PLIN5_MOUSE
ID PLIN5_MOUSE Reviewed; 463 AA.
AC Q8BVZ1; Q78IK8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Perilipin-5;
DE AltName: Full=Lipid droplet-associated protein PAT-1;
DE AltName: Full=Lipid storage droplet protein 5;
DE AltName: Full=Myocardial LD protein;
GN Name=Plin5; Synonyms=Lsdp5, Mldp, Oxpat, Pat1;
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), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INDUCTION, AND ALTERNATIVE INITIATION.
RC STRAIN=C57BL/6J;
RX PubMed=17234449; DOI=10.1016/j.bbalip.2006.11.011;
RA Dalen K.T., Dahl T., Holter E., Arntsen B., Londos C., Sztalryd C.,
RA Nebb H.I.;
RT "LSDP5 is a PAT protein specifically expressed in fatty acid oxidizing
RT tissues.";
RL Biochim. Biophys. Acta 1771:210-227(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RA Tansey J.T., Kimmel A.R., Hlavin E.M., Dickey L.O., Londos C.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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].
RC STRAIN=FVB/N; TISSUE=Liver;
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 FUNCTION IN LIPOLYSIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=17130488; DOI=10.2337/db06-0399;
RA Wolins N.E., Quaynor B.K., Skinner J.R., Tzekov A., Croce M.A.,
RA Gropler M.C., Varma V., Yao-Borengasser A., Rasouli N., Kern P.A.,
RA Finck B.N., Bickel P.E.;
RT "OXPAT/PAT-1 is a PPAR-induced lipid droplet protein that promotes fatty
RT acid utilization.";
RL Diabetes 55:3418-3428(2006).
RN [6]
RP IDENTIFICATION, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16571721; DOI=10.1074/jbc.m601682200;
RA Yamaguchi T., Matsushita S., Motojima K., Hirose F., Osumi T.;
RT "MLDP, a novel PAT family protein localized to lipid droplets and enriched
RT in the heart, is regulated by peroxisome proliferator-activated receptor
RT alpha.";
RL J. Biol. Chem. 281:14232-14240(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, 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 [8]
RP FUNCTION IN LIPOLYSIS, AND INTERACTION WITH ABHD5.
RX PubMed=19064991; DOI=10.1074/jbc.m808251200;
RA Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z.;
RT "Functional interactions between Mldp (LSDP5) and Abhd5 in the control of
RT intracellular lipid accumulation.";
RL J. Biol. Chem. 284:3049-3057(2009).
RN [9]
RP INTERACTION WITH LIPE, AND SUBCELLULAR LOCATION.
RX PubMed=19717842; DOI=10.1074/jbc.m109.006726;
RA Wang H., Hu L., Dalen K., Dorward H., Marcinkiewicz A., Russell D.,
RA Gong D., Londos C., Yamaguchi T., Holm C., Rizzo M.A., Brasaemle D.,
RA Sztalryd C.;
RT "Activation of hormone-sensitive lipase requires two steps, protein
RT phosphorylation and binding to the PAT-1 domain of lipid droplet coat
RT proteins.";
RL J. Biol. Chem. 284:32116-32125(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-163, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, and Lung;
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 [11]
RP INTERACTION WITH ABHD5 AND PNPLA2, REGION, AND HOMOOLIGOMERIZATION.
RX PubMed=21148142; DOI=10.1074/jbc.m110.180711;
RA Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z., Zhou L.;
RT "Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase.";
RL J. Biol. Chem. 286:5126-5135(2011).
RN [12]
RP FUNCTION IN LIPOLYSIS, INTERACTION WITH PNPLA2, REGION, AND PHOSPHORYLATION
RP BY PKA.
RX PubMed=21393244; DOI=10.1074/jbc.m110.207779;
RA Wang H., Bell M., Sreenivasan U., Sreenevasan U., Hu H., Liu J., Dalen K.,
RA Londos C., Yamaguchi T., Rizzo M.A., Coleman R., Gong D., Brasaemle D.,
RA Sztalryd C.;
RT "Unique regulation of adipose triglyceride lipase (ATGL) by perilipin 5, a
RT lipid droplet-associated protein.";
RL J. Biol. Chem. 286:15707-15715(2011).
