CWH43_SCHPO
ID CWH43_SCHPO Reviewed; 971 AA.
AC Q9HDZ2; P78781; Q9P6M4;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein cwh43;
GN Name=cwh43; ORFNames=SPAC589.12, SPAC688.01;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 571-971.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
CC -!- FUNCTION: Involved in the maintenance of cell wall integrity. Required
CC for the replacement of the diacylglycerol moiety by ceramides during
CC GPI-anchor maturation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PGAP2 family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PGAP2IP family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAC19769.1; -; Genomic_DNA.
DR EMBL; D89130; BAA13792.1; -; mRNA.
DR PIR; T42374; T42374.
DR RefSeq; NP_594060.2; NM_001019484.2.
DR AlphaFoldDB; Q9HDZ2; -.
DR SMR; Q9HDZ2; -.
DR BioGRID; 278628; 7.
DR STRING; 4896.SPAC589.12.1; -.
DR TCDB; 9.B.131.1.9; the post-gpi attachment protein (p-gap2) family.
DR MaxQB; Q9HDZ2; -.
DR PaxDb; Q9HDZ2; -.
DR PRIDE; Q9HDZ2; -.
DR EnsemblFungi; SPAC589.12.1; SPAC589.12.1:pep; SPAC589.12.
DR GeneID; 2542152; -.
DR KEGG; spo:SPAC589.12; -.
DR PomBase; SPAC589.12; cwh43.
DR VEuPathDB; FungiDB:SPAC589.12; -.
DR eggNOG; KOG3979; Eukaryota.
DR HOGENOM; CLU_009808_0_0_1; -.
DR InParanoid; Q9HDZ2; -.
DR OMA; ITAGIWT; -.
DR PhylomeDB; Q9HDZ2; -.
DR PRO; PR:Q9HDZ2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:PomBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IMP:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:PomBase.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR027317; PGAP2IP.
DR PANTHER; PTHR14859:SF1; PTHR14859:SF1; 1.
DR Pfam; PF10277; Frag1; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..971
FT /note="Protein cwh43"
FT /id="PRO_0000116831"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..242
FT /note="PGAP2-like"
FT /evidence="ECO:0000250"
FT REGION 243..971
FT /note="PGAP2IP-like"
FT /evidence="ECO:0000250"
FT ACT_SITE 826
FT /evidence="ECO:0000250"
SQ SEQUENCE 971 AA; 110034 MW; 8F2E788E6F01C4C5 CRC64;
MTEKTSSLVF SAQYVALVHT ICSFAAFFIP LALALYTHYY QVVKNEFYGY PEEWFPSVSA
TIGDWYPERS VFQWLIALTA TPRLLVLLLW FTLSGISRPS VIITTALGVL RTALCGGWVY
VTSTDDHDWH DIFMIGYLIS NAPWFILVSK CSPVNSMASR IRNIGSALFV LTIFPLIYWY
IQHKFKHIPG AYTVYAFFEW SLILWDILFD SALYWDFKPL VFNLHTSKTY SNPSSFATRK
KEKGEHLSYA EAAAVGTQAK NIKKDSNVKC SKKQILFSLL YFSSEVYLSF VFWSVLTSLG
LLVWYFPLWH MGISGYEACI LFELSPFLLG IPLLRKFASK VPVIFLFLNV IGIAAYKLED
PVHRLFVTAF SVCCECLAWT SLFSNISPEN LAIERKISTF LFGLLASSIA KYSFFSNNPI
WPILNETNGG KQIPALIVGI IACLIFAIFH VQQTTANAVE HFKLRKITAL SAALSLGTVL
FCLHTFLCDS TVLMTWSWDG YPIKGPQPYP HGAVSIVVSI CAVLVAPYLY QSGAFMLIGF
VLACFGSYFM YINHGWCSYL GGLIFTSYVL IYSFASIRIS SFYSPAKVWG GAFLVYILYS
LAHVWVVAYE FVPGGPILRE RTSYILIFIG WNLAALVPAY SGESKEPNKA DSSVVDIKQS
DSSYRRRSFK KSLLTGFCLA LMALKFAIQN MPPYDYTPYH PNEKLFTAGI WTIHFGLDNF
MYASENRIRD AVRDMELDVF GLLESDTQRL IMGFRDLTQV LAHDLGMYAD YGPGPDKHTW
GAALLSKFPI VNSTHHLLPS PQGELAPAIH ATLDVYGELI DVVVSHNGQY ESQLDRRLQS
TELARIMRES PRPLVFLGYV VSNVGQEPQT ILTRDTGMLD IEPADYDRWC QYIFYRGVKR
IGYARLHRST ITDTELQTGK FLVTKDLGRN VRIDKEHVPE SHRYPSLFEG TGVNGHYYDN
NLVVHEPWYY D
