PTSS1_CHICK
ID PTSS1_CHICK Reviewed; 473 AA.
AC Q5ZM65; F1P3L7;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphatidylserine synthase 1;
DE Short=PSS-1;
DE Short=PtdSer synthase 1;
DE EC=2.7.8.29 {ECO:0000250|UniProtKB:P48651};
DE AltName: Full=Serine-exchange enzyme I;
GN Name=PTDSS1; ORFNames=RCJMB04_2p18;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: Catalyzes a base-exchange reaction in which the polar head
CC group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is
CC replaced by L-serine (By similarity). Catalyzes mainly the conversion
CC of phosphatidylcholine but also converts, in vitro and to a lesser
CC extent, phosphatidylethanolamine (By similarity).
CC {ECO:0000250|UniProtKB:P48651}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a
CC 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine;
CC Xref=Rhea:RHEA:27606, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:64612; EC=2.7.8.29;
CC Evidence={ECO:0000250|UniProtKB:P48651};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607;
CC Evidence={ECO:0000250|UniProtKB:P48651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + L-serine = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + choline; Xref=Rhea:RHEA:45088,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:P48651};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45089;
CC Evidence={ECO:0000250|UniProtKB:P48651};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q99LH2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q99LH2}. Note=Highly enriched in the
CC mitochondria-associated membrane (MAM). {ECO:0000250|UniProtKB:Q99LH2}.
CC -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
CC {ECO:0000305}.
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DR EMBL; AJ719519; CAG31178.1; -; mRNA.
DR EMBL; AADN02024909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001026676.1; NM_001031505.1.
DR AlphaFoldDB; Q5ZM65; -.
DR STRING; 9031.ENSGALP00000025730; -.
DR PaxDb; Q5ZM65; -.
DR Ensembl; ENSGALT00000059601; ENSGALP00000045213; ENSGALG00000030185.
DR GeneID; 428374; -.
DR KEGG; gga:428374; -.
DR CTD; 9791; -.
DR VEuPathDB; HostDB:geneid_428374; -.
DR eggNOG; KOG2735; Eukaryota.
DR GeneTree; ENSGT00530000063576; -.
DR HOGENOM; CLU_037661_3_0_1; -.
DR InParanoid; Q5ZM65; -.
DR OMA; QYYMYVT; -.
DR OrthoDB; 818196at2759; -.
DR PhylomeDB; Q5ZM65; -.
DR TreeFam; TF300012; -.
DR UniPathway; UPA00948; -.
DR PRO; PR:Q5ZM65; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000030185; Expressed in liver and 13 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106258; F:L-serine-phosphatidylcholine phosphatidyltransferase activity; IEA:RHEA.
DR GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR004277; PSS.
DR Pfam; PF03034; PSS; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Phosphatidylserine synthase 1"
FT /id="PRO_0000416031"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..72
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..186
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..286
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..355
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..473
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 420..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..473
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 184
FT /note="R -> H (in Ref. 1; CAG31178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 55511 MW; 89D57ED2B2F40029 CRC64;
MAACVGSRTL SKDDVNYRLH FRMINEQQVE DITLEFFYRP HTITLLSFTI LSLMAFAFTR
DDSVPEENIW RGILSVIFFF LIISVLAFPN GPFTRPHPAI WRMVFGLSVL YFLFLVFVLF
LNFEQVKAVM YWLDPNLRYA TREADIMEYA VNCHVITWER ILSHFDIFAF GHFWGWAMKA
LLIRSYGLCW TISITWELTE LFFMHLLPNF AECWWDQVIL DILLCNGGGI WLGMVVCRFL
EMRTYHWASF KDIHTTTGKI KRAVLQFTPA SWTYVRWFDP KSSFQRVAGI YLFMIIWQLT
ELNTFFLKHI FVFQASHPLS WGRILFIGII TAPTVRQYYA YLTDTQCKRV GTQCWVFGVI
AFLEAIVCIK FGQDLFSKTQ ILYVVFWLLC VAFTTFLCLY GMVWYAEYYG HREKTLSESE
DSPYSPDASW LHSKFSKGAD NSPPKHPVNS ESHSSRRRNR HSRSKVTNGI GKK