RN [13]
RP FUNCTION IN LIPID HOMEOSTASIS, AND REGION.
RX PubMed=21885430; DOI=10.1194/jlr.m017939;
RA Wang H., Sreenivasan U., Sreenevasan U., Hu H., Saladino A., Polster B.M.,
RA Lund L.M., Gong D.W., Stanley W.C., Sztalryd C.;
RT "Perilipin 5, a lipid droplet-associated protein, provides physical and
RT metabolic linkage to mitochondria.";
RL J. Lipid Res. 52:2159-2168(2011).
RN [14]
RP FUNCTION IN LIPOGENESIS, AND DISRUPTION PHENOTYPE.
RX PubMed=22532565; DOI=10.1074/jbc.m111.328708;
RA Kuramoto K., Okamura T., Yamaguchi T., Nakamura T.Y., Wakabayashi S.,
RA Morinaga H., Nomura M., Yanase T., Otsu K., Usuda N., Matsumura S.,
RA Inoue K., Fushiki T., Kojima Y., Hashimoto T., Sakai F., Hirose F.,
RA Osumi T.;
RT "Perilipin 5, a lipid droplet-binding protein, protects heart from
RT oxidative burden by sequestering fatty acid from excessive oxidation.";
RL J. Biol. Chem. 287:23852-23863(2012).
RN [15]
RP FUNCTION IN LIPID STORAGE, AND REGION.
RX PubMed=22675471; DOI=10.1371/journal.pone.0036712;
RA Li H., Song Y., Zhang L.J., Gu Y., Li F.F., Pan S.Y., Jiang L.N., Liu F.,
RA Ye J., Li Q.;
RT "LSDP5 enhances triglyceride storage in hepatocytes by influencing
RT lipolysis and fatty acid beta-oxidation of lipid droplets.";
RL PLoS ONE 7:E36712-E36712(2012).
RN [16]
RP INDUCTION.
RX PubMed=23423172; DOI=10.1152/ajpendo.00523.2012;
RA Chen W., Chang B., Wu X., Li L., Sleeman M., Chan L.;
RT "Inactivation of Plin4 downregulates Plin5 and reduces cardiac lipid
RT accumulation in mice.";
RL Am. J. Physiol. 304:E770-E779(2013).
RN [17] {ECO:0000305}
RP FUNCTION IN LYPOLYSIS, AND SUBCELLULAR LOCATION.
RX PubMed=23345411; DOI=10.1194/jlr.m032466;
RA Wang H., Sreenivasan U., Gong D.W., O'Connell K.A., Dabkowski E.R.,
RA Hecker P.A., Ionica N., Konig M., Mahurkar A., Sun Y., Stanley W.C.,
RA Sztalryd C.;
RT "Cardiomyocyte-specific perilipin 5 overexpression leads to myocardial
RT steatosis and modest cardiac dysfunction.";
RL J. Lipid Res. 54:953-965(2013).
RN [18]
RP INDUCTION.
RX PubMed=23606724; DOI=10.1194/jlr.m038992;
RA Bindesboll C., Berg O., Arntsen B., Nebb H.I., Dalen K.T.;
RT "Fatty acids regulate perilipin5 in muscle by activating PPARdelta.";
RL J. Lipid Res. 54:1949-1963(2013).
CC -!- FUNCTION: Lipid droplet-associated protein that maintains the balance
CC between lipogenesis and lipolysis and also regulates fatty acid
CC oxidation in oxidative tissues. Recruits mitochondria to the surface of
CC lipid droplets and is involved in lipid droplet homeostasis by
CC regulating both the storage of fatty acids in the form of triglycerides
CC and the release of fatty acids for mitochondrial fatty acid oxidation.
CC In lipid droplet triacylglycerol hydrolysis, plays a role as a
CC scaffolding protein for three major key lipolytic players: ABHD5,
CC PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of
CC PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets.
CC Phosphorylation by PKA enables lipolysis probably by promoting release
CC of ABHD5 from the perilipin scaffold and by facilitating interaction of
CC ABHD5 with PNPLA2. Also increases lipolysis through interaction with
CC LIPE and upon PKA-mediated phosphorylation of LIPE.
