NDRG2_MOUSE
ID NDRG2_MOUSE Reviewed; 371 AA.
AC Q9QYG0; Q3TI48; Q3TY42; Q3U3T5; Q69ZN2; Q8C661;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein NDRG2;
DE AltName: Full=N-myc downstream-regulated gene 2 protein;
DE AltName: Full=Protein Ndr2;
GN Name=Ndrg2; Synonyms=Kiaa1248, Ndr2;
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=Embryo;
RX PubMed=10581191; DOI=10.1006/bbrc.1999.1780;
RA Okuda T., Kondoh H.;
RT "Identification of new genes ndr2 and ndr3 which are related to
RT Ndr1/RTP/Drg1 but show distinct tissue specificity and response to N-myc.";
RL Biochem. Biophys. Res. Commun. 266:208-215(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Head, and Visual cortex;
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 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 [4]
RP PROTEIN SEQUENCE OF 62-84; 155-176 AND 278-287, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-371.
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [6]
RP PHOSPHORYLATION AT THR-330; SER-332; THR-348 AND SER-350, AND TISSUE
RP SPECIFICITY.
RX PubMed=15461589; DOI=10.1042/bj20041057;
RA Murray J.T., Campbell D.G., Morrice N., Auld G.C., Shpiro N., Marquez R.,
RA Peggie M., Bain J., Bloomberg G.B., Grahammer F., Lang F., Wulff P.,
RA Kuhl D., Cohen P.;
RT "Exploitation of KESTREL to identify NDRG family members as physiological
RT substrates for SGK1 and GSK3.";
RL Biochem. J. 384:477-488(2004).
RN [7]
RP PHOSPHORYLATION AT SER-332 AND THR-348, AND SUBCELLULAR LOCATION.
RX PubMed=14985363; DOI=10.1074/jbc.m401504200;
RA Burchfield J.G., Lennard A.J., Narasimhan S., Hughes W.E., Wasinger V.C.,
RA Corthals G.L., Okuda T., Kondoh H., Biden T.J., Schmitz-Peiffer C.;
RT "Akt mediates insulin-stimulated phosphorylation of Ndrg2: evidence for
RT cross-talk with protein kinase C theta.";
RL J. Biol. Chem. 279:18623-18632(2004).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=15207261; DOI=10.1016/j.nbd.2004.01.003;
RA Mitchelmore C., Buechmann-Moller S., Rask L., West M.J., Troncoso J.C.,
RA Jensen N.A.;
RT "NDRG2: a novel Alzheimer's disease associated protein.";
RL Neurobiol. Dis. 16:48-58(2004).
RN [9]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16520977; DOI=10.1007/s00441-005-0137-5;
RA Hu X.-L., Liu X.-P., Deng Y.-C., Lin S.-X., Wu L., Zhang J., Wang L.-F.,
RA Wang X.-B., Li X., Shen L., Zhang Y.-Q., Yao L.-B.;
RT "Expression analysis of the NDRG2 gene in mouse embryonic and adult
RT tissues.";
RL Cell Tissue Res. 325:67-76(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; THR-330; SER-332;
RP THR-334; SER-335; SER-338 AND THR-357, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-328; THR-330 AND
RP SER-332, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; THR-330; SER-332;
RP THR-334; SER-335; SER-338; SER-344; THR-348; SER-350; SER-352; SER-353;
RP SER-355 AND SER-370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP TISSUE SPECIFICITY.
RX PubMed=21636852; DOI=10.1074/jbc.m111.256446;
RA Yamamoto H., Kokame K., Okuda T., Nakajo Y., Yanamoto H., Miyata T.;
RT "NDRG4 protein-deficient mice exhibit spatial learning deficits and
RT vulnerabilities to cerebral ischemia.";
RL J. Biol. Chem. 286:26158-26165(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 40-313.
RX PubMed=21247902; DOI=10.1074/jbc.m110.170803;
RA Hwang J., Kim Y., Kang H.B., Jaroszewski L., Deacon A.M., Lee H.,
RA Choi W.C., Kim K.J., Kim C.H., Kang B.S., Lee J.O., Oh T.K., Kim J.W.,
RA Wilson I.A., Kim M.H.;
RT "Crystal structure of the human N-Myc downstream-regulated gene 2 protein
RT provides insight into its role as a tumor suppressor.";
RL J. Biol. Chem. 286:12450-12460(2011).
