PTSS2_MOUSE
ID PTSS2_MOUSE Reviewed; 473 AA.
AC Q9Z1X2; Q8BHL2; Q8CCI8; Q8CCY7; Q922A1; Q9CY68;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phosphatidylserine synthase 2;
DE Short=PSS-2;
DE Short=PtdSer synthase 2;
DE EC=2.7.8.29 {ECO:0000269|PubMed:10432300, ECO:0000269|PubMed:10938271, ECO:0000269|PubMed:12361952, ECO:0000269|PubMed:23071296};
DE AltName: Full=Serine-exchange enzyme II;
GN Name=Ptdss2; Synonyms=Pss2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=10432300; DOI=10.1042/bj3420057;
RA Stone S.J., Vance J.E.;
RT "Cloning and expression of murine liver phosphatidylserine synthase (PSS)-
RT 2: differential regulation of phospholipid metabolism by PSS1 and PSS2.";
RL Biochem. J. 342:57-64(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpus striatum, Embryo, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=10938271; DOI=10.1074/jbc.m002865200;
RA Stone S.J., Vance J.E.;
RT "Phosphatidylserine synthase-1 and -2 are localized to mitochondria-
RT associated membranes.";
RL J. Biol. Chem. 275:34534-34540(2000).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12361952; DOI=10.1074/jbc.m207734200;
RA Bergo M.O., Gavino B.J., Steenbergen R., Sturbois B., Parlow A.F.,
RA Sanan D.A., Skarnes W.C., Vance J.E., Young S.G.;
RT "Defining the importance of phosphatidylserine synthase 2 in mice.";
RL J. Biol. Chem. 277:47701-47708(2002).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18343815; DOI=10.1074/jbc.m800714200;
RA Arikketh D., Nelson R., Vance J.E.;
RT "Defining the importance of phosphatidylserine synthase-1 (PSS1):
RT unexpected viability of PSS1-deficient mice.";
RL J. Biol. Chem. 283:12888-12897(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23071296; DOI=10.1194/jlr.m031989;
RA Kimura A.K., Kim H.Y.;
RT "Phosphatidylserine synthase 2: high efficiency for synthesizing
RT phosphatidylserine containing docosahexaenoic acid.";
RL J. Lipid Res. 54:214-222(2013).
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 (PubMed:10432300, PubMed:10938271,
CC PubMed:23071296, PubMed:12361952). Catalyzes the conversion of
CC phosphatatidylethanolamine and does not act on phosphatidylcholine
CC (PubMed:10938271, PubMed:23071296). Can utilize both
CC phosphatidylethanolamine (PE) plasmalogen and diacyl PE as substrate
CC and the latter is six times better utilized, indicating the importance
CC of an ester linkage at the sn-1 position (PubMed:23071296). Although it
CC shows no sn-1 fatty acyl preference, exhibits significant preference
CC towards docosahexaenoic acid (22:6n-3) compared with 18:1 or 20:4 at
CC the sn-2 position (PubMed:23071296). {ECO:0000269|PubMed:10432300,
CC ECO:0000269|PubMed:10938271, ECO:0000269|PubMed:12361952,
CC ECO:0000269|PubMed:23071296}.
