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Mitogen-activated protein kinase kinase kinase 13 (EC 2.7.11.25) (Leucine zipper-bearing kinase) (Mixed lineage kinase) (MLK)

 M3K13_HUMAN             Reviewed;         966 AA.
O43283; B2R6U2; B4DLE3; B4DMV2; B4DZJ4; D3DNU1; Q05BY6; Q15450;
Q2NKN3;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 155.
RecName: Full=Mitogen-activated protein kinase kinase kinase 13;
EC=2.7.11.25;
AltName: Full=Leucine zipper-bearing kinase;
AltName: Full=Mixed lineage kinase;
Short=MLK;
Name=MAP3K13 {ECO:0000312|HGNC:HGNC:6852};
Synonyms=LZK {ECO:0000312|EMBL:BAA24817.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:BAA24817.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
AUTOPHOSPHORYLATION.
TISSUE=Cerebellum {ECO:0000269|PubMed:9353328};
PubMed=9353328; DOI=10.1074/jbc.272.45.28622;
Sakuma H., Ikeda A., Oka S., Kozutsumi Y., Zanetta J., Kawasaki T.;
"Molecular cloning and functional expression of a cDNA encoding a new
member of mixed lineage protein kinase from human brain.";
J. Biol. Chem. 272:28622-28629(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=Brain, Testis, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 230-340 (ISOFORM 1).
PubMed=8274451;
Schultz S.J., Nigg E.A.;
"Identification of 21 novel human protein kinases, including 3 members
of a family related to the cell cycle regulator nimA of Aspergillus
nidulans.";
Cell Growth Differ. 4:821-830(1993).
[7] {ECO:0000305}
HOMODIMERIZATION.
PubMed=11163770; DOI=10.1016/S0014-5793(00)02432-7;
Ikeda A., Masaki M., Kozutsumi Y., Oka S., Kawasaki T.;
"Identification and characterization of functional domains in a mixed
lineage kinase LZK.";
FEBS Lett. 488:190-195(2001).
[8] {ECO:0000305}
FUNCTION, AND INTERACTION WITH MAPK8IP1.
PubMed=11726277; DOI=10.1093/oxfordjournals.jbchem.a003048;
Ikeda A., Hasegawa K., Masaki M., Moriguchi T., Nishida E.,
Kozutsumi Y., Oka S., Kawasaki T.;
"Mixed lineage kinase LZK forms a functional signaling complex with
JIP-1, a scaffold protein of the c-Jun NH(2)-terminal kinase
pathway.";
J. Biochem. 130:773-781(2001).
[9] {ECO:0000305}
FUNCTION, INTERACTION WITH PRDX3, AND MUTAGENESIS OF LYS-195.
PubMed=12492477; DOI=10.1046/j.1432-1033.2003.03363.x;
Masaki M., Ikeda A., Shiraki E., Oka S., Kawasaki T.;
"Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB
synergistically.";
Eur. J. Biochem. 270:76-83(2003).
[10]
VARIANTS [LARGE SCALE ANALYSIS] GLY-517; LYS-712 AND LEU-746.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Activates the JUN N-terminal pathway through activation
of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3
to regulate the activation of NF-kappa-B in the cytosol. This
activation is kinase-dependent and involves activating the IKK
complex, the IKBKB-containing complex that phosphorylates
inhibitors of NF-kappa-B. {ECO:0000269|PubMed:11726277,
ECO:0000269|PubMed:12492477, ECO:0000269|PubMed:9353328}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:9353328}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q60700};
-!- ACTIVITY REGULATION: Activated by autophosphorylation and
homodimerization. {ECO:0000269|PubMed:11163770,
ECO:0000269|PubMed:9353328}.
-!- SUBUNIT: Homodimer; forms dimers through the leucine-zipper motif.
Interacts with the C-terminus of MAPK8IP1 through the kinase
catalytic domain. Binds PRDX3. Associates with the IKK complex
through the kinase domain. {ECO:0000269|PubMed:11163770,
ECO:0000269|PubMed:11726277, ECO:0000269|PubMed:12492477}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1168480, EBI-1168480;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9353328}.
Membrane {ECO:0000269|PubMed:9353328}; Peripheral membrane protein
{ECO:0000269|PubMed:9353328}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=O43283-1; Sequence=Displayed;
Name=2;
IsoId=O43283-3; Sequence=VSP_036567, VSP_036568;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay. No
experimental confirmation available.;
Name=3;
IsoId=O43283-4; Sequence=VSP_036563, VSP_036566;
Name=4;
IsoId=O43283-5; Sequence=VSP_036562, VSP_036569;
Name=5;
IsoId=O43283-6; Sequence=VSP_036564, VSP_036565;
-!- TISSUE SPECIFICITY: Expressed in the adult brain, liver, placenta
and pancreas, with expression strongest in the pancreas.
