PSN2_MOUSE
ID PSN2_MOUSE Reviewed; 448 AA.
AC Q61144; O54977; P97934; P97935; Q91VS3; Q9D616;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Presenilin-2;
DE Short=PS-2;
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=Presenilin-2 NTF subunit;
DE Contains:
DE RecName: Full=Presenilin-2 CTF subunit;
GN Name=Psen2; Synonyms=Ad4h, Alg3, Ps-2, Psnl2;
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).
RC TISSUE=Liver;
RX PubMed=8940094; DOI=10.1074/jbc.271.49.31025;
RA Vito P., Wolozin B., Ganjei J.K., Iwasaki K., Lacana E., D'Adamio L.;
RT "Requirement of the familial Alzheimer's disease gene PS2 for apoptosis.
RT Opposing effect of ALG-3.";
RL J. Biol. Chem. 271:31025-31028(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=NIH Swiss;
RA Sahara N., Mori H., Shirasawa T.;
RT "Molecular cloning of mouse presenilin 2 gene.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 340-448 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8560270; DOI=10.1126/science.271.5248.521;
RA Vito P., Lacana E., D'Adamio L.;
RT "Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's
RT disease gene ALG-3.";
RL Science 271:521-525(1996).
RN [6]
RP INTERACTION WITH DOCK3.
RX PubMed=12093789; DOI=10.1083/jcb.200110151;
RA Chen Q., Kimura H., Schubert D.;
RT "A novel mechanism for the regulation of amyloid precursor protein
RT metabolism.";
RL J. Cell Biol. 158:79-89(2002).
RN [7]
RP FUNCTION.
RX PubMed=16959576; DOI=10.1016/j.cell.2006.06.059;
RA Tu H., Nelson O., Bezprozvanny A., Wang Z., Lee S.F., Hao Y.H.,
RA Serneels L., De Strooper B., Yu G., Bezprozvanny I.;
RT "Presenilins form ER Ca2+ leak channels, a function disrupted by familial
RT Alzheimer's disease-linked mutations.";
RL Cell 126:981-993(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-25; SER-30 AND
RP SER-52, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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).
CC -!- FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral membrane proteins such as Notch receptors and APP (amyloid-
CC beta precursor protein). Requires the other members of the gamma-
CC secretase complex to have a protease activity. May play a role in
CC intracellular signaling and gene expression or in linking chromatin to
CC the nuclear membrane. May function in the cytoplasmic partitioning of
CC proteins (By similarity). The holoprotein functions as a calcium-leak
CC channel that allows the passive movement of calcium from endoplasmic
CC reticulum to cytosol and is involved in calcium homeostasis
CC (PubMed:16959576). Is a regulator of mitochondrion-endoplasmic
CC reticulum membrane tethering and modulates calcium ions shuttling
CC between ER and mitochondria (By similarity).
CC {ECO:0000250|UniProtKB:P49810, ECO:0000269|PubMed:16959576}.
CC -!- SUBUNIT: Homodimer. Component of the gamma-secretase complex, a complex
CC composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN),
CC APH1 (APH1A or APH1B) and PEN2. Such minimal complex is sufficient for
CC secretase activity, although other components may exist. Interacts with
CC DOCK3. Interacts with HERPUD1, FLNA, FLNB and PARL (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61144-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61144-2; Sequence=VSP_008383, VSP_008384;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in the
CC liver.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A22A family. {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; U57324; AAC52937.1; -; mRNA.
DR EMBL; U57325; AAC53311.1; -; mRNA.
DR EMBL; AF038935; AAB92660.1; -; mRNA.
DR EMBL; AK014706; BAB29514.1; -; mRNA.
DR EMBL; BC010403; AAH10403.1; -; mRNA.
DR EMBL; U49111; AAC52935.1; -; mRNA.
DR CCDS; CCDS15567.1; -. [Q61144-1]
DR RefSeq; NP_001122077.1; NM_001128605.1.
DR RefSeq; NP_035313.2; NM_011183.3.
DR RefSeq; XP_006496775.1; XM_006496712.2.
DR RefSeq; XP_011237078.1; XM_011238776.2.
DR AlphaFoldDB; Q61144; -.
DR SMR; Q61144; -.
DR BioGRID; 202415; 11.
DR ComplexPortal; CPX-4236; Gamma-secretase complex, Aph1a-Psen2 variant.
DR ComplexPortal; CPX-4237; Gamma-secretase complex, Aph1b-Psen2 variant.
DR IntAct; Q61144; 1.
DR MINT; Q61144; -.
DR STRING; 10090.ENSMUSP00000010753; -.
DR MEROPS; A22.002; -.
DR iPTMnet; Q61144; -.
DR PhosphoSitePlus; Q61144; -.
DR SwissPalm; Q61144; -.
DR EPD; Q61144; -.
DR jPOST; Q61144; -.
DR MaxQB; Q61144; -.
DR PaxDb; Q61144; -.
DR PeptideAtlas; Q61144; -.
DR PRIDE; Q61144; -.
DR ProteomicsDB; 301997; -. [Q61144-1]
DR ProteomicsDB; 301998; -. [Q61144-2]
DR DNASU; 19165; -.
DR GeneID; 19165; -.
DR KEGG; mmu:19165; -.
DR UCSC; uc007dwe.1; mouse. [Q61144-2]
DR CTD; 5664; -.
