SEC22_SCHPO
ID SEC22_SCHPO Reviewed; 215 AA.
AC Q9Y7L0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein transport protein sec22;
GN Name=sec22; ORFNames=SPBC2A9.08c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=20537132; DOI=10.1186/gb-2010-11-6-r60;
RA Han T.X., Xu X.Y., Zhang M.J., Peng X., Du L.L.;
RT "Global fitness profiling of fission yeast deletion strains by barcode
RT sequencing.";
RL Genome Biol. 11:R60.1-R60.13(2010).
CC -!- FUNCTION: Nonessential SNARE involved in targeting and fusion of ER-
CC derived transport vesicles with the Golgi complex as well as Golgi-
CC derived retrograde transport vesicles with the ER. {ECO:0000250}.
CC -!- SUBUNIT: Component of two distinct SNARE complexes consisting of sed5,
CC bos1, bet1 and sec22 or ufe1, use1, sec20 and sec22. Ykt6 can probably
CC replace sec22 as subunit of either complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
CC Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Leads to sensitivity to thiabendazole,
CC camptothecin, DNA damaging agents, and microtubule depolymerizing
CC drugs. {ECO:0000269|PubMed:20537132}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; CU329671; CAB39850.2; -; Genomic_DNA.
DR PIR; T40099; T40099.
DR RefSeq; NP_596218.2; NM_001022137.2.
DR AlphaFoldDB; Q9Y7L0; -.
DR SMR; Q9Y7L0; -.
DR BioGRID; 276838; 3.
DR STRING; 4896.SPBC2A9.08c.1; -.
DR iPTMnet; Q9Y7L0; -.
DR MaxQB; Q9Y7L0; -.
DR PaxDb; Q9Y7L0; -.
DR PRIDE; Q9Y7L0; -.
DR EnsemblFungi; SPBC2A9.08c.1; SPBC2A9.08c.1:pep; SPBC2A9.08c.
DR GeneID; 2540308; -.
DR KEGG; spo:SPBC2A9.08c; -.
DR PomBase; SPBC2A9.08c; sec22.
DR VEuPathDB; FungiDB:SPBC2A9.08c; -.
DR eggNOG; KOG0862; Eukaryota.
DR HOGENOM; CLU_054453_4_1_1; -.
DR InParanoid; Q9Y7L0; -.
DR OMA; ERSYPRK; -.
DR Reactome; R-SPO-204005; COPII-mediated vesicle transport.
DR Reactome; R-SPO-5694530; Cargo concentration in the ER.
DR Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q9Y7L0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:PomBase.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; ISS:PomBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; NAS:PomBase.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISS:PomBase.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
DR CDD; cd14824; Longin; 1.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR044565; Sec22.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45837; PTHR45837; 1.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 3: Inferred from homology;
KW Coiled coil; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..215
FT /note="Protein transport protein sec22"
FT /id="PRO_0000206767"
FT TOPO_DOM 1..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 9..118
FT /note="Longin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00231"
FT DOMAIN 133..193
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
SQ SEQUENCE 215 AA; 24903 MW; 666A803AC412CC39 CRC64;
MVKSTTVTRL DGLPLAASVD DESTERNLES HKKQAKLILK RLSPTSEKRA SIESGDYTFH
YLIDNGICYL CICEQSYPRK LAFSYLEELA GEFWNSFGEE ALQPGLRPYA FVQFDTFMQK
SKRVYNTPRA NDNLDKLNTE LKDVTRVMTK NIEDLLYRGD SLEKMADLSS DLRYSSAKYK
KAARRVNLEA LWRQYGPVSI IALLFLIFVY WRFFA