{ECO:0000269|PubMed:9353328}.
-!- PTM: Autophosphorylated on serine and threonine residues.
{ECO:0000269|PubMed:9353328}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI11727.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
Sequence=BAG59505.1; Type=Erroneous termination; Positions=740; Note=Translated as Tyr.; Evidence={ECO:0000305};
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EMBL; AB001872; BAA24817.1; -; mRNA.
EMBL; AK296961; BAG59505.1; ALT_SEQ; mRNA.
EMBL; AK297646; BAG60014.1; -; mRNA.
EMBL; AK302951; BAG64106.1; -; mRNA.
EMBL; AK312714; BAG35589.1; -; mRNA.
EMBL; AC099661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC128680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC132516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78224.1; -; Genomic_DNA.
EMBL; CH471052; EAW78225.1; -; Genomic_DNA.
EMBL; BC031677; AAH31677.1; -; mRNA.
EMBL; BC111726; AAI11727.1; ALT_SEQ; mRNA.
EMBL; Z25428; CAA80915.1; -; mRNA.
CCDS; CCDS3270.1; -. [O43283-1]
CCDS; CCDS56298.1; -. [O43283-5]
PIR; I38218; I38218.
RefSeq; NP_001229243.1; NM_001242314.1. [O43283-1]
RefSeq; NP_001229246.1; NM_001242317.1. [O43283-5]
RefSeq; NP_004712.1; NM_004721.4. [O43283-1]
RefSeq; XP_011511612.1; XM_011513310.2. [O43283-1]
RefSeq; XP_016862945.1; XM_017007456.1. [O43283-1]
UniGene; Hs.591306; -.
UniGene; Hs.634586; -.
ProteinModelPortal; O43283; -.
SMR; O43283; -.
BioGrid; 114614; 12.
IntAct; O43283; 3.
STRING; 9606.ENSP00000265026; -.
BindingDB; O43283; -.
ChEMBL; CHEMBL1163124; -.
GuidetoPHARMACOLOGY; 2073; -.
iPTMnet; O43283; -.
PhosphoSitePlus; O43283; -.
BioMuta; MAP3K13; -.
PaxDb; O43283; -.
PeptideAtlas; O43283; -.
PRIDE; O43283; -.
ProteomicsDB; 48852; -.
ProteomicsDB; 48853; -. [O43283-3]
ProteomicsDB; 48854; -. [O43283-4]
ProteomicsDB; 48855; -. [O43283-5]
ProteomicsDB; 48856; -. [O43283-6]
Ensembl; ENST00000265026; ENSP00000265026; ENSG00000073803. [O43283-1]
Ensembl; ENST00000424227; ENSP00000399910; ENSG00000073803. [O43283-1]
Ensembl; ENST00000433092; ENSP00000389798; ENSG00000073803. [O43283-6]
Ensembl; ENST00000438053; ENSP00000403561; ENSG00000073803. [O43283-3]
Ensembl; ENST00000443863; ENSP00000409325; ENSG00000073803. [O43283-4]
Ensembl; ENST00000446828; ENSP00000411483; ENSG00000073803. [O43283-5]
GeneID; 9175; -.
KEGG; hsa:9175; -.
UCSC; uc003fph.5; human. [O43283-1]
CTD; 9175; -.
DisGeNET; 9175; -.
EuPathDB; HostDB:ENSG00000073803.13; -.
GeneCards; MAP3K13; -.
HGNC; HGNC:6852; MAP3K13.
HPA; HPA016497; -.
HPA; HPA036691; -.
HPA; HPA036692; -.
MIM; 604915; gene.
neXtProt; NX_O43283; -.
OpenTargets; ENSG00000073803; -.
PharmGKB; PA30596; -.
eggNOG; KOG4721; Eukaryota.
eggNOG; ENOG410YKX2; LUCA.
GeneTree; ENSGT00900000140790; -.
HOVERGEN; HBG052383; -.
InParanoid; O43283; -.
KO; K04422; -.
OMA; ENPMQFE; -.
OrthoDB; EOG091G0905; -.
PhylomeDB; O43283; -.
TreeFam; TF105119; -.
SignaLink; O43283; -.
SIGNOR; O43283; -.
ChiTaRS; MAP3K13; human.
GeneWiki; MAP3K13; -.
GenomeRNAi; 9175; -.
PRO; PR:O43283; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000073803; Expressed in 225 organ(s), highest expression level in corpus epididymis.
CleanEx; HS_MAP3K13; -.
ExpressionAtlas; O43283; baseline and differential.
Genevisible; O43283; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0000186; P:activation of MAPKK activity; IDA:UniProtKB.
GO; GO:0007254; P:JNK cascade; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017419; MAP3K12_MAP3K13.
InterPro; IPR027258; MAPKKK13.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
PIRSF; PIRSF500742; MAPKKK13; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 966 Mitogen-activated protein kinase kinase
kinase 13.