DR MGI; MGI:109284; Psen2.
DR eggNOG; KOG2736; Eukaryota.
DR InParanoid; Q61144; -.
DR OrthoDB; 797738at2759; -.
DR PhylomeDB; Q61144; -.
DR Reactome; R-MMU-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-MMU-193692; Regulated proteolysis of p75NTR.
DR Reactome; R-MMU-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-MMU-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-MMU-9017802; Noncanonical activation of NOTCH3.
DR BioGRID-ORCS; 19165; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Psen2; mouse.
DR PRO; PR:Q61144; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61144; protein.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0070765; C:gamma-secretase complex; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:HGNC-UCL.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:HGNC-UCL.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IMP:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IMP:MGI.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; ISO:MGI.
DR GO; GO:0034205; P:amyloid-beta formation; ISO:MGI.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IDA:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0048854; P:brain morphogenesis; IGI:MGI.
DR GO; GO:0006816; P:calcium ion transport; IPI:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR GO; GO:0001708; P:cell fate specification; IGI:MGI.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IGI:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IGI:MGI.
DR GO; GO:0030900; P:forebrain development; IGI:MGI.
DR GO; GO:0001942; P:hair follicle development; IGI:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007611; P:learning or memory; IGI:MGI.
DR GO; GO:0040011; P:locomotion; IGI:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:HGNC-UCL.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IC:ComplexPortal.
DR GO; GO:0007613; P:memory; IGI:MGI.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; ISS:UniProtKB.
DR GO; GO:0002573; P:myeloid leukocyte differentiation; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IMP:BHF-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IMP:BHF-UCL.
DR GO; GO:0150076; P:neuroinflammatory response; IMP:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; IGI:CACAO.
DR GO; GO:0007220; P:Notch receptor processing; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:HGNC-UCL.
DR GO; GO:0050820; P:positive regulation of coagulation; IMP:MGI.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IMP:BHF-UCL.
DR GO; GO:0051604; P:protein maturation; IGI:MGI.
DR GO; GO:0019538; P:protein metabolic process; IGI:MGI.
DR GO; GO:0016485; P:protein processing; IGI:MGI.
DR GO; GO:0015031; P:protein transport; IGI:MGI.
DR GO; GO:0110097; P:regulation of calcium import into the mitochondrion; ISS:UniProtKB.
DR GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; IGI:MGI.
DR GO; GO:0043393; P:regulation of protein binding; IGI:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IGI:MGI.
DR GO; GO:0043589; P:skin morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001756; P:somitogenesis; IGI:MGI.
DR GO; GO:0002286; P:T cell activation involved in immune response; IGI:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IGI:MGI.
DR GO; GO:0048538; P:thymus development; IGI:MGI.
DR Gene3D; 1.10.472.100; -; 1.
DR InterPro; IPR001493; Pept_A22A_PS2.
DR InterPro; IPR001108; Peptidase_A22A.
DR InterPro; IPR006639; Preselin/SPP.
DR InterPro; IPR042524; Presenilin_C.
DR PANTHER; PTHR10202; PTHR10202; 1.
DR Pfam; PF01080; Presenilin; 2.
DR PRINTS; PR01072; PRESENILIN.
DR PRINTS; PR01074; PRESENILIN2.
DR SMART; SM00730; PSN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Membrane; Notch signaling pathway; Phosphoprotein; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..297
FT /note="Presenilin-2 NTF subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025607"
FT CHAIN 298..448
FT /note="Presenilin-2 CTF subunit"
FT /id="PRO_0000025608"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..138
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..200
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..249
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..388
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 414..416
FT /note="PAL"
FT ACT_SITE 263
FT /evidence="ECO:0000250"
FT ACT_SITE 366
FT /evidence="ECO:0000250"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT VAR_SEQ 296..332
FT /note="SAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFG -> CEWSHASARHW
FT GVSRWPFVEAWKWAVVLISDRLYILS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008383"
FT VAR_SEQ 333..448
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008384"
FT CONFLICT 40
FT /note="D -> G (in Ref. 3; BAB29514)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..87
FT /note="KR -> ND (in Ref. 3; BAB29514)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="R -> H (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="V -> A (in Ref. 1; AAC52937)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="Missing (in Ref. 2; AAB92660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 49983 MW; 54787212DCBB2C78 CRC64;
MLAFMASDSE EEVCDERTSL MSAESPTSRS CQEGRPGPED GESTAQWRTQ ESEEDCEEDP
DRYACSGAPG RPSGLEEELT LKYGAKRVIM LFVPVTLCMI VVVATIKSVR FYTEKNGQLI
YTPFTEDTPS VGQRLLNSVL NTLIMISVIV VMTIFLVVLY KYRCYKFIHG WLIMSSLMLL
FLFTYIYLGE VLKTYNVAMD YPTLFLAVWN FGAVGMVCIH WKGPLVLQQA YLIVISALMA
LVFIKYLPEW SAWVILGAIS VYDLVAVLCP KGPLRMLVET AQERNEPIFP ALIYSSAMVW
TVGMAKLDPS SQGALQLPYD PEMEEDSYDS FGEPSYPEAF EAPLPGYPGE ELEEEEERGV
KLGLGDFIFY SVLVGKAAAT GNGDWNTTLA CFIAILIGLC LTLLLLAVFK KALPALPISI
TFGLIFYFST DNLVRPFMDT LASHQLYI
