SEC14_SCHPO
ID SEC14_SCHPO Reviewed; 286 AA.
AC Q10137;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sec14 cytosolic factor;
DE AltName: Full=Phosphatidylinositol/phosphatidyl-choline transfer protein;
DE Short=PI/PC TP;
DE AltName: Full=Sporulation-specific protein 20;
GN Name=sec14; Synonyms=spo20; ORFNames=SPAC3H8.10;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11294895; DOI=10.1091/mbc.12.4.901;
RA Nakase Y., Nakamura T., Hirata A., Routt S.M., Skinner H.B.,
RA Bankaitis V.A., Shimoda C.;
RT "The Schizosaccharomyces pombe spo20(+) gene encoding a homologue of
RT Saccharomyces cerevisiae Sec14 plays an important role in forespore
RT membrane formation.";
RL Mol. Biol. Cell 12:901-917(2001).
RN [2]
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 transport of secretory proteins from the Golgi
CC complex. Catalyzes the transfer of phosphatidylinositol and
CC phosphatidylcholine between membranes in vitro. Essential for viability
CC and secretion. {ECO:0000269|PubMed:11294895}.
CC -!- FUNCTION: Has a direct role in controlling cell septation and in
CC forespore membrane formation. {ECO:0000269|PubMed:11294895}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11294895}. Prospore
CC membrane {ECO:0000269|PubMed:11294895}. Note=Nuclear, during meiosis.
CC Associated with the forespore membrane during sporulation. During
CC interphase found at the cell poles and during M-phase is located at
CC both the cell poles and the medial region.
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; CU329670; CAA93167.1; -; Genomic_DNA.
DR PIR; T38768; T38768.
DR RefSeq; NP_593003.1; NM_001018402.2.
DR AlphaFoldDB; Q10137; -.
DR SMR; Q10137; -.
DR BioGRID; 280042; 63.
DR STRING; 4896.SPAC3H8.10.1; -.
DR iPTMnet; Q10137; -.
DR MaxQB; Q10137; -.
DR PaxDb; Q10137; -.
DR PRIDE; Q10137; -.
DR EnsemblFungi; SPAC3H8.10.1; SPAC3H8.10.1:pep; SPAC3H8.10.
DR GeneID; 2543628; -.
DR KEGG; spo:SPAC3H8.10; -.
DR PomBase; SPAC3H8.10; -.
DR VEuPathDB; FungiDB:SPAC3H8.10; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_014001_0_1_1; -.
DR InParanoid; Q10137; -.
DR OMA; CECAGGC; -.
DR PhylomeDB; Q10137; -.
DR PRO; PR:Q10137; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IDA:PomBase.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:PomBase.
DR GO; GO:0030437; P:ascospore formation; IMP:PomBase.
DR GO; GO:0031322; P:ascospore-type prospore-specific spindle pole body remodeling; IMP:PomBase.
DR GO; GO:0048193; P:Golgi vesicle transport; IMP:PomBase.
DR GO; GO:0120010; P:intermembrane phospholipid transfer; ISM:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 4: Predicted;
KW Membrane; Nucleus; Protein transport; Reference proteome; Transport.
FT CHAIN 1..286
FT /note="Sec14 cytosolic factor"
FT /id="PRO_0000210742"
FT DOMAIN 94..267
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 32746 MW; EAA6C59189FE3EFF CRC64;
MSETISDPYP LTNPNAPLGH PGHLNSTQQA TLDSMRLELQ KLGYTERLDD ATLLRFLRAR
KFNLQQSLEM FIKCEKWRKE FGVDDLIKNF HYDEKEAVSK YYPQFYHKTD IDGRPVYVEQ
LGNIDLKKLY QITTPERMMQ NLVYEYEMLA LKRFPACSRK AGGLIETSCT IMDLKGVGIT
SIHSVYSYIR QASSISQDYY PERMGKFYVI NAPWGFSSAF NLIKGFLDEA TVKKIHILGS
NYKSALLEQI PADNLPAKLG GNCQCPGGCE LSDAGPWHEE QWMNKN
