P4R3B_HUMAN
ID P4R3B_HUMAN Reviewed; 849 AA.
AC Q5MIZ7; Q6P9B0; Q86XB8; Q9BQJ0; Q9BRK2; Q9H913; Q9P2G0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 3B;
DE AltName: Full=SMEK homolog 2;
GN Name=PPP4R3B {ECO:0000312|HGNC:HGNC:29267};
GN Synonyms=KIAA1387, PP4R3B, SMEK2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT VAL-503.
RX PubMed=15616564; DOI=10.1038/nature03159;
RA Kittler R., Putz G., Pelletier L., Poser I., Heninger A.-K., Drechsel D.,
RA Fischer S., Konstantinova I., Habermann B., Grabner H., Yaspo M.-L.,
RA Himmelbauer H., Korn B., Neugebauer K., Pisabarro M.T., Buchholz F.;
RT "An endoribonuclease-prepared siRNA screen in human cells identifies genes
RT essential for cell division.";
RL Nature 432:1036-1040(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-503, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Brain, and Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 524-849.
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP INTERACTION WITH PPP4C AND PPP4R2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16085932; DOI=10.1074/mcp.m500231-mcp200;
RA Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R., Fields S.,
RA Sonenberg N., Hafen E., Raught B., Aebersold R.;
RT "A novel, evolutionarily conserved protein phosphatase complex involved in
RT cisplatin sensitivity.";
RL Mol. Cell. Proteomics 4:1725-1740(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18487071; DOI=10.1016/j.biocel.2008.03.021;
RA Martin-Granados C., Philp A., Oxenham S.K., Prescott A.R., Cohen P.T.W.;
RT "Depletion of protein phosphatase 4 in human cells reveals essential roles
RT in centrosome maturation, cell migration and the regulation of Rho
RT GTPases.";
RL Int. J. Biochem. Cell Biol. 40:2315-2332(2008).
RN [10]
RP IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3B COMPLEX.
RX PubMed=18614045; DOI=10.1016/j.molcel.2008.05.016;
RA Chowdhury D., Xu X., Zhong X., Ahmed F., Zhong J., Liao J., Dykxhoorn D.M.,
RA Weinstock D.M., Pfeifer G.P., Lieberman J.;
RT "A PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA
RT replication.";
RL Mol. Cell 31:33-46(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-840, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4
CC (PP4). May regulate the activity of PPP4C at centrosomal microtubule
CC organizing centers.
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits. Component of the PP4 complex PPP4C-PPP4R2-PPP4R3B.
CC {ECO:0000269|PubMed:18614045}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18487071}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:18487071}. Nucleus {ECO:0000269|PubMed:18487071}.
CC Note=In interphase localized in the cytoplasm and (with higher levels)
CC the nucleus. During metaphase located in pericentriolar regions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5MIZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5MIZ7-2; Sequence=VSP_021261;
CC Name=3;
CC IsoId=Q5MIZ7-3; Sequence=VSP_021261, VSP_021262;
CC Name=4;
CC IsoId=Q5MIZ7-4; Sequence=VSP_021259, VSP_021260;
CC Name=5;
CC IsoId=Q5MIZ7-5; Sequence=VSP_021258, VSP_021263;
CC -!- TISSUE SPECIFICITY: Moderately expressed in tissues and specific brain
CC regions examined. {ECO:0000269|PubMed:10718198}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SMEK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92625.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY825268; AAV97750.1; -; mRNA.
DR EMBL; AY825269; AAV97751.1; -; mRNA.
DR EMBL; AB037808; BAA92625.1; ALT_INIT; mRNA.
DR EMBL; AK023148; BAB14430.1; -; mRNA.
DR EMBL; AC015982; AAY24270.1; -; Genomic_DNA.
DR EMBL; BC006215; AAH06215.1; -; mRNA.
DR EMBL; BC045714; AAH45714.1; -; mRNA.