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:0000269|PubMed:10432300, ECO:0000269|PubMed:10938271,
CC ECO:0000269|PubMed:12361952, ECO:0000269|PubMed:23071296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27607;
CC Evidence={ECO:0000305|PubMed:23071296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + L-serine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-
CC sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:41484,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:73007,
CC ChEBI:CHEBI:75029; Evidence={ECO:0000269|PubMed:23071296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41485;
CC Evidence={ECO:0000305|PubMed:23071296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphoethanolamine + L-serine = 1-hexadecanoyl-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoserine +
CC ethanolamine; Xref=Rhea:RHEA:41488, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78261, ChEBI:CHEBI:78262;
CC Evidence={ECO:0000269|PubMed:23071296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41489;
CC Evidence={ECO:0000305|PubMed:23071296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC 3-phosphoethanolamine + L-serine = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphoserine + ethanolamine;
CC Xref=Rhea:RHEA:41500, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:78268, ChEBI:CHEBI:78269;
CC Evidence={ECO:0000269|PubMed:23071296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41501;
CC Evidence={ECO:0000305|PubMed:23071296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphoethanolamine + L-serine = 1-octadecanoyl-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphoserine +
CC ethanolamine; Xref=Rhea:RHEA:41492, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78265, ChEBI:CHEBI:78266;
CC Evidence={ECO:0000269|PubMed:23071296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41493;
CC Evidence={ECO:0000305|PubMed:23071296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenyl)-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-
CC sn-glycero-3-phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phospho-L-serine
CC + ethanolamine; Xref=Rhea:RHEA:41496, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78263, ChEBI:CHEBI:78264;
CC Evidence={ECO:0000269|PubMed:23071296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41497;
CC Evidence={ECO:0000305|PubMed:23071296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + L-serine = 1-octadecanoyl-2-(9Z-octadecenoyl)-
CC sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:40795,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57603, ChEBI:CHEBI:75038,
CC ChEBI:CHEBI:78260; Evidence={ECO:0000269|PubMed:23071296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40796;
CC Evidence={ECO:0000305|PubMed:23071296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenyl)-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho-L-serine + ethanolamine;
CC Xref=Rhea:RHEA:41600, ChEBI:CHEBI:33384, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:78340, ChEBI:CHEBI:78341;
CC Evidence={ECO:0000269|PubMed:23071296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41601;
CC Evidence={ECO:0000305|PubMed:23071296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenyl)-2-(5Z,8Z,11Z,14Z- eicosatetraenoyl)-sn-
CC glycero-3-phosphoethanolamine + L-serine = 1-(1Z-octadecenyl)-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-L-serine +
CC ethanolamine; Xref=Rhea:RHEA:41604, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:78342, ChEBI:CHEBI:78343;
CC Evidence={ECO:0000269|PubMed:23071296};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41605;
CC Evidence={ECO:0000305|PubMed:23071296};
CC -!- ACTIVITY REGULATION: Almost complete inhibition by ethanolamine in both
CC the mitochondria-associated membrane (MAM) and endoplasmic reticulum
CC (ER) per se. {ECO:0000269|PubMed:10938271}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10938271}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10938271}. Membrane {ECO:0000269|PubMed:23071296}.
CC Note=Highly enriched in the mitochondria-associated membrane (MAM).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z1X2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z1X2-2; Sequence=VSP_010637, VSP_010638;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Detected at lower
CC levels in kidney and heart. {ECO:0000269|PubMed:10432300,
CC ECO:0000269|PubMed:12361952}.
CC -!- DISRUPTION PHENOTYPE: Null mice exhibit a reduction of more than 95% in
CC serine exchange in testis and approximately 90% reduction in brain and
CC liver. Testis weight is reduced and some animals are infertile.
CC Elimination of either Pss1 or Pss2, but not both, is compatible with
CC mouse viability. Mice can tolerate as little as 10% serine-exchange
CC activity and are viable with small amounts of phosphatidylserine and
CC phosphatidylethanolamine content. {ECO:0000269|PubMed:12361952,
CC ECO:0000269|PubMed:18343815}.
CC -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
CC {ECO:0000305}.
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DR EMBL; AF099053; AAC98383.1; -; mRNA.
DR EMBL; AK021249; BAB32347.1; -; mRNA.
DR EMBL; AK031906; BAC27599.1; -; mRNA.
DR EMBL; AK032686; BAC27987.1; -; mRNA.
DR EMBL; AK036368; BAC29399.1; -; mRNA.
DR EMBL; AK081275; BAC38180.1; -; mRNA.
DR EMBL; BC009013; AAH09013.1; -; mRNA.
DR EMBL; BC053517; AAH53517.1; -; mRNA.
DR CCDS; CCDS22001.1; -. [Q9Z1X2-1]
DR RefSeq; NP_038810.2; NM_013782.4. [Q9Z1X2-1]
DR AlphaFoldDB; Q9Z1X2; -.
DR SMR; Q9Z1X2; -.
DR STRING; 10090.ENSMUSP00000026568; -.
DR SwissLipids; SLP:000000710; -.
DR GlyGen; Q9Z1X2; 1 site.
DR iPTMnet; Q9Z1X2; -.
