ID S9VUT4_SCHCR Unreviewed; 1421 AA.
AC S9VUT4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=C2 domain-containing protein {ECO:0000313|EMBL:EPY49929.1};
GN ORFNames=SPOG_03398 {ECO:0000313|EMBL:EPY49929.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY49929.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY49929.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
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).
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DR EMBL; KE546994; EPY49929.1; -; Genomic_DNA.
DR RefSeq; XP_013025267.1; XM_013169813.1.
DR STRING; 653667.S9VUT4; -.
DR EnsemblFungi; EPY49929; EPY49929; SPOG_03398.
DR GeneID; 25037715; -.
DR eggNOG; KOG1012; Eukaryota.
DR HOGENOM; CLU_253068_0_0_1; -.
DR OMA; EVMDHED; -.
DR OrthoDB; 2787577at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd21678; SMP_TCB; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR017147; Tricalbin.
DR PANTHER; PTHR46980:SF3; C2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46980; TRICALBIN-1-RELATED; 1.
DR Pfam; PF00168; C2; 4.
DR PIRSF; PIRSF037232; Tricalbin; 2.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 3.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51847; SMP; 1.
PE 4: Predicted;
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 264..468
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 459..579
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 731..855
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1049..1169
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 155370 MW; D038CED187A322F2 CRC64;
MEGNQPSAAE PVISQSTKVV SESPSLNHQD KVVSTAKETR PVPQVPGKEP GEVTSTVRDA
APTNSSQSSS PSSPSNVMKG VPAESRAPQA LPHTSSSATT DRKEPAAQNP VSTSPKVKKP
DEPTGQSAQM PASHPLEATN PQKEEPDALI GWRSLHKTSV EQMRTFVQDA LSVFEWDSGR
VERSVLDMYL PGKLNGQWWQ SSLILASISV LSWLASKFFF CRWQILIIII FLSTFVYGSN
AIALRRTVRD EVIREMMKNP TNVDYETMDW FNVIFQRLWM LNEPMISRMI VTNVEQSVAE
YLPSFVPEVR FSSFTLGSKA PRIDGIRTHL ATEPNVVLMD VDFSYTPNDT LDISGASSCR
VNSAVSLRVK VGKGKFMFTL PVSTKDIFVS GQIRLRCKLS EEFPFIKTAS VCLLSTPKLS
ATVRPFDFSL FDADVFYIPG FNQFLHEQMT TILSPLAMWP NMLDLDLSSL MAGIAPFAPA
GVIAIKVYSA RRNEYLKSKT TKPSSYVAAL TNGYEHGRSP VRANTYTPIF EHTIYAVVSS
FNDPLELSLF DPESASLPFG TTYINTRSLV EKGFISDIQP LLFNAVNQGS VAYDATFFPS
LFPKKTLDGN LIEPPATPKG ILQLSLGCIN NIVELSGLEK KTQLIYSVSV DSKEIGSKTS
KFVDRAPINL SATTFIQNRE TQKIQITVSK KIKKEPNQLI GSMVIPLNKL LEANQSTYPF
KEKPSSSMDI SSSWIPVNVT EEKNAESYLK DLIGVMRIST IKANNCVSSD FALKKNDPYV
RVLVNGSVVG RTVHALNNTN PIWNEVLYAP VLADTDVIEL EVMDHEDSGH DKSLGFVEIP
VKSFKDASRK TEKTALANQI FGTDDIETLK LISRKGGSTR ITLTVNCDFR PCLRIASDDE
PTSKGEGNKA AVTESVNDKA ETSSITSLIS VSEACKYPSG LSMMSVRSAE LQAEGVELRI
FTDNCAFPFL TTGIARSKTP RWSAFGLSMI RELEYSETTF QLTDGSSKDP HIIAEHTEKT
SKLISESLGH VYAVDIQGPN GKINRVRISM NYLPVPMLLN PVESFINTGS LHFNLYNGKD
LPVGDIRSSD PYVVLKMNNE EVYKSKVIKK NLNPVWDEET DVIIQNRLLD TFDLICYDWD
LGEAADVLGS HHIDLNSLEP NVQSQSELNL EGKRGKINVG LRFEPGWYRR SPELHGSLPD
NFFSVANKGA KFLIGGIGAA GGFAINGVGS AGDLALNGVG SAGGLALNGV GAAGDLGGKA
VSGFTDTGKN LFKGVTGKGP KSARNNEQID AMSTQTASSV APRSSSAATI PTTAGKQELS
KFRLFVTNGS DCPHKLVKVV ITDKQGRTFK TRSHKGPSPK WNEQIPIGWN LGDVLHVSLI
SSNLIGHSKF GEATFSETAV GTFKVPFEGS TTSVEMRVEA V
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