RTN3_MOUSE
ID RTN3_MOUSE Reviewed; 964 AA.
AC Q9ES97; Q3UF62; Q544J1; Q68FE4; Q6IM69; Q6R8K6; Q6R8K7; Q6T929; Q8C6D5;
AC Q8CCU2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Reticulon-3;
GN Name=Rtn3;
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 3).
RX PubMed=11990451;
RA Hamada N., Iwahashi J., Suzuki K., Ogi H., Kashiwagi T., Hara K.,
RA Toyoda M., Yamada T., Toyoda T.;
RT "Molecular cloning and characterization of the mouse reticulon 3 cDNA.";
RL Cell. Mol. Biol. 48:163-172(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND IDENTIFICATION (ISOFORM 4).
RX PubMed=12832288; DOI=10.1096/fj.02-1166hyp;
RA Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.;
RT "A reticular rhapsody: phylogenic evolution and nomenclature of the
RT RTN/Nogo gene family.";
RL FASEB J. 17:1238-1247(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 83-964 (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5),
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=FVB/N;
RX PubMed=15350194; DOI=10.1042/bj20040458;
RA Di Scala F., Dupuis L., Gaiddon C., De Tapia M., Jokic N.,
RA Gonzalez de Aguilar J.-L., Raul J.-S., Ludes B., Loeffler J.-P.;
RT "Tissue specificity and regulation of the N-terminal diversity of reticulon
RT 3.";
RL Biochem. J. 385:125-134(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15946766; DOI=10.1016/j.molbrainres.2005.04.020;
RA Cai Y., Saiyin H., Lin Q., Zhang P., Tang L., Pan X., Yu L.;
RT "Identification of a new RTN3 transcript, RTN3-A1, and its distribution in
RT adult mouse brain.";
RL Brain Res. Mol. Brain Res. 138:236-243(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Huang X., Zhou Y., Qiang H., Yuan J., Qiang B.;
RT "Cloning and expression profile of a novel mouse cDNA encoding a human RTN3
RT homolog.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Heart, Hippocampus, Medulla oblongata, Sympathetic ganglion, Thymus,
RC Tongue, and Vagina;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [8]
RP PROTEIN SEQUENCE OF 103-110; 153-164 AND 204-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [9]
RP INTERACTION WITH ATL1 AND ATL2.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the tubular
RT ER network.";
RL Cell 138:549-561(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-225; SER-230;
RP SER-233; SER-529; SER-596; SER-597 AND SER-673, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [11]
RP FUNCTION.
RX PubMed=24262037; DOI=10.1042/bj20131186;
RA Yamamoto Y., Yoshida A., Miyazaki N., Iwasaki K., Sakisaka T.;
RT "Arl6IP1 has the ability to shape the mammalian ER membrane in a reticulon-
RT like fashion.";
RL Biochem. J. 458:69-79(2014).
RN [12]
RP INTERACTION WITH TMEM33.
RX PubMed=25612671;
RA Urade T., Yamamoto Y., Zhang X., Ku Y., Sakisaka T.;
RT "Identification and characterization of TMEM33 as a reticulon-binding
RT protein.";
RL Kobe J. Med. Sci. 60:E57-E65(2014).
CC -!- FUNCTION: May be involved in membrane trafficking in the early
CC secretory pathway. Inhibits BACE1 activity and amyloid precursor
CC protein processing. May induce caspase-8 cascade and apoptosis. May
CC favor BCL2 translocation to the mitochondria upon endoplasmic reticulum
CC stress (PubMed:24262037). Induces the formation of endoplasmic
CC reticulum tubules. Acts also as an inflammation-resolving regulator by
CC interacting with both TRIM25 and RIG-I/DDX58, subsequently impairing
CC DDX58 'Lys-63'-linked polyubiquitination leading to IRF3 and NF-kappa-B
CC inhibition (By similarity). {ECO:0000250|UniProtKB:O95197,
CC ECO:0000269|PubMed:24262037}.
