YFRD_SCHPO
ID YFRD_SCHPO Reviewed; 1562 AA.
AC Q9UT43; Q9P6S8;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Putative phospholipid-transporting ATPase C821.13c;
DE EC=7.6.2.1;
GN ORFNames=SPAC821.13c, SPAC955.01c;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-954, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB57447.1; -; Genomic_DNA.
DR PIR; T41724; T41724.
DR RefSeq; XP_001713045.1; XM_001712993.2.
DR AlphaFoldDB; Q9UT43; -.
DR SMR; Q9UT43; -.
DR BioGRID; 280591; 1.
DR STRING; 4896.SPAC821.13c.1; -.
DR iPTMnet; Q9UT43; -.
DR MaxQB; Q9UT43; -.
DR PaxDb; Q9UT43; -.
DR PRIDE; Q9UT43; -.
DR EnsemblFungi; SPAC821.13c.1; SPAC821.13c.1:pep; SPAC821.13c.
DR PomBase; SPAC821.13c; -.
DR VEuPathDB; FungiDB:SPAC821.13c; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q9UT43; -.
DR OMA; FIIMFNT; -.
DR PhylomeDB; Q9UT43; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-936837; Ion transport by P-type ATPases.
DR PRO; PR:Q9UT43; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030173; C:integral component of Golgi membrane; IC:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; ISO:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0045332; P:phospholipid translocation; ISO:PomBase.
DR Gene3D; 3.40.1110.10; -; 2.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 2.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1562
FT /note="Putative phospholipid-transporting ATPase C821.13c"
FT /id="PRO_0000046240"
FT TOPO_DOM 1..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 596..614
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..1309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1310..1330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1331..1332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1333..1353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1354..1381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1382..1402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1403..1414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1415..1435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1436..1443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1444..1464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1465..1490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1491..1511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1512..1562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 684
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1562 AA; 176725 MW; 2B2B138BF8CB5E6E CRC64;
MKSSGIAGDS NGFETNFLNE TTNREEDGAF NWNAADDGTN ERREDIHVRF QDSALPLGID
ENELDEIDIN GDSKKLDSVE VDESHDVNSP SDSRLKSSFK SVLELTANSM VSVLTPSTKT
EQTSKGKGKK KKAHVSFLEG PVEEIPLDDI EPTSPREASP VFNGRPPIPP EFLKSRHKEF
TIPNPLQFIS NFLSNLFSRD TRYLKSSHGR IIIINPYDDS SQIDERTGKP YMQNSIVSSR
YNKYNFVPLQ IIAQFSKTAN CYFLLIAIMQ MIPGWSTTGT YTTIIPLLIF ISIAILREGF
DNYRRYRQDR VENRIQTQVL RHVDVDPPIV EEHSSFFRRR RWRRSRSQES ASRSTIRSTD
EREPERTSED PPQLPPSPSS PSSPALSVKP NIDPQPPLYN STLTTTRSIP ANKPTFFWAS
CDRKDVRVGD IIRLTSDQTL PADVIALSSP NPNGAIYIET AALDGETSLK TRLVNSTLRS
LCKDINDLIR LSGTCTVEDP NGDLYNFNGS MKLDSIQGEI PLSNNDVLYR GSNLRNTSEL
FALVIFTGEE SKIRMNAVRN VSVKAPSMQK VTNRIVIFIF ALVVSMAIYC TAAYFVWQKK
VERKLWYLTN SKLSFVPILV SFIILYNTMV PISLYVSMEI IRVFQTFLVQ SDIDLYYPEN
DTRCEVRSSS ILEELGQVTH VFSDKTGTLT DNIMLFRNLS VGGFAWQHVG AENPKLVSTS
QKSDDLDGEA KPPQLENIQG TTIQLLQYVH DNPHTTFSKR VRIFLLNLAI CHTCLPSFDE
ENQIYKYQSI SPDELALVHA AQQLGYIVID RDIDSLTIRL HYPLDPHSHP IAKTYRILNI
IEFTSKRKCM SVIVRMPNGR ICLFCKGADS AIIKRLRLSN LAKRKDKSVT KAEQARKSIE
IDKAIIRNSQ STSRPSLTAS RPSLSRRRND YINNVTSWLD ERREKMGVVR PRASTSILET
RRRPAVGRHS LAGGERLMED KKYLSKQEEA EGSIYESLNH NDAKLFENTF EHVHAFATDG
LRTLMYAHRF IDESEYQSWK LVNDAALNSL SNRQQLLDEA ADLIEKDLEF AGATAIEDKL
QVGVPESINS LFRAGIKFWM LTGDKKETAI NIGHSCGVIK EYSTVVVMGS LDGVEGSDET
VSGGQRLSLD RPPTNDPASL MIHQLISCMN AIHSNSLAHL VIVIDGSTLA DIENDPELFL
LFINTAVEAD SVICCRSSPM QKALMVQKVR NTLEKAVTLA IGDGANDIAM IQEAHVGIGI
AGREGLQAAR SSDFSIGRFK FLIKLLFCHG RWSYVRLSKY ILGTFYKEQF FFLMQAIMQP
FVGYTGQSLY ESWGLTCFNT LFSSLCVIGL GIFEKDLSAS TVIAVPELYQ KGINNEAFNW
RVYFGWCSIA FIQAFLVFYV TYSLFGMKEL NDNNIFAYGQ LIFTAAIFIM NFKLVFIEMQ
YINIISIIVL VLTSLAWFLF NIFISEHYPD KNLYLARSQF LHHFGKNPSW WLTMLFVMVC
ALTIDIVAQM LRRTLRPTDT DIFVEMENDA FVRSRFEQES GEFLQANAPS VDEIEQYLKS
RD
