YF49_SCHPO
ID YF49_SCHPO Reviewed; 2699 AA.
AC Q6LA55;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=UPF0648 protein C3H5.09c;
GN ORFNames=SPAC3H5.09c;
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 REVISION OF GENE MODEL.
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the UPF0648 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16593.2; -; Genomic_DNA.
DR PIR; T38755; T38755.
DR RefSeq; NP_594183.2; NM_001019607.2.
DR AlphaFoldDB; Q6LA55; -.
DR SMR; Q6LA55; -.
DR STRING; 4896.SPAC3H5.09c.1; -.
DR iPTMnet; Q6LA55; -.
DR MaxQB; Q6LA55; -.
DR PaxDb; Q6LA55; -.
DR PRIDE; Q6LA55; -.
DR EnsemblFungi; SPAC3H5.09c.1; SPAC3H5.09c.1:pep; SPAC3H5.09c.
DR GeneID; 2543405; -.
DR KEGG; spo:SPAC3H5.09c; -.
DR PomBase; SPAC3H5.09c; -.
DR VEuPathDB; FungiDB:SPAC3H5.09c; -.
DR eggNOG; KOG1910; Eukaryota.
DR HOGENOM; CLU_000592_0_0_1; -.
DR InParanoid; Q6LA55; -.
DR OMA; YYMSRRA; -.
DR PRO; PR:Q6LA55; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; TAS:PomBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; TAS:PomBase.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; TAS:PomBase.
DR InterPro; IPR045167; FMP27.
DR InterPro; IPR019443; FMP27_C.
DR InterPro; IPR019409; FMP27_DUF2405.
DR InterPro; IPR019441; FMP27_GFWDK_dom.
DR InterPro; IPR019439; FMP27_N.
DR InterPro; IPR019415; FMP27_SW_dom.
DR InterPro; IPR019449; FMP27_WPPW_dom.
DR PANTHER; PTHR15678; PTHR15678; 1.
DR Pfam; PF10351; Apt1; 1.
DR Pfam; PF10293; DUF2405; 1.
DR Pfam; PF10344; Fmp27; 1.
DR Pfam; PF10347; Fmp27_GFWDK; 1.
DR Pfam; PF10305; Fmp27_SW; 1.
DR Pfam; PF10359; Fmp27_WPPW; 1.
DR SMART; SM01214; Fmp27_GFWDK; 1.
DR SMART; SM01215; Fmp27_SW; 1.
DR SMART; SM01216; Fmp27_WPPW; 1.
PE 3: Inferred from homology;
KW Coiled coil; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2699
FT /note="UPF0648 protein C3H5.09c"
FT /id="PRO_0000350759"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 975..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2393..2447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2606..2632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2647..2676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1006..1033
FT /evidence="ECO:0000255"
FT COILED 1758..1818
FT /evidence="ECO:0000255"
FT COMPBIAS 982..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2394..2410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2425..2447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1003
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2032
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2699 AA; 311842 MW; F5E0C46146B79272 CRC64;
MNPLFPFSLL NPSTMWSSSQ NTSFVWVVIA TGFLFHLVLF VLSYVLGWPF TNFGFFSVYG
LRHTFRNGDS VFISYVALRL HRPSTSKPYL LRIVTKGLIY TPSLSSANDA QSAGKNENQR
SRLVFKAKRE EEKTEEKFCH AVYMSNLLRN VEQKWIQFLH KSWMKWLHIS IQESQLTFPS
