TAPT1_SCHPO
ID TAPT1_SCHPO Reviewed; 649 AA.
AC O60067;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Endoplasmic reticulum membrane protein 65 {ECO:0000250|UniProtKB:P40085};
GN ORFNames=SPBC13G1.05 {ECO:0000312|PomBase:SPBC13G1.05};
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-94, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: May be involved in membrane protein folding.
CC {ECO:0000250|UniProtKB:P40085}.
CC -!- SUBUNIT: Interacts with slp1. {ECO:0000250|UniProtKB:P40085}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TAPT1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA18658.1; -; Genomic_DNA.
DR PIR; T39406; T39406.
DR RefSeq; NP_596554.1; NM_001022475.2.
DR AlphaFoldDB; O60067; -.
DR STRING; 4896.SPBC13G1.05.1; -.
DR iPTMnet; O60067; -.
DR MaxQB; O60067; -.
DR PaxDb; O60067; -.
DR PRIDE; O60067; -.
DR EnsemblFungi; SPBC13G1.05.1; SPBC13G1.05.1:pep; SPBC13G1.05.
DR GeneID; 2539819; -.
DR KEGG; spo:SPBC13G1.05; -.
DR PomBase; SPBC13G1.05; -.
DR VEuPathDB; FungiDB:SPBC13G1.05; -.
DR eggNOG; KOG2490; Eukaryota.
DR HOGENOM; CLU_003655_1_1_1; -.
DR InParanoid; O60067; -.
DR OMA; SHQELKW; -.
DR PhylomeDB; O60067; -.
DR PRO; PR:O60067; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0035437; P:maintenance of protein localization in endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISO:PomBase.
DR InterPro; IPR008010; Tatp1.
DR PANTHER; PTHR13317; PTHR13317; 1.
DR Pfam; PF05346; DUF747; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..649
FT /note="Endoplasmic reticulum membrane protein 65"
FT /id="PRO_0000328879"
FT TOPO_DOM 1..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P40085"
FT TRANSMEM 166..186
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..302
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P40085"
FT TRANSMEM 303..323
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P40085"
FT TRANSMEM 367..387
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..414
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P40085"
FT TRANSMEM 415..435
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P40085"
FT TRANSMEM 480..500
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..557
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P40085"
FT TRANSMEM 558..578
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P40085"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 649 AA; 74732 MW; 7C7CB9ED14136D87 CRC64;
MGSNTSPGQA DPLESENESS LTSRFLPNKR DGGKDNESVI PEKEEPDLNE PVLAVPLPKS
RYALTKRSSS SEYPRRSAST SAKKNVIPIT RSYSTTFFSK TNDQPTVTGN QDKPISRLRA
SKLQIQNFWN YICFELLAND TVPANPIKEK HVENFLATPY AIEKTFLFGW FVSVDSFLYI
FTLFPIRVLI SFFTLSRCIF QGLFSTFFHR NSSPNRSLPR SRKIDLLKLL LIFSTSILIR
KIDVSRLYHI IRAQASIRFY VLYNVLEIAD RLCCALGQDV LDCLFSNHIL SFNFWNPAGW
MTFFYYFAIS LAYMVLHTLV LLYQIITLNV TVNSYSNAVL ALLMSNQLVE IKGAVFKKFE
KENLFQLTCS DVVERFQITI MVIIIFLRNL AELYTTSSLD QPLLTFKRLK TLLAPFFWVI
GSELFVDWLK HAFIIKFNYI KPSIYSRFTD VLCHDYVASG AQLTQTVTGC SQQVARRMGL
PVLPLVCVFI RTSMQTWSMF RSTHSMKQEI AKSIGTIFPT KDNYVYYLPN KEANTYNAGK
EASWETLLLS VVRGKSGIAF LFFMAIMLKL LLGKAILAIT QSRYESMQQR EEKINSWERE
RKANNFFRGH IEIDKKTKDF LNNSKDDLPV PKSPLLTLER YAMHSKRIW