CC {ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:19064991,
CC ECO:0000269|PubMed:21393244, ECO:0000269|PubMed:21885430,
CC ECO:0000269|PubMed:22532565, ECO:0000269|PubMed:22675471,
CC ECO:0000269|PubMed:23345411}.
CC -!- SUBUNIT: Homooligomer. Interacts with PNPLA2; prevents interaction of
CC PNPLA2 with ABHD5. Interacts with ABHD5; targets ABHD5 to lipid
CC droplets and promotes interaction of ABHD5 with PNPLA2. Interacts with
CC LIPE. {ECO:0000269|PubMed:19064991, ECO:0000269|PubMed:19717842,
CC ECO:0000269|PubMed:21148142, ECO:0000269|PubMed:21393244}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:16571721,
CC ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:17234449,
CC ECO:0000269|PubMed:19717842, ECO:0000269|PubMed:23345411}. Cytoplasm
CC {ECO:0000269|PubMed:17234449, ECO:0000269|PubMed:19717842}.
CC Mitochondrion {ECO:0000250|UniProtKB:M0R7Z9}. Note=Lipid droplet
CC surface-associated (PubMed:17234449, PubMed:17130488, PubMed:16571721).
CC Exchanges between lipid droplets and the cytoplasm (PubMed:19717842).
CC {ECO:0000269|PubMed:16571721, ECO:0000269|PubMed:17130488,
CC ECO:0000269|PubMed:17234449, ECO:0000269|PubMed:19717842}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BVZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BVZ1-2; Sequence=VSP_034085;
CC -!- TISSUE SPECIFICITY: Highly expressed in oxidative tissues, including
CC heart, liver, brown adipose tissue (BAT) and slow-twitch fibers of
CC skeletal muscle. Lower expression in epididymal white adipose tissue
CC and anterior tibialis and quadriceps. Expressed in adrenal glands.
CC Isoform 2 has the highest expression in heart.
CC {ECO:0000269|PubMed:16571721, ECO:0000269|PubMed:17130488,
CC ECO:0000269|PubMed:17234449}.
CC -!- INDUCTION: Up-regulated by fasting, PPARD, PPARA and PLIN4. Increased
CC in muscle of high-fat diet fed mice. Induced by unsaturated long chain
CC fatty acid in muscle. {ECO:0000269|PubMed:16571721,
CC ECO:0000269|PubMed:17130488, ECO:0000269|PubMed:17234449,
CC ECO:0000269|PubMed:23423172, ECO:0000269|PubMed:23606724}.
CC -!- PTM: Phosphorylated by PKA. Phosphorylated on serine in skeletal muscle
CC at rest or with lipolytic stimulation. {ECO:0000269|PubMed:21393244}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice lack detectable lipid
CC droplets in heart. The triacylglycerol and fatty acid content in heart
CC is lower. {ECO:0000269|PubMed:22532565}.
CC -!- SIMILARITY: Belongs to the perilipin family. {ECO:0000305}.
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DR EMBL; DQ473305; ABF13218.1; -; mRNA.
DR EMBL; AY919875; AAX12443.1; -; mRNA.
DR EMBL; AK075872; BAC36019.1; -; mRNA.
DR EMBL; BC024138; AAH24138.2; -; mRNA.
DR CCDS; CCDS37662.1; -. [Q8BVZ1-1]
DR RefSeq; NP_001070816.1; NM_001077348.1. [Q8BVZ1-1]
DR RefSeq; NP_080150.2; NM_025874.3. [Q8BVZ1-1]
DR AlphaFoldDB; Q8BVZ1; -.
DR SMR; Q8BVZ1; -.
DR BioGRID; 211843; 2.
DR STRING; 10090.ENSMUSP00000019808; -.
DR iPTMnet; Q8BVZ1; -.
DR PhosphoSitePlus; Q8BVZ1; -.
DR SwissPalm; Q8BVZ1; -.
DR jPOST; Q8BVZ1; -.
DR MaxQB; Q8BVZ1; -.
DR PaxDb; Q8BVZ1; -.
DR PeptideAtlas; Q8BVZ1; -.
DR PRIDE; Q8BVZ1; -.