DR EMBL; BC060855; AAH60855.1; -; mRNA.
DR EMBL; AL136556; CAB66491.2; -; mRNA.
DR CCDS; CCDS1855.1; -. [Q5MIZ7-3]
DR CCDS; CCDS46289.1; -. [Q5MIZ7-1]
DR CCDS; CCDS62913.1; -. [Q5MIZ7-2]
DR RefSeq; NP_001116436.2; NM_001122964.2. [Q5MIZ7-1]
DR RefSeq; NP_001269779.1; NM_001282850.1. [Q5MIZ7-2]
DR RefSeq; NP_065196.1; NM_020463.3. [Q5MIZ7-3]
DR AlphaFoldDB; Q5MIZ7; -.
DR BioGRID; 121459; 62.
DR ComplexPortal; CPX-1844; PPP4C-PPP4R2-PPP4R3B protein phosphatase 4 complex.
DR IntAct; Q5MIZ7; 25.
DR MINT; Q5MIZ7; -.
DR STRING; 9606.ENSP00000483228; -.
DR ChEMBL; CHEMBL4105714; -.
DR iPTMnet; Q5MIZ7; -.
DR PhosphoSitePlus; Q5MIZ7; -.
DR BioMuta; PPP4R3B; -.
DR DMDM; 334302843; -.
DR EPD; Q5MIZ7; -.
DR jPOST; Q5MIZ7; -.
DR MassIVE; Q5MIZ7; -.
DR MaxQB; Q5MIZ7; -.
DR PaxDb; Q5MIZ7; -.
DR PeptideAtlas; Q5MIZ7; -.
DR PRIDE; Q5MIZ7; -.
DR ProteomicsDB; 63574; -. [Q5MIZ7-1]
DR ProteomicsDB; 63575; -. [Q5MIZ7-2]
DR ProteomicsDB; 63576; -. [Q5MIZ7-3]
DR ProteomicsDB; 63577; -. [Q5MIZ7-4]
DR ProteomicsDB; 63578; -. [Q5MIZ7-5]
DR Antibodypedia; 73190; 164 antibodies from 25 providers.
DR DNASU; 57223; -.
DR Ensembl; ENST00000611717.4; ENSP00000478677.1; ENSG00000275052.5. [Q5MIZ7-3]
DR Ensembl; ENST00000616288.4; ENSP00000484116.1; ENSG00000275052.5. [Q5MIZ7-2]
DR Ensembl; ENST00000616407.2; ENSP00000483228.1; ENSG00000275052.5. [Q5MIZ7-1]
DR GeneID; 57223; -.
DR KEGG; hsa:57223; -.
DR MANE-Select; ENST00000616407.2; ENSP00000483228.1; NM_001122964.3; NP_001116436.3.
DR UCSC; uc032nnw.2; human. [Q5MIZ7-1]
DR CTD; 57223; -.
DR DisGeNET; 57223; -.
DR GeneCards; PPP4R3B; -.
DR HGNC; HGNC:29267; PPP4R3B.
DR HPA; ENSG00000275052; Low tissue specificity.
DR MIM; 610352; gene.
DR neXtProt; NX_Q5MIZ7; -.
DR OpenTargets; ENSG00000275052; -.
DR PharmGKB; PA162403977; -.
DR VEuPathDB; HostDB:ENSG00000275052; -.
DR eggNOG; KOG2175; Eukaryota.
DR GeneTree; ENSGT00390000018199; -.
DR HOGENOM; CLU_004909_3_0_1; -.
DR InParanoid; Q5MIZ7; -.
DR OMA; YHRYMIS; -.
DR OrthoDB; 388216at2759; -.
DR PhylomeDB; Q5MIZ7; -.
DR TreeFam; TF315190; -.
DR PathwayCommons; Q5MIZ7; -.
DR SignaLink; Q5MIZ7; -.
DR BioGRID-ORCS; 57223; 18 hits in 1068 CRISPR screens.