CC -!- FUNCTION: Contributes to the regulation of the Wnt signaling pathway.
CC Down-regulates CTNNB1-mediated transcriptional activation of target
CC genes, such as CCND1, and may thereby act as tumor suppressor. May be
CC involved in dendritic cell and neuron differentiation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14985363,
CC ECO:0000269|PubMed:16520977}. Cytoplasm, perinuclear region
CC {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=In
CC neurons, seems to concentrate at axonal growth cone. Perinuclear in
CC neurons (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QYG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QYG0-2; Sequence=VSP_019009;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in brain, heart and
CC liver, and at lower levels in kidney, colon, skeletal muscle, adrenal
CC gland, ovary and uterus (at protein level).
CC {ECO:0000269|PubMed:15461589, ECO:0000269|PubMed:16520977,
CC ECO:0000269|PubMed:21636852}.
CC -!- DEVELOPMENTAL STAGE: Expression is restricted to the developing heart
CC at the stage of 9.5 dpc, and increases after 11.5 dpc as development of
CC tissues and organs proceeds. Present in many developing tissues
CC including heart, brain, lung, liver, gut, kidney, skeletal muscle,
CC cartilage and epidermis (at protein level).
CC {ECO:0000269|PubMed:15207261, ECO:0000269|PubMed:16520977}.
CC -!- SIMILARITY: Belongs to the NDRG family. {ECO:0000305}.
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DR EMBL; AB033921; BAA85882.1; -; mRNA.
DR EMBL; AK076514; BAC36373.1; -; mRNA.
DR EMBL; AK154597; BAE32700.1; -; mRNA.
DR EMBL; AK158900; BAE34721.1; -; mRNA.
DR EMBL; AK168011; BAE39998.1; -; mRNA.
DR EMBL; BC012963; AAH12963.1; -; mRNA.
DR EMBL; AK173136; BAD32414.1; -; mRNA.
DR CCDS; CCDS27047.1; -. [Q9QYG0-1]
DR CCDS; CCDS49486.1; -. [Q9QYG0-2]
DR RefSeq; NP_001139431.1; NM_001145959.1. [Q9QYG0-2]
DR RefSeq; NP_038892.1; NM_013864.2. [Q9QYG0-1]
DR RefSeq; XP_006519161.2; XM_006519098.3.
DR RefSeq; XP_006519162.2; XM_006519099.3.
DR RefSeq; XP_006519166.1; XM_006519103.1.
DR RefSeq; XP_006519167.1; XM_006519104.3.
DR RefSeq; XP_006519168.1; XM_006519105.2.
DR RefSeq; XP_017171534.1; XM_017316045.1.
DR RefSeq; XP_017171535.1; XM_017316046.1.
DR RefSeq; XP_017171536.1; XM_017316047.1.
DR RefSeq; XP_017171538.1; XM_017316049.1.
DR RefSeq; XP_017171539.1; XM_017316050.1.
DR RefSeq; XP_017171540.1; XM_017316051.1.
DR PDB; 2QMQ; X-ray; 1.70 A; A=40-313.
DR PDBsum; 2QMQ; -.
DR AlphaFoldDB; Q9QYG0; -.
DR SMR; Q9QYG0; -.
DR BioGRID; 205892; 9.
DR IntAct; Q9QYG0; 2.
DR STRING; 10090.ENSMUSP00000004673; -.
DR ESTHER; mouse-ndr2; Ndr_family.
DR iPTMnet; Q9QYG0; -.
DR PhosphoSitePlus; Q9QYG0; -.
DR SwissPalm; Q9QYG0; -.
DR EPD; Q9QYG0; -.
DR jPOST; Q9QYG0; -.
DR MaxQB; Q9QYG0; -.
DR PaxDb; Q9QYG0; -.
DR PeptideAtlas; Q9QYG0; -.
DR PRIDE; Q9QYG0; -.
DR ProteomicsDB; 286161; -. [Q9QYG0-1]
DR ProteomicsDB; 286162; -. [Q9QYG0-2]
DR Antibodypedia; 142; 388 antibodies from 38 providers.
DR DNASU; 29811; -.
