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A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc)

 AKP13_RAT               Reviewed;        2760 AA.
F1M3G7; Q8VHU6;
08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
03-APR-2013, sequence version 2.
20-JUN-2018, entry version 64.
RecName: Full=A-kinase anchor protein 13;
Short=AKAP-13;
AltName: Full=AKAP-Lbc {ECO:0000303|PubMed:17537920};
Name=Akap13 {ECO:0000312|RGD:727893};
Synonyms=Rt13 {ECO:0000303|PubMed:11696353};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000312|EMBL:AAL40924.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 1151-1748, AND INTERACTION WITH RHOA AND
PRKAR2A.
STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAL40924.1};
TISSUE=Kidney {ECO:0000312|EMBL:AAL40924.1};
PubMed=11696353; DOI=10.1016/S0014-5793(01)02995-7;
Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V.,
Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.;
"Ht31: the first protein kinase A anchoring protein to integrate
protein kinase A and Rho signaling.";
FEBS Lett. 507:264-268(2001).
[4]
FUNCTION, AND INDUCTION BY PHENYLEPHRINE.
PubMed=17537920; DOI=10.1073/pnas.0701099104;
Appert-Collin A., Cotecchia S., Nenniger-Tosato M., Pedrazzini T.,
Diviani D.;
"The A-kinase anchoring protein (AKAP)-Lbc-signaling complex mediates
alpha1 adrenergic receptor-induced cardiomyocyte hypertrophy.";
Proc. Natl. Acad. Sci. U.S.A. 104:10140-10145(2007).
[5]
FUNCTION.
PubMed=20139090; DOI=10.1074/jbc.M110.106856;
Mayers C.M., Wadell J., McLean K., Venere M., Malik M., Shibata T.,
Driggers P.H., Kino T., Guo X.C., Koide H., Gorivodsky M.,
Grinberg A., Mukhopadhyay M., Abu-Asab M., Westphal H., Segars J.H.;
"The Rho guanine nucleotide exchange factor AKAP13 (BRX) is essential
for cardiac development in mice.";
J. Biol. Chem. 285:12344-12354(2010).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1585; SER-1628;
SER-1630; SER-1891; SER-1894; SER-1907; SER-2292; SER-2511 AND
SER-2676, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[7]
FUNCTION, AND INTERACTION WITH IKBKB.
PubMed=23090968; DOI=10.1128/MCB.00887-12;
del Vescovo C.D., Cotecchia S., Diviani D.;
"A-kinase-anchoring protein-Lbc anchors IkappaB kinase beta to support
interleukin-6-mediated cardiomyocyte hypertrophy.";
Mol. Cell. Biol. 33:14-27(2013).
[8]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH PKN1; MAPK14; ZAK AND
MAP2K3.
PubMed=23716597; DOI=10.1128/MCB.00031-13;
Perez Lopez I., Cariolato L., Maric D., Gillet L., Abriel H.,
Diviani D.;
"A-kinase anchoring protein Lbc coordinates a p38 activating signaling
complex controlling compensatory cardiac hypertrophy.";
Mol. Cell. Biol. 33:2903-2917(2013).
[9]
TISSUE SPECIFICITY.
PubMed=25892096; DOI=10.1002/jbmr.2534;
Koide H., Holmbeck K., Lui J.C., Guo X.C., Driggers P., Chu T.,
Tatsuno I., Quaglieri C., Kino T., Baron J., Young M.F., Robey P.G.,
Segars J.H.;
"Mice deficient in AKAP13 (BRX) are osteoporotic and have impaired
osteogenesis.";
J. Bone Miner. Res. 30:1887-1895(2015).
-!- FUNCTION: Scaffold protein that plays an important role in
assembling signaling complexes downstream of several types of G
protein-coupled receptors. Activates RHOA in response to signaling
via G protein-coupled receptors via its function as Rho guanine
nucleotide exchange factor (PubMed:17537920). May also activate
other Rho family members. Part of a kinase signaling complex that
links ADRA1A and ADRA1B adrenergic receptor signaling to the
activation of downstream p38 MAP kinases, such as MAPK11 and
MAPK14 (PubMed:17537920, PubMed:23716597). Part of a signaling
complex that links ADRA1B signaling to the activation of RHOA and
IKBKB/IKKB, leading to increased NF-kappa-B transcriptional
activity (PubMed:23090968). Part of a RHOA-dependent signaling
cascade that mediates responses to lysophosphatidic acid (LPA), a
signaling molecule that activates G-protein coupled receptors and
potentiates transcriptional activation of the glucocorticoid
receptor NR3C1 (By similarity). Part of a signaling cascade that
stimulates MEF2C-dependent gene expression in response to
lysophosphatidic acid (LPA) (PubMed:20139090). Part of a signaling
pathway that activates MAPK11 and/or MAPK14 and leads to increased
transcription activation of the estrogen receptors ESR1 and ESR2
(By similarity). Part of a signaling cascade that links cAMP and
EGFR signaling to BRAF signaling and to PKA-mediated
phosphorylation of KSR1, leading to the activation of downstream
MAP kinases, such as MAPK1 or MAPK3 (By similarity). Functions as
scaffold protein that anchors cAMP-dependent protein kinase (PKA)
and PRKD1. This promotes activation of PRKD1, leading to increased
phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy
(By similarity). Has no guanine nucleotide exchange activity on
CDC42, Ras or Rac (By similarity). Required for normal embryonic
heart development, and in particular for normal sarcomere
formation in the developing cardiomyocytes (By similarity). Plays
a role in cardiomyocyte growth and cardiac hypertrophy in response
to activation of the beta-adrenergic receptor by phenylephrine or
isoproterenol (PubMed:17537920). Required for normal adaptive
cardiac hypertrophy in response to pressure overload (By
similarity). Plays a role in osteogenesis (By similarity).