CC -!- SUBUNIT: Homodimer. Interacts with RTN4. Isoform 3 interacts with
CC BACE1, BACE2, BCL2 and FADD (By similarity). Interacts with ATL1 and
CC ATL2 (PubMed:19665976). Isoform 3 interacts with TMEM33
CC (PubMed:25612671). Interacts with ZFYVE27 and with KIF5A in a ZFYVE27-
CC dependent manner (By similarity). Interacts with DDX58 (By similarity).
CC Interacts with TRIM25 (By similarity). {ECO:0000250|UniProtKB:O95197,
CC ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:25612671}.
CC -!- INTERACTION:
CC Q9ES97-3; Q8WXF7: ATL1; Xeno; NbExp=3; IntAct=EBI-1487798, EBI-2410266;
CC Q9ES97-3; Q8NHH9: ATL2; Xeno; NbExp=2; IntAct=EBI-1487798, EBI-2410430;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15350194}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15350194}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O95197}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=A1, A4b, B;
CC IsoId=Q9ES97-1; Sequence=Displayed;
CC Name=2; Synonyms=A2, A3b;
CC IsoId=Q9ES97-2; Sequence=VSP_023763;
CC Name=3; Synonyms=B1, A1, Rtn3c;
CC IsoId=Q9ES97-3; Sequence=VSP_023762;
CC Name=4; Synonyms=B2, A2;
CC IsoId=Q9ES97-4; Sequence=VSP_023764;
CC Name=5; Synonyms=A4a;
CC IsoId=Q9ES97-5; Sequence=VSP_023765;
CC -!- TISSUE SPECIFICITY: Isoform 1, isoform 3, isoform 4 and isoform 5 are
CC expressed in spinal cord. Isoform 1 is present in brain, where it is
CC expressed in the neurons of cerebral cortex, hippocampus, hypothalamus
CC and cerebellum (at protein level). {ECO:0000269|PubMed:15350194,
CC ECO:0000269|PubMed:15946766}.
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DR EMBL; AB046114; BAB62070.1; -; mRNA.
DR EMBL; BK001796; DAA01968.1; -; mRNA.
DR EMBL; AY164700; AAP47278.1; -; mRNA.
DR EMBL; AY507126; AAR98631.1; -; mRNA.
DR EMBL; AY507127; AAR98632.1; -; mRNA.
DR EMBL; AY427822; AAR08193.1; -; mRNA.
DR EMBL; AY750849; AAU81931.1; -; mRNA.
DR EMBL; AF195940; AAG31360.1; -; mRNA.
DR EMBL; AK032109; BAC27708.1; -; mRNA.
DR EMBL; AK036892; BAC29625.1; -; mRNA.
DR EMBL; AK049845; BAC33952.1; -; mRNA.
DR EMBL; AK075883; BAC36028.1; -; mRNA.
DR EMBL; AK088670; BAC40493.1; -; mRNA.
DR EMBL; AK146505; BAE27220.1; -; mRNA.
DR EMBL; AK148792; BAE28664.1; -; mRNA.
DR EMBL; AK148947; BAE28699.1; -; mRNA.
DR EMBL; AK165683; BAE38336.1; -; mRNA.
DR EMBL; BC014697; AAH14697.1; -; mRNA.
DR EMBL; BC036717; AAH36717.1; -; mRNA.
DR EMBL; BC079882; AAH79882.1; -; mRNA.
