SCS22_SCHPO
ID SCS22_SCHPO Reviewed; 319 AA.
AC Q10484;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Vesicle-associated membrane protein-associated protein scs22;
DE Short=VAMP-associated protein scs22;
GN Name=scs22; ORFNames=SPAC17C9.12;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-236; SER-237 AND SER-281, AND
RP IDENTIFICATION BY 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).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23041194; DOI=10.1016/j.cub.2012.08.047;
RA Zhang D., Vjestica A., Oliferenko S.;
RT "Plasma membrane tethering of the cortical ER necessitates its finely
RT reticulated architecture.";
RL Curr. Biol. 22:2048-2052(2012).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26877082; DOI=10.1016/j.cub.2015.12.070;
RA Zhang D., Bidone T.C., Vavylonis D.;
RT "ER-PM Contacts Define Actomyosin Kinetics for Proper Contractile Ring
RT Assembly.";
RL Curr. Biol. 26:647-653(2016).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29290560; DOI=10.1016/j.cub.2017.11.055;
RA Ng A.Y.E., Ng A.Q.E., Zhang D.;
RT "ER-PM contacts restrict exocytic sites for polarized morphogenesis.";
RL Curr. Biol. 28:146-153(2018).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32023460; DOI=10.1016/j.celrep.2019.12.098;
RA Ng A.Q.E., Ng A.Y.E., Zhang D.;
RT "Plasma membrane furrows control plasticity of ER-PM contacts.";
RL Cell Rep. 30:1434-1446(2020).
RN [7]
RP FUNCTION, AND INTERACTION WITH EPR1.
RX DOI=10.1016/j.molcel.2020.07.019;
RA Zhao D., Zou C.X., Liu X.M., Jiang Z.D., Yu Z.Q., Suo F., Du T.Y.,
RA Dong M.Q., He W., Du L.L.;
RT "A UPR-induced soluble ER-phagy receptor acts with VAPs to confer ER stress
RT resistance.";
RL Mol. Cell 79:1-15(2020).
CC -!- FUNCTION: Vesicle-associated membrane protein-associated protein (VAP)
CC implicated in maintaining the cortical endoplasmic reticulum (ER)-
CC plasma membrane (PM) attachment (PubMed:23041194, PubMed:26877082,
CC PubMed:29290560, PubMed:32023460). ER-PM contacts function to modulate
CC the distribution of contractile ring components to ensure robust ring
CC assembly (PubMed:26877082). ER-PM contacts function also in controlling
CC exocytosis and maintenance of cell polarity regulating cell shape
CC (PubMed:29290560). VAPs play an important role in regulating eisosome
CC assembly (PubMed:32023460). VAPs also contribute to ER-phagy by
CC tethering atg8 to the ER membrane, but also by maintaining the ER-
CC plasma membrane contact (Ref.7). {ECO:0000269|PubMed:23041194,
CC ECO:0000269|PubMed:26877082, ECO:0000269|PubMed:29290560,
CC ECO:0000269|PubMed:32023460, ECO:0000269|Ref.7}.
CC -!- SUBUNIT: Interacts with epr1. {ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23041194}; Single-pass type IV membrane protein
CC {ECO:0000255}. Note=Localizes at the cortical endoplasmic reticulum-
CC plasma membrane contact sites. {ECO:0000269|PubMed:23041194}.
CC -!- DOMAIN: The MSP domain is required for binding to the FFAT motif of
CC target proteins. {ECO:0000250|UniProtKB:P40075}.
CC -!- DISRUPTION PHENOTYPE: Leads to he dissociation of the cortical
CC endoplasmic reticulum (ER) from the cell periphery and its accumulation
CC in the cytoplasm, in particular in the vicinity of cell tips; when scs2
CC is also deleted (PubMed:23041194, PubMed:26877082, PubMed:29290560,
CC PubMed:32023460). Affects contractile ring assembly and displays severe
CC cytokinetic defects; when scs2 is also deleted (PubMed:26877082).
CC {ECO:0000269|PubMed:23041194, ECO:0000269|PubMed:26877082,
CC ECO:0000269|PubMed:29290560, ECO:0000269|PubMed:32023460}.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAA97357.1; -; Genomic_DNA.
DR PIR; T11592; T11592.
DR RefSeq; NP_594594.1; NM_001020022.2.
DR AlphaFoldDB; Q10484; -.
DR SMR; Q10484; -.
DR BioGRID; 278654; 13.
DR STRING; 4896.SPAC17C9.12.1; -.
DR iPTMnet; Q10484; -.
DR MaxQB; Q10484; -.
DR PaxDb; Q10484; -.
DR PRIDE; Q10484; -.
DR EnsemblFungi; SPAC17C9.12.1; SPAC17C9.12.1:pep; SPAC17C9.12.
DR GeneID; 2542179; -.
DR KEGG; spo:SPAC17C9.12; -.
DR PomBase; SPAC17C9.12; -.
DR VEuPathDB; FungiDB:SPAC17C9.12; -.
DR eggNOG; KOG0439; Eukaryota.
DR HOGENOM; CLU_032848_1_1_1; -.
DR InParanoid; Q10484; -.
DR OMA; VPQIHNT; -.
DR Reactome; R-SPO-9013106; RHOC GTPase cycle.
DR PRO; PR:Q10484; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0033149; F:FFAT motif binding; IBA:GO_Central.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IPI:PomBase.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IBA:GO_Central.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IMP:PomBase.
DR GO; GO:0051685; P:maintenance of ER location; IMP:PomBase.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:PomBase.
DR GO; GO:0061709; P:reticulophagy; IMP:PomBase.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like_sf.
DR InterPro; IPR016763; VAP.
DR PANTHER; PTHR10809; PTHR10809; 1.
DR Pfam; PF00635; Motile_Sperm; 1.
DR PIRSF; PIRSF019693; VAMP-associated; 1.
DR SUPFAM; SSF49354; SSF49354; 1.
DR PROSITE; PS50202; MSP; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..319
FT /note="Vesicle-associated membrane protein-associated
FT protein scs22"
FT /id="PRO_0000213482"
FT TOPO_DOM 1..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 299..319
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 1..121
FT /note="MSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT REGION 127..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 319 AA; 34005 MW; 2B7E6C5E1099F077 CRC64;
MALECDSTIV FPRPLTRLVK CDLELRNTAP YPIGFKVKTT APKQYCVRPN GGRIEANSAV
SVEVILQPLD HEPAPGTKCR DKFLVQSTEL KPELQGMDIA DIWTQVSKAN ISERKIRCVY
SEGPSTANAH ANAHHQPAQT TTTSIPTSAT DNYTTVNGNV NQSYSKGIDG TALPSTHANP
VAAPSTATTQ HTQLPKTSAV SHQKPHEAPS TAVKAPTATV AENEPYPKPQ SVPTTTSPNN
ENNALRSTAN VINNTRQSTA TSPSMFAGNS GNQIGLARVS SSFGRPTSGA KVVPQIHNTV
TVQTAFLLAI ICFLIGLLF