/FTId=PRO_0000086264.
DOMAIN 168 409 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 174 182 ATP. {ECO:0000250|UniProtKB:Q12852,
ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 433 454 Leucine-zipper 1.
REGION 486 507 Leucine-zipper 2.
REGION 815 828 Acidic. {ECO:0000305}.
ACT_SITE 279 279 Proton acceptor.
{ECO:0000250|UniProtKB:Q12852,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 195 195 ATP. {ECO:0000250|UniProtKB:Q60700,
ECO:0000255|PROSITE-ProRule:PRU00159}.
VAR_SEQ 1 207 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036562.
VAR_SEQ 1 144 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036563.
VAR_SEQ 122 128 RSGSGSG -> RYLGSAI (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036564.
VAR_SEQ 129 966 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036565.
VAR_SEQ 145 159 IGKAYSTDYKLQQQD -> MSYVECKCLQLENKN (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036566.
VAR_SEQ 159 160 DT -> VF (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036567.
VAR_SEQ 161 966 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036568.
VAR_SEQ 208 220 LRKLKHPNIIAFK -> MYCGIQILALWER (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036569.
VARIANT 44 44 E -> K (in dbSNP:rs35266179).
/FTId=VAR_051640.
VARIANT 517 517 R -> G (in dbSNP:rs56408536).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040708.
VARIANT 712 712 E -> K (in dbSNP:rs56309231).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040709.
VARIANT 746 746 P -> L (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040710.
VARIANT 915 915 R -> H (in dbSNP:rs3732576).
/FTId=VAR_030577.
MUTAGEN 195 195 K->A: Kinase inactive. Fails to activate
NF-kappa-B.
{ECO:0000269|PubMed:12492477}.
CONFLICT 106 106 D -> G (in Ref. 2; BAG59505).
{ECO:0000305}.
CONFLICT 230 232 CII -> YLY (in Ref. 6; CAA80915).
{ECO:0000305}.
CONFLICT 268 268 N -> D (in Ref. 2; BAG59505).
{ECO:0000305}.
CONFLICT 339 340 FG -> MV (in Ref. 6; CAA80915).
{ECO:0000305}.
CONFLICT 508 508 E -> G (in Ref. 2; BAG64106).
{ECO:0000305}.
CONFLICT 821 821 G -> R (in Ref. 2; BAG60014).
{ECO:0000305}.
SEQUENCE 966 AA; 108296 MW; 9687F38C8AB20AB1 CRC64;
MANFQEHLSC SSSPHLPFSE SKTFNGLQDE LTAMGNHPSP KLLEDQQEKG MVRTELIESV
HSPVTTTVLT SVSEDSRDQF ENSVLQLREH DESETAVSQG NSNTVDGEST SGTEDIKIQF
SRSGSGSGGF LEGLFGCLRP VWNIIGKAYS TDYKLQQQDT WEVPFEEISE LQWLGSGAQG
AVFLGKFRAE EVAIKKVREQ NETDIKHLRK LKHPNIIAFK GVCTQAPCYC IIMEYCAHGQ
LYEVLRAGRK ITPRLLVDWS TGIASGMNYL HLHKIIHRDL KSPNVLVTHT DAVKISDFGT
SKELSDKSTK MSFAGTVAWM APEVIRNEPV SEKVDIWSFG VVLWELLTGE IPYKDVDSSA
IIWGVGSNSL HLPVPSTCPD GFKILMKQTW QSKPRNRPSF RQTLMHLDIA SADVLATPQE
TYFKSQAEWR EEVKKHFEKI KSEGTCIHRL DEELIRRRRE ELRHALDIRE HYERKLERAN
NLYMELSAIM LQLEMREKEL IKREQAVEKK YPGTYKRHPV RPIIHPNAME KLMKRKGVPH
KSGMQTKRPD LLRSEGIPTT EVAPTASPLS GSPKMSTSSS KSRYRSKPRH RRGNSRGSHS
DFAAILKNQP AQENSPHPTY LHQAQSQYPS LHHHNSLQQQ YQQPPPAMSQ SHHPRLNMHG
QDIATCANNL RYFGPAAALR SPLSNHAQRQ LPGSSPDLIS TAMAADCWRS SEPDKGQAGP
WGCCQADAYD PCLQCRPEQY GSLDIPSAEP VGRSPDLSKS PAHNPLLENA QSSEKTEENE
FSGCRSESSL GTSHLGTPPA LPRKTRPLQK SGDDSSEEEE GEVDSEVEFP RRQRPHRCIS
SCQSYSTFSS ENFSVSDGEE GNTSDHSNSP DELADKLEDR LAEKLDDLLS QTPEIPIDIS
SHSDGLSDKE CAVRRVKTQM SLGKLCVEER GYENPMQFEE SDCDSSDGEC SDATVRTNKH
YSSATW


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