SPO14_SCHPO
ID SPO14_SCHPO Reviewed; 395 AA.
AC Q10659; Q9HFE9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Membrane glycoprotein spo14;
DE AltName: Full=SEC12-like protein;
DE AltName: Full=Sporulation-specific protein 14;
GN Name=spo14; Synonyms=st11, stl1; ORFNames=SPBC3H7.01, SPBP16F5.01c;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1396601; DOI=10.1002/j.1460-2075.1992.tb05514.x;
RA d'Enfert C., Gensse M., Gaillardin C.;
RT "Fission yeast and a plant have functional homologues of the Sar1 and Sec12
RT proteins involved in ER to Golgi traffic in budding yeast.";
RL EMBO J. 11:4205-4211(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12631727; DOI=10.1091/mbc.e02-08-0504;
RA Nakamura-Kubo M., Nakamura T., Hirata A., Shimoda C.;
RT "The fission yeast spo14(+) gene encoding a functional homologue of budding
RT yeast Sec12 is required for the development of forespore membranes.";
RL Mol. Biol. Cell 14:1109-1124(2003).
RN [3]
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 the formation of transport vesicles from the ER.
CC This function involves the cytoplasmic domain of the protein, which is
CC thought to interact with the small GTP-binding protein sar1.
CC {ECO:0000269|PubMed:12631727, ECO:0000269|PubMed:1396601}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein. Golgi apparatus, cis-Golgi network membrane;
CC Single-pass type II membrane protein. Note=Cycling between endoplasmic
CC reticulum and the early Golgi.
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DR EMBL; M95798; AAA35345.1; -; mRNA.
DR EMBL; AB036755; BAA89460.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20297.1; -; Genomic_DNA.
DR PIR; S28606; S28606.
DR RefSeq; XP_001713132.1; XM_001713080.2.
DR AlphaFoldDB; Q10659; -.
DR SMR; Q10659; -.
DR BioGRID; 277512; 2.
DR STRING; 4896.SPBC3H7.01.1; -.
DR MaxQB; Q10659; -.
DR PaxDb; Q10659; -.
DR PRIDE; Q10659; -.
DR EnsemblFungi; SPBC3H7.01.1; SPBC3H7.01.1:pep; SPBC3H7.01.
DR PomBase; SPBC3H7.01; spo14.
DR VEuPathDB; FungiDB:SPBC3H7.01; -.
DR eggNOG; KOG0771; Eukaryota.
DR HOGENOM; CLU_706283_0_0_1; -.
DR InParanoid; Q10659; -.
DR OMA; RVEIYDW; -.
DR Reactome; R-SPO-204005; COPII-mediated vesicle transport.
DR PRO; PR:Q10659; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0030437; P:ascospore formation; IMP:PomBase.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IMP:PomBase.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:PomBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:PomBase.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045260; Sec12-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR23284; PTHR23284; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Repeat; Signal-anchor; Sporulation;
KW Transmembrane; Transmembrane helix; Transport; WD repeat.
FT CHAIN 1..395
FT /note="Membrane glycoprotein spo14"
FT /id="PRO_0000051225"
FT TOPO_DOM 1..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..395
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 250..285
FT /note="WD 1"
FT REPEAT 290..326
FT /note="WD 2"
SQ SEQUENCE 395 AA; 45078 MW; 7E09AAA50BD5F2C0 CRC64;
MAELHLSFPA YSLCWINNHQ MAVGGGGGTT KSGVKNKLKL LSYEDYEPEV GEGHTKFIEH
GEIELKHSDD AVMSLGYFKN ELIAGINNTI DGKLIDHLRL YGRKDKLFEE KNALRLTDFD
NDEQYQRLCL FEPLHDAICI SCTNKSFFII SKNDHKVLFE KHGSDVYDVS STEDKLAIAV
DDRVEIYDWN TFELVQVLYM PVERATVRGV SFLPNQSIVA AYNYIKDSKR FASLVRFDYS
SKNQLWRFGM IRDLKNAKGV TCFCCDKENG MIIVAGADCS IRFMSLDLTK LSQVYKHSLP
VTDMQLSPDS EALVSVSADG LLCLQFVGKF KNLSAVKLED AGVILRLSLM FPFVLAILYF
YLQLLFPDEK LDAIHRFFSF ILHIFSKYTI RNYDL