DR PhosphoSitePlus; Q9Z1X2; -.
DR EPD; Q9Z1X2; -.
DR jPOST; Q9Z1X2; -.
DR MaxQB; Q9Z1X2; -.
DR PaxDb; Q9Z1X2; -.
DR PeptideAtlas; Q9Z1X2; -.
DR PRIDE; Q9Z1X2; -.
DR ProteomicsDB; 301920; -. [Q9Z1X2-1]
DR ProteomicsDB; 301921; -. [Q9Z1X2-2]
DR Antibodypedia; 41975; 103 antibodies from 15 providers.
DR DNASU; 27388; -.
DR Ensembl; ENSMUST00000026568; ENSMUSP00000026568; ENSMUSG00000025495. [Q9Z1X2-1]
DR GeneID; 27388; -.
DR KEGG; mmu:27388; -.
DR UCSC; uc009kjp.1; mouse. [Q9Z1X2-2]
DR UCSC; uc009kjq.1; mouse. [Q9Z1X2-1]
DR CTD; 81490; -.
DR MGI; MGI:1351664; Ptdss2.
DR VEuPathDB; HostDB:ENSMUSG00000025495; -.
DR eggNOG; KOG2735; Eukaryota.
DR GeneTree; ENSGT00530000063576; -.
DR HOGENOM; CLU_037661_4_1_1; -.
DR InParanoid; Q9Z1X2; -.
DR OMA; MKYIDPN; -.
DR OrthoDB; 818196at2759; -.
DR PhylomeDB; Q9Z1X2; -.
DR TreeFam; TF300012; -.
DR BRENDA; 2.7.8.29; 3474.
DR Reactome; R-MMU-1483101; Synthesis of PS.
DR UniPathway; UPA00948; -.
DR BioGRID-ORCS; 27388; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ptdss2; mouse.
DR PRO; PR:Q9Z1X2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z1X2; protein.
DR Bgee; ENSMUSG00000025495; Expressed in fetal liver hematopoietic progenitor cell and 265 other tissues.
DR ExpressionAtlas; Q9Z1X2; baseline and differential.
DR Genevisible; Q9Z1X2; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IMP:MGI.
DR GO; GO:0106245; F:L-serine-phosphatidylethanolamine phosphatidyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IMP:MGI.
DR InterPro; IPR004277; PSS.
DR Pfam; PF03034; PSS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Phosphatidylserine synthase 2"
FT /id="PRO_0000056833"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..74
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..291
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..473
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2GV22"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 264..303
FT /note="GKMKRIAFQFTPYSWVRFEWKPASSLHRWLAVCGIILVFL -> YILGVIEG
FT NHRALGPQGQGLATWEGGKQNIRVVESDC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010637"
FT VAR_SEQ 304..473
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010638"
FT CONFLICT 4
FT /note="G -> A (in Ref. 1; AAC98383)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="G -> A (in Ref. 2; BAC27599)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="T -> A (in Ref. 1; AAC98383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 55021 MW; 09ECB04E5B906F63 CRC64;
MRRGERRVAG GSGSESPLLK GRRSTESEVY DDGTNTFFWR AHTLTVLFIL TCALGYVTLL
EETPQDTAYN TKRGIVASIL VFLCFGVTQA KDGPFSRPHP AYWRFWLCVS VVYELFLIFI
LFQTVQDGRQ FLKYVDPRLG VPLPERDYGG NCLIYDADNK TDPFHNIWDK LDGFVPAHFI
GWYLKTLMIR DWWMCMIISV MFEFLEYSLE HQLPNFSECW WDHWIMDVLV CNGLGIYCGM
KTLEWLSLKT YKWQGLWNIP TYKGKMKRIA FQFTPYSWVR FEWKPASSLH RWLAVCGIIL
VFLLAELNTF YLKFVLWMPP EHYLVLLRLV FFVNVGGVAM REIYDFMDEL KPHRKLGQQA
WLVAAITVTE LLIVVKYDPH TLTLSLPFYI SQCWTLGSIL VLTWTVWRFF LRDITMRYKE
TRRQKQQSHQ ARAVNNRDGH PGPDDDLLGT GTAEEEGTTN DGVTAEEGTS AAS
