEVETL LSSLAPLHEE IHSITEKIHD LDLFDI
