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 27-MAR-2024, entry version 125. 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}. 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; 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; 14. DR STRING; 284812.Q10484; -. DR iPTMnet; Q10484; -. DR MaxQB; Q10484; -. DR PaxDb; 4896-SPAC17C9-12-1; -. DR EnsemblFungi; SPAC17C9.12.1; SPAC17C9.12.1:pep; SPAC17C9.12. DR GeneID; 2542179; -. DR KEGG; spo:SPAC17C9.12; -. DR PomBase; SPAC17C9.12; scs22. DR VEuPathDB; FungiDB:SPAC17C9.12; -. DR eggNOG; KOG0439; Eukaryota. DR HOGENOM; CLU_032848_1_1_1; -. DR InParanoid; Q10484; -. DR OMA; VPQIHNT; -. 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: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; Immunoglobulins; 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:SF6; AT11025P-RELATED; 1. DR PANTHER; PTHR10809; VESICLE-ASSOCIATED MEMBRANE PROTEIN-ASSOCIATED PROTEIN; 1. DR Pfam; PF00635; Motile_Sperm; 1. DR PIRSF; PIRSF019693; VAMP-associated; 1. DR SUPFAM; SSF49354; PapD-like; 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 //