DR CCDS; CCDS29525.1; -. [Q9ES97-2]
DR CCDS; CCDS29526.1; -. [Q9ES97-3]
DR CCDS; CCDS37906.1; -. [Q9ES97-1]
DR CCDS; CCDS70927.1; -. [Q9ES97-4]
DR CCDS; CCDS89331.1; -. [Q9ES97-5]
DR RefSeq; NP_001003933.1; NM_001003933.2. [Q9ES97-2]
DR RefSeq; NP_001003934.1; NM_001003934.2. [Q9ES97-1]
DR RefSeq; NP_001258415.1; NM_001271486.1. [Q9ES97-5]
DR RefSeq; NP_001258416.1; NM_001271487.1. [Q9ES97-4]
DR RefSeq; NP_444306.1; NM_053076.3. [Q9ES97-3]
DR AlphaFoldDB; Q9ES97; -.
DR SMR; Q9ES97; -.
DR BioGRID; 203034; 6.
DR CORUM; Q9ES97; -.
DR IntAct; Q9ES97; 5.
DR STRING; 10090.ENSMUSP00000065810; -.
DR TCDB; 8.A.102.1.2; the reticulon (reticulon) family.
DR iPTMnet; Q9ES97; -.
DR PhosphoSitePlus; Q9ES97; -.
DR SwissPalm; Q9ES97; -.
DR EPD; Q9ES97; -.
DR jPOST; Q9ES97; -.
DR MaxQB; Q9ES97; -.
DR PaxDb; Q9ES97; -.
DR PeptideAtlas; Q9ES97; -.
DR PRIDE; Q9ES97; -.
DR ProteomicsDB; 256803; -. [Q9ES97-1]
DR ProteomicsDB; 256804; -. [Q9ES97-2]
DR ProteomicsDB; 256805; -. [Q9ES97-3]
DR ProteomicsDB; 256806; -. [Q9ES97-4]
DR ProteomicsDB; 256807; -. [Q9ES97-5]
DR TopDownProteomics; Q9ES97-1; -. [Q9ES97-1]
DR TopDownProteomics; Q9ES97-3; -. [Q9ES97-3]
DR TopDownProteomics; Q9ES97-4; -. [Q9ES97-4]
DR TopDownProteomics; Q9ES97-5; -. [Q9ES97-5]
DR Antibodypedia; 2923; 203 antibodies from 32 providers.
DR DNASU; 20168; -.
DR Ensembl; ENSMUST00000025667; ENSMUSP00000025667; ENSMUSG00000024758. [Q9ES97-4]
DR Ensembl; ENSMUST00000065304; ENSMUSP00000065810; ENSMUSG00000024758. [Q9ES97-1]
DR Ensembl; ENSMUST00000088169; ENSMUSP00000085494; ENSMUSG00000024758. [Q9ES97-3]
DR Ensembl; ENSMUST00000088171; ENSMUSP00000085496; ENSMUSG00000024758. [Q9ES97-2]
DR Ensembl; ENSMUST00000235593; ENSMUSP00000158024; ENSMUSG00000024758. [Q9ES97-5]
DR GeneID; 20168; -.
DR KEGG; mmu:20168; -.
DR UCSC; uc008glb.2; mouse. [Q9ES97-1]
DR UCSC; uc008gld.2; mouse. [Q9ES97-2]
DR UCSC; uc008gle.2; mouse. [Q9ES97-3]
DR UCSC; uc012bhv.2; mouse. [Q9ES97-5]
DR UCSC; uc033hiw.1; mouse. [Q9ES97-4]
DR CTD; 10313; -.
DR MGI; MGI:1339970; Rtn3.
DR VEuPathDB; HostDB:ENSMUSG00000024758; -.
DR eggNOG; KOG1792; Eukaryota.
DR GeneTree; ENSGT00940000157482; -.
DR HOGENOM; CLU_011704_0_0_1; -.
DR InParanoid; Q9ES97; -.
DR OMA; KYQDHVD; -.
DR OrthoDB; 423549at2759; -.
DR PhylomeDB; Q9ES97; -.
DR TreeFam; TF105431; -.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 20168; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Rtn3; mouse.
DR PRO; PR:Q9ES97; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9ES97; protein.