DR Ensembl; ENSMUST00000004673; ENSMUSP00000004673; ENSMUSG00000004558. [Q9QYG0-1]
DR Ensembl; ENSMUST00000111632; ENSMUSP00000107259; ENSMUSG00000004558. [Q9QYG0-2]
DR GeneID; 29811; -.
DR KEGG; mmu:29811; -.
DR UCSC; uc007tnk.2; mouse. [Q9QYG0-1]
DR UCSC; uc007tnl.2; mouse. [Q9QYG0-2]
DR CTD; 57447; -.
DR MGI; MGI:1352498; Ndrg2.
DR VEuPathDB; HostDB:ENSMUSG00000004558; -.
DR eggNOG; KOG2931; Eukaryota.
DR GeneTree; ENSGT00950000182872; -.
DR HOGENOM; CLU_035361_1_0_1; -.
DR InParanoid; Q9QYG0; -.
DR OMA; KTCFQPL; -.
DR OrthoDB; 854690at2759; -.
DR PhylomeDB; Q9QYG0; -.
DR TreeFam; TF313168; -.
DR BioGRID-ORCS; 29811; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ndrg2; mouse.
DR EvolutionaryTrace; Q9QYG0; -.
DR PRO; PR:Q9QYG0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9QYG0; protein.
DR Bgee; ENSMUSG00000004558; Expressed in hindlimb stylopod muscle and 307 other tissues.
DR ExpressionAtlas; Q9QYG0; baseline and differential.
DR Genevisible; Q9QYG0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IDA:MGI.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0099173; P:postsynapse organization; ISO:MGI.
DR GO; GO:0090361; P:regulation of platelet-derived growth factor production; IMP:MGI.
DR GO; GO:0010574; P:regulation of vascular endothelial growth factor production; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IDA:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR004142; NDRG.
DR InterPro; IPR030690; NDRG2.
DR PANTHER; PTHR11034; PTHR11034; 1.
DR PANTHER; PTHR11034:SF17; PTHR11034:SF17; 1.
DR Pfam; PF03096; Ndr; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Neurogenesis; Phosphoprotein;
KW Reference proteome; Tumor suppressor; Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT CHAIN 2..371
FT /note="Protein NDRG2"
FT /id="PRO_0000441168"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN36"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 330
FT /note="Phosphothreonine; by SGK1"
FT /evidence="ECO:0000269|PubMed:15461589,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 332
FT /note="Phosphoserine; by PKC/PRKCQ or SGK1"
FT /evidence="ECO:0000269|PubMed:14985363,
FT ECO:0000269|PubMed:15461589, ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 348
FT /note="Phosphothreonine; by PKB/AKT1 or SGK1"
FT /evidence="ECO:0000269|PubMed:14985363,
FT ECO:0000269|PubMed:15461589, ECO:0007744|PubMed:21183079"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15461589,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 26..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019009"
FT CONFLICT 253
FT /note="L -> P (in Ref. 2; BAE39998)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="R -> S (in Ref. 2; BAE39998)"
FT /evidence="ECO:0000305"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:2QMQ"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:2QMQ"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:2QMQ"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2QMQ"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:2QMQ"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2QMQ"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:2QMQ"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2QMQ"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2QMQ"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:2QMQ"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:2QMQ"
SQ SEQUENCE 371 AA; 40789 MW; A5237C04278197B2 CRC64;
MAELQEVQIT EEKPLLPGQT PETAKEAELA ARILLDQGQT HSVETPYGSV TFTVYGTPKP
KRPAIFTYHD VGLNYKSCFQ PLFRFGDMQE IIQNFVRVHV DAPGMEEGAP VFPLGYQYPS
LDQLADMIPC ILQYLNFSTI IGVGVGAGAY ILSRYALNHP DTVEGLVLIN IDPNAKGWMD
WAAHKLTGLT SSIPDMILGH LFSQEELSGN SELIQKYRGI IQHAPNLENI ELYWNSYNNR
RDLNFERGGE TTLKCPVMLV VGDQAPHEDA VVECNSKLDP TQTSFLKMAD SGGQPQLTQP
GKLTEAFKYF LQGMGYMASS CMTRLSRSRT ASLTSAASID GSRSRSRTLS QSSESGTLPS
GPPGHTMEVS C