VGTFELGSLS MEMRPETNNV VGYENPSDPE LVSSCVICSI RLANLVYIDR RQSSQQITDY
LDLSLQTYYS LDKSNVPDTI LRLRSSIKVG VLYIDLDTPL FEHLLNSNSS GGNHSSSSSS
SGKVHVMKDN VEAALLKLQE AQIQIGTLKL WKRNVTGCGA TYILNGSDFG LNLILLNKKN
PSHRMFFPVE ACVHQILASA LSFNVESITP GHSPHVLLNI PLVTITCLTS ALAEYARDAS
DLHQLQNSIL RVNSTLTSPS LDLRLELLHD VLSCFPKKHD STSRKKPKFP YQYFPYMKFS
VSLYEPALRF LIASKSDSDF PGMLVANLSS MFLDIKYSPS SEHIFEIESS LRLSSNKVFY
HNPKNKKWLI NTSDLITFSL GYICNNDHGS LNMFFRDFQI RIEEEEVINS LKKFIILTKI
KSEQVGPRKP RTKLVEPLLF RIPKWLKHIQ LEVHSLLLVI TAIRPEISPE PRGINCSIDK
IHSLYLNDKK SRSQGMRKFD LNLELLMIKS IIFKNGKSLN SHLFLQIPNI NFIVSTILRD
NTAISRFTTE INFLRCFASL LHNCCIFYAY RACSSLFGEN KSHKRIEKTN TSPQEPGVVP
EGWNFDFRLK NARVSIFLDD DVSLLLDCGG FTTLKKTEKK YAEMHAKFIQ IHTKNSDVPT
LWDRFLALGN VRYQLKDLSD LEKLHQVTCS YISIRIPHKF IPFILIESAI NTVKAAIRVS
AEPLTIDQQH DLAEEIKQPR VVPHIQIKST KFKFEVDDDP FECRLGMNYR IGLTEQQMRI
DRWNIFEERA NLLRKAKDPS PKSASESSSF YQNGSDIDDN DSNSSNTSNH TTENANAQQR
KLEDLNRSFE DFLGSRPTNN SSFLKNVSVD EDTAREKLME YDSLSWISNI KRIREFRYHR
LRIRRMTAWP ESDALDKHIL FKENIIPIPI RPPLVDISLL NFDFTLDKPS FPLEELPKFL
NTVGRGQPLD YGYSIYFPMY IDWKMDEAKF LIRDYPLPLV YIPKLGRGQD KRISSWHLKS
NMVITEQQAT LAAIRDVSVK VIPADLTKEG IPYVVNVTRT VSPIKTFSKT EIDVNSSLPT
FLLWCNSYQP ALSDMTRIMD TFTKMPIDPS EKLGFWDKIR LVAHSQIRLR WLEDGDVFLS
LKGSRDPYVI LGEGAGFQFC WSGNVSWDIG CDENPANFMI VDSDKFYLTI PDFPRQINGI
LEGKPLPTKS TKRSYTTFGV LKDLRCRKVI AKLVGKVRWR AGFVPERHCD EDCTVCNRKK
ACRLWNFKPH WQVITRIPQY CHDTHYGVYD AYRDFRSHYI HCSLALESPR YLDDANAFEN
VNSYNTIHLT PLVFSHFSSW WNLFSNNMSY PLRSGNLFPT LDSSPNKKFG RHLATFKYAL
ELTPLFISHM YNYKTNKNWQ DRTASATGLK ARVDNFTIDL HQRSEKHEVK NKANLGRKHQ
EATSMKVHLA EIDFKTIDLR AISASFDEGA LDNSDSIPAN VLDEEEKECF SFKNVDGPAN
WVDIDDYHEA DWLLPQQNEK CSIYPLAFSP RFTYYRHTKC HRRNEKNEKE IIPDTCRFGD
EFTHRCLMPS RENPKAVQYE LLQKRRKELE EFMSSEQERI GFLKSQLESN NDSEEVRQEY
EELTKRIVTL SDHYRLLEYL LKDESSCSQA SQCSENGQVD LSYASLSESV HAFNNRFVAH
NVQVKWNNFI RNAVMSYVHE VERVRGFAYY MSQKAIVFLR DLEKRTESAN DDFFGNYTED
DEDRENARHL LKFLLEDSKK RFWVKTSDAD REHGSEEGNT NSISNNEYDI IQSYVFRFIS
PQIQLQCSSN PEKAVIISIQ SLQIKILSVV DPIFPDNDIN YLIERRFLCK VNESQFFISK
KSDFEVVNAS SLVLNEYGCE HNTVWPPWVP FETTFDFVLT PAAFSRFLHR VSFSVIYTKH
NDLRLQETVH STRAFFEDLD THADTLTFDF PRVVFSTDSS QYYDIFTIIT DLLLYKEPAQ
KQRNQRLEEI MLAADFSDLT GTSEVVRALQ ARVHRLLDLK LQHQLYDVTF GIYAHIAQQL
FLQNELHRCG EELYYLIESI AAVQNRGIHQ NKVRSNLSWF LMAKEVVWHL LEDNKKPFLD
VRLQNATFRR IENSDASNFN TLEIEFMKGS NLAPGCQFEN IICPYFNHEF SNEQLLQQKF
IRIHWEVLEA VAGIQVIQHF EINLFPLSLQ IEQELATKLF AYAFPNRNES DGFPHIYSRN
HDKRKENGSQ GEADNSNYSG SLMRRRTNDQ EEDALATPSS SRRDSRSKRA SLIDFTIDKC
LDVDDEGRME LQSMLDRAGS NMLITYFKIP SVVLRLSYRG TGGLGLENIT GFVFTVPTME
YRNEVCSYLD LAMKLKHDLI RTVVSHTGKL LVEKVKGNYH LKEHEREVSS ELLNLQQLSA
EHNRHADLES MVMARDDYIN VQQPLAEENQ EEGSPASAIS RNHSTRSSLN SPRQFWAYHG
SRSKKIADIV KRHIPPTING KRSKNKGNEG SNARVDFYND ERYDPVKREL ILGASNRRK