DR ChiTaRS; PPP4R3B; human.
DR GeneWiki; SMEK2; -.
DR GenomeRNAi; 57223; -.
DR Pharos; Q5MIZ7; Tbio.
DR PRO; PR:Q5MIZ7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q5MIZ7; protein.
DR Bgee; ENSG00000275052; Expressed in bronchial epithelial cell and 193 other tissues.
DR Genevisible; Q5MIZ7; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IPI:ComplexPortal.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; IMP:ComplexPortal.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:2000779; P:regulation of double-strand break repair; IMP:ComplexPortal.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006887; DUF625.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF04802; SMK-1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..849
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 3B"
FT /id="PRO_0000254603"
FT DOMAIN 1..100
FT /note="WH1"
FT REGION 714..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..566
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021258"
FT VAR_SEQ 49..55
FT /note="SLLLESK -> KVIGTVE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021259"
FT VAR_SEQ 56..849
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021260"
FT VAR_SEQ 491..522
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15616564"
FT /id="VSP_021261"
FT VAR_SEQ 536..589
FT /note="DNYQTAQLLALILELLTFCVEHHTYHIKNYIMNKDLLRRVLVLMNSKHTFLA
FT LC -> G (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021262"
FT VAR_SEQ 693..699
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021263"
FT VARIANT 293
FT /note="S -> T (in dbSNP:rs34999684)"
FT /id="VAR_057734"
FT VARIANT 503
FT /note="I -> V (in dbSNP:rs2903704)"
FT /evidence="ECO:0000269|PubMed:10718198,
FT ECO:0000269|PubMed:15616564"
FT /id="VAR_065187"
FT CONFLICT 806
FT /note="K -> E (in Ref. 3; BAB14430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 849 AA; 97458 MW; CEA2C74C0F2B3D27 CRC64;
MSDTRRRVKV YTLNEDRQWD DRGTGHVSST YVEELKGMSL LVRAESDGSL LLESKINPNT
AYQKQQDTLI VWSEAENYDL ALSFQEKAGC DEIWEKICQV QGKDPSVEVT QDLIDESEEE
RFEEMPETSH LIDLPTCELN KLEEIADLVT SVLSSPIRRE KLALALENEG YIKKLLQLFQ
ACENLENTEG LHHLYEIIRG ILFLNKATLF EVMFSDECIM DVVGCLEYDP ALAQPKRHRE
FLTKTAKFKE VIPITDSELR QKIHQTYRVQ YIQDIILPTP SVFEENFLST LTSFIFFNKV
EIVSMLQEDE KFLSEVFAQL TDEATDDDKR RELVNFFKEF CAFSQTLQPQ NRDAFFKTLA
KLGILPALEI VMGMDDLQVR SAATDIFSYL VEFSPSMVRE FVMQEAQQSD DDILLINVVI
EQMICDTDPE LGGAVQLMGL LRTLIDPENM LATTNKTEKS EFLNFFYNHC MHVLTAPLLT
NTSEDKCEKD FFLKHYRYSW SFICTPSHSH SHSTPSSSIS QDNIVGSNKN NTICPDNYQT
AQLLALILEL LTFCVEHHTY HIKNYIMNKD LLRRVLVLMN SKHTFLALCA LRFMRRIIGL
KDEFYNRYIT KGNLFEPVIN ALLDNGTRYN LLNSAVIELF EFIRVEDIKS LTAHIVENFY
KALESIEYVQ TFKGLKTKYE QEKDRQNQKL NSVPSILRSN RFRRDAKALE EDEEMWFNED
EEEEGKAVVA PVEKPKPEDD FPDNYEKFME TKKAKESEDK ENLPKRTSPG GFKFTFSHSA
SAANGTNSKS VVAQIPPATS NGSSSKTTNL PTSVTATKGS LVGLVDYPDD EEEDEEEESS
PRKRPRLGS