DR ProteomicsDB; 289620; -. [Q8BVZ1-1]
DR ProteomicsDB; 289621; -. [Q8BVZ1-2]
DR Antibodypedia; 23670; 174 antibodies from 15 providers.
DR Ensembl; ENSMUST00000019808; ENSMUSP00000019808; ENSMUSG00000011305. [Q8BVZ1-1]
DR Ensembl; ENSMUST00000113072; ENSMUSP00000108695; ENSMUSG00000011305. [Q8BVZ1-1]
DR GeneID; 66968; -.
DR KEGG; mmu:66968; -.
DR UCSC; uc008daz.1; mouse. [Q8BVZ1-1]
DR CTD; 440503; -.
DR MGI; MGI:1914218; Plin5.
DR VEuPathDB; HostDB:ENSMUSG00000011305; -.
DR eggNOG; KOG4790; Eukaryota.
DR GeneTree; ENSGT00950000182920; -.
DR HOGENOM; CLU_035133_1_0_1; -.
DR InParanoid; Q8BVZ1; -.
DR OMA; ISTDQDQ; -.
DR OrthoDB; 1437332at2759; -.
DR PhylomeDB; Q8BVZ1; -.
DR TreeFam; TF328397; -.
DR BioGRID-ORCS; 66968; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q8BVZ1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BVZ1; protein.
DR Bgee; ENSMUSG00000011305; Expressed in interventricular septum and 131 other tissues.
DR Genevisible; Q8BVZ1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0035473; F:lipase binding; IPI:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IMP:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019915; P:lipid storage; IDA:CACAO.
DR GO; GO:0051646; P:mitochondrion localization; IMP:UniProtKB.
DR GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; IDA:UniProtKB.
DR GO; GO:0060192; P:negative regulation of lipase activity; IMP:UniProtKB.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:UniProtKB.
DR GO; GO:0035359; P:negative regulation of peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IDA:UniProtKB.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IDA:UniProtKB.
DR GO; GO:0060193; P:positive regulation of lipase activity; ISS:UniProtKB.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
DR GO; GO:0010890; P:positive regulation of sequestering of triglyceride; IDA:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR004279; Perilipin.
DR Pfam; PF03036; Perilipin; 1.
DR PIRSF; PIRSF036881; PAT; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cytoplasm; Lipid droplet; Lipid metabolism;
KW Mitochondrion; Phosphoprotein; Reference proteome.
FT CHAIN 1..463
FT /note="Perilipin-5"
FT /id="PRO_0000338983"
FT REGION 1..188
FT /note="Essential for lipid droplet targeting"
FT REGION 1..123
FT /note="Interaction with LIPE"
FT /evidence="ECO:0000269|PubMed:19717842"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..463
FT /note="Interaction with PNPLA2 and ABHD5"
FT REGION 433..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..463
FT /note="Necessary for mitochondria recruitment at the lipid
FT droplet surface"
FT COMPBIAS 13..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00G26"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034085"
SQ SEQUENCE 463 AA; 50474 MW; E232342603E3F303 CRC64;
MDQRGEDTTL APHSRMSGDQ TAQDPGSSLG ELDQQNVVNR VVALPLVKAT CTAVSSAYNS
AKDRHPLLGS ACRLAEHCVC SVTTCALDHA QPLLEHLQPQ LATVNDLACR GLDKLEEKLP
FLQQPSDMVV TSAKDTVAKS VTGMVDLAQR GRRWSGELRR SMSQAMDMVL GKSEKLVDRF
LPMTEAELAV LAAEAEGPEV GTVEEQRQQQ GYFVRLGSLS ARLRHLAYEH SLGKLRQSKH
RTQEMLAQLQ ETLELIQHMQ RGASPSPTFH PPKTQELWGS WSPCLENGRS HSEVELETLA
LSRSLTLELQ NAVDALAGCV RGLPPSAQAK VAEVQRSVDA LQATFADAHC LGDVAPTALA
EGRGSVARAH ACVDEFLDLV LRAMPLPWLV GPFAPILVEQ SEPLINLATC VDEVVGDPDP
RWAHMDWPAQ KRAWEAESAD PGGQEAEPPR GQGKHTMMPE LDF