DR Bgee; ENSMUSG00000024758; Expressed in facial nucleus and 273 other tissues.
DR Genevisible; Q9ES97; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0071787; P:endoplasmic reticulum tubular network formation; IDA:UniProtKB.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; ISO:MGI.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR003388; Reticulon.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT CHAIN 2..964
FT /note="Reticulon-3"
FT /id="PRO_0000168164"
FT TOPO_DOM 2..795
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 796..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 820..876
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 877..899
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 900..903
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 904..926
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 927..964
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 776..964
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..964
FT /note="Interaction with FADD"
FT /evidence="ECO:0000250"
FT REGION 932..934
FT /note="Interaction with BACE1"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6RJR6"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95197"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 593
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6RJR6"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 49..775
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11990451,
FT ECO:0000303|PubMed:12832288, ECO:0000303|PubMed:15350194,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|Ref.5"
FT /id="VSP_023762"
FT VAR_SEQ 49..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15946766"
FT /id="VSP_023763"
FT VAR_SEQ 68..775
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_023764"
FT VAR_SEQ 68..388
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023765"
FT CONFLICT 17
FT /note="S -> P (in Ref. 3; AAR98631)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="S -> P (in Ref. 3; AAR98632)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="E -> G (in Ref. 3; AAR98632)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="M -> I (in Ref. 6; BAC36028)"
FT /evidence="ECO:0000305"
FT CONFLICT 964
FT /note="E -> K (in Ref. 6; BAE28664/BAE28699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 964 AA; 103879 MW; 5170809A696F8F7A CRC64;
MAESSAATQS PSVSSSSSGA EPSALGGGGG SPGACPALGA KSCGSSCADS FVSSSSSQPV
SIFSTSQAGL SSLCSDEPPS KSMTSSFLSS SEIHNPDPTT PLGEKSETLG SQFVLAKGKD
PLVLLDKKKL DSPQGTNKDR VDAPVSLATG IPCSHPSIPD SFPEQPAFLS KEIGPAEEWV
VKDQEPKNPN KVPDGEDRSA LDFGQSKAEH ICTYSLSPSE LPVASVEKDS PESPFEVIID
KATFDREFKD LYKENPNDLG GWAAHGDRES PADLLEMNDK LFPLRNKEAG RYPSSVLLGR
QFSHTTAALE EVSRCVNDMH NFTNEILTWD LDPQAKQQAN KTSCTTESTG LDRSELRSEI
PVINLKTNPQ QKMPVCSFNG STPITKSTGD WTEAFTEGKP VRDYLSSTKE AGGNGVPGSS
QLHSELPGSM PEKWVSGSGA ATVEVTLPNL RGAWPNSVMG EVTEVDSSGE SDDTVIEDIT
EKPDSLPSAA AKTSEREIKE TPSRETVRSE MCENSEQPQA QPETPTQKSL EGEVASQVPN
TLNEVTPEKL DMTNNPKVCS AAPPSVLNET GFSLTVPASA KLESLLGKYV EDTDGSSPED
LMAVLTGAEE KGIVDKEEGD VLEAVLEKIA DFKNTLPVEL LHESELSGSE TKNIKSKYSE
DSRETTGGAP TMSPDLEQEQ LTIRAIKELG ERQAEKVQDE GISSGGKLKQ TFAPQSGPQS
SSDILEHTDV KTGSDLGIPK NPTIIKNTRI DSISSLTKTE MVNKNVLARL LSDFPVHDLI
FWRDVKKTGF VFGTTLIMLL SLAAFSVISV VSYLILALLS VTISFRVYKS VIQAVQKSEE
GHPFKAYLDV DITLSSEAFH NYMNAAMVHV NKALKLIIRL FLVEDLVDSL KLAVFMWLMT
YVGAVFNGIT LLILAELLVF SVPIVYEKYK TQIDHYVGIA RDQTKSIVEK IQAKLPGIAK
KKAE
