SEC9_SCHPO
ID SEC9_SCHPO Reviewed; 419 AA.
AC O74786;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Protein transport protein sec9;
GN Name=sec9; ORFNames=SPBC26H8.02c;
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).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF LEU-228.
RX PubMed=16272747; DOI=10.1247/csf.30.15;
RA Nakamura T., Kashiwazaki J., Shimoda C.;
RT "A fission yeast SNAP-25 homologue, SpSec9, is essential for cytokinesis
RT and sporulation.";
RL Cell Struct. Funct. 30:15-24(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in cell separation, a final step of cytokinesis
CC and in the assembly of the forespore membrane. May have a role in the
CC transport of secretory proteins to these growing sites.
CC {ECO:0000269|PubMed:16272747}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21094.1; -; Genomic_DNA.
DR PIR; T40014; T40014.
DR RefSeq; NP_596643.1; NM_001022565.2.
DR AlphaFoldDB; O74786; -.
DR SMR; O74786; -.
DR BioGRID; 277149; 2.
DR STRING; 4896.SPBC26H8.02c.1; -.
DR iPTMnet; O74786; -.
DR MaxQB; O74786; -.
DR PaxDb; O74786; -.
DR PRIDE; O74786; -.
DR EnsemblFungi; SPBC26H8.02c.1; SPBC26H8.02c.1:pep; SPBC26H8.02c.
DR GeneID; 2540623; -.
DR KEGG; spo:SPBC26H8.02c; -.
DR PomBase; SPBC26H8.02c; sec9.
DR VEuPathDB; FungiDB:SPBC26H8.02c; -.
DR eggNOG; KOG3065; Eukaryota.
DR HOGENOM; CLU_020823_2_0_1; -.
DR InParanoid; O74786; -.
DR OMA; NDPYARK; -.
DR PhylomeDB; O74786; -.
DR Reactome; R-SPO-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR Reactome; R-SPO-9013026; RHOB GTPase cycle.
DR PRO; PR:O74786; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:PomBase.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
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; IGI:PomBase.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; NAS:PomBase.
DR GO; GO:0006906; P:vesicle fusion; ISO:PomBase.
DR InterPro; IPR000727; T_SNARE_dom.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..419
FT /note="Protein transport protein sec9"
FT /id="PRO_0000213611"
FT DOMAIN 203..265
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 356..418
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 228
FT /note="L->P: In sec9-10; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:16272747"
SQ SEQUENCE 419 AA; 46431 MW; CE1FA0E5196BF959 CRC64;
MKKLFKKKKG VSPHMYMLPE ESNSNTATNA PSYSVGGTTA NSYSSNSYND NNNSNSTYGS
SNNYGNYGSS NNYGSYGASN TYGSNGSSNN YGNYGATNSN GDAGYSITPI RNDPYARKDM
PPMKSSAAVT ERPSMHRSAP SQDTLDLKKQ ELFAGARIQN DDESTTDTIP HNDDGTEGDE
YGEGYRDGYE EDQEVEAIKQ KIQFVKQDSL SSTRNALLMA GNAEQMGLAT LANLGEQTEK
IATAEKELDI SKIHAKRAEE QARELKTLNR SMFAIHVPKP WGKAKRVAAE EARLAAKRDA
ERQDEMLNRQ FAYRSQKRID QAMKDNMKSN KKKGDSKGVS ILERSHYQFE PDAEDDAMEK
EIDGNLDQIG ALATRLKGLA YATGQEIDSQ NARLGSIHDK SDRLDTDVYL NVERLRHIH
