SCS2_SCHPO
ID SCS2_SCHPO Reviewed; 383 AA.
AC O60119;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Vesicle-associated membrane protein-associated protein scs2;
DE Short=VAMP-associated protein scs2;
DE AltName: Full=VAP homolog 1;
GN Name=scs2; ORFNames=SPBC16G5.05c;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-237; SER-259;
RP SER-261 AND SER-268, AND 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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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 [5]
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 [6]
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 [7]
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 [8]
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.8). {ECO:0000269|PubMed:23041194,
CC ECO:0000269|PubMed:26877082, ECO:0000269|PubMed:29290560,
CC ECO:0000269|PubMed:32023460, ECO:0000269|Ref.8}.
CC -!- SUBUNIT: Interacts with epr1. {ECO:0000269|Ref.8}.
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
CC scs22 is also deleted (PubMed:23041194, PubMed:26877082,
CC PubMed:29290560, PubMed:32023460). Affects contractile ring assembly
CC and displays severe cytokinetic defects; when scs22 is also deleted
CC (PubMed:26877082). {ECO:0000269|PubMed:23041194,
CC ECO:0000269|PubMed:26877082, ECO:0000269|PubMed:29290560,
CC 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; CU329671; CAA19025.1; -; Genomic_DNA.
DR PIR; T39597; T39597.
DR RefSeq; NP_596754.1; NM_001023774.2.
DR AlphaFoldDB; O60119; -.
DR SMR; O60119; -.
DR BioGRID; 276553; 12.
DR STRING; 4896.SPBC16G5.05c.1; -.
DR iPTMnet; O60119; -.
DR MaxQB; O60119; -.
DR PaxDb; O60119; -.
DR PRIDE; O60119; -.
DR EnsemblFungi; SPBC16G5.05c.1; SPBC16G5.05c.1:pep; SPBC16G5.05c.
DR PomBase; SPBC16G5.05c; -.
DR VEuPathDB; FungiDB:SPBC16G5.05c; -.
DR eggNOG; KOG0439; Eukaryota.
DR HOGENOM; CLU_032848_1_0_1; -.
DR InParanoid; O60119; -.
DR OMA; DRKIRCV; -.
DR PhylomeDB; O60119; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-9013106; RHOC GTPase cycle.
DR Reactome; R-SPO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR PRO; PR:O60119; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; EXP:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; EXP:PomBase.
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:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0051685; P:maintenance of ER location; IMP: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 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..383
FT /note="Vesicle-associated membrane protein-associated
FT protein scs2"
FT /id="PRO_0000314099"
FT TOPO_DOM 1..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 363..383
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 1..123
FT /note="MSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT REGION 127..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 383 AA; 41235 MW; 02C5778278C6EAC5 CRC64;
MSVECSGELF FYPPFTTMSK ELISVHNPNP EPVIFKVKTT APKHYCVRPN SGKIEPKSTV
NVQVLLQAMK EEPAPDFKCR DKFLIQSMAI GDADTSNVEN YHEFWTEMEK QGRSIFDRKI
RCVYSTKQPP QSADKQVENT STSNPPVSVE GSENLASSVG GPTAVGVSLD EAQNDFNGAK
DHLSNGVNTV VPDSTFRSTF ESAQIPDASV VQTVVTDADN GAASVKDTIV TAESASSKGA
DVARSKVQDI IDNEIPKPSE SPRRSVSSTP PVHPPPPVPQ NLSAVNEEFD TKKNDFDSKL
PESTPAVEKV SENLGSETRE SLQGAKPAAG AHSSDNALEQ IKPSYSADPS SSTGASLTES
PGIPPNIVII LCLIFFLIGY LFF