{ECO:0000250|UniProtKB:E9Q394, ECO:0000250|UniProtKB:Q12802,
ECO:0000269|PubMed:17537920, ECO:0000269|PubMed:20139090,
ECO:0000269|PubMed:23090968}.
-!- SUBUNIT: Interacts with the cAMP-dependent protein kinase (PKA)
holoenzyme and with the regulatory subunit PRKAR2A
(PubMed:11696353). Interacts with RHOA (PubMed:11696353).
Interacts also with RHOB and RHOC. Identified in a ternary complex
with RHOA and PRKAR2A. Identified in a complex with NR3C1 and
RHOA. Interacts with BRAF and KSR1. Identified in a complex with
BRAF and KSR1 (By similarity). Component of a signaling complex
containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3
(PubMed:23716597). Within this complex, AKAP13 interacts directly
with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By
similarity). Interacts (phosphorylated form) with YWHAB and YWHAZ.
Interaction with YWHAB inhibits activation of RHOA, interferes
with PKN1 binding and activation of MAP kinases. Interacts with
GNA12. Interacts with IKBKB (PubMed:23090968). Interacts with
ESR1, THRA, PPARA and NME2 (By similarity). Interacts (via the C-
terminal domain after the PH domain) with MEF2C and RXRB.
Interacts (via the C-terminal domain after the PH domain) with
PRKD1 (By similarity). {ECO:0000250|UniProtKB:E9Q394,
ECO:0000250|UniProtKB:Q12802, ECO:0000269|PubMed:11696353,
ECO:0000269|PubMed:23090968, ECO:0000269|PubMed:23716597}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q12802}. Cytoplasm
{ECO:0000250|UniProtKB:Q12802}. Cytoplasm, cell cortex
{ECO:0000250|UniProtKB:Q12802}. Nucleus
{ECO:0000250|UniProtKB:Q12802}. Membrane
{ECO:0000250|UniProtKB:Q12802}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q12802}. Note=Colocalizes with the actin
cytoskeleton at the cell cortex. {ECO:0000250|UniProtKB:Q12802}.
-!- TISSUE SPECIFICITY: Detected in bone osteoblasts (at protein
level). {ECO:0000269|PubMed:25892096}.
-!- INDUCTION: Up-regulated in cardiomyocytes in response to
phenylephrine (in vitro). {ECO:0000269|PubMed:17537920}.
-!- DOMAIN: The DH domain is sufficient for interaction with RHOA, and
for guanine nucleotide exchange (GEF) activity with RHOA. Forms
that lack C-terminal regulatory domains have transforming activity
and function as oncogenes. {ECO:0000250|UniProtKB:Q12802}.
-!- DOMAIN: The PH domain does not play a role in lipid-binding.
Instead, it inhibits the guanine nucleotide exchange (GEF)
activity of the isolated DH domain (in vitro).
{ECO:0000250|UniProtKB:Q12802}.
-!- DOMAIN: The C-terminal domain after the PH domain is involved in
protein-protein interactions that are required for normal,
compensatory cardiac hypertrophy in response to pressure overload.
{ECO:0000250|UniProtKB:E9Q394}.
-!- SEQUENCE CAUTION:
Sequence=AAL40924.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AABR07004317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07004318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR07004319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473980; EDM08537.1; -; Genomic_DNA.
EMBL; AF387102; AAL40924.1; ALT_INIT; mRNA.
RefSeq; NP_001099741.2; NM_001106271.2.
UniGene; Rn.2027; -.
SMR; F1M3G7; -.
STRING; 10116.ENSRNOP00000014802; -.
iPTMnet; F1M3G7; -.
PhosphoSitePlus; F1M3G7; -.
PaxDb; F1M3G7; -.
PeptideAtlas; F1M3G7; -.
PRIDE; F1M3G7; -.
Ensembl; ENSRNOT00000014802; ENSRNOP00000014802; ENSRNOG00000010964.
GeneID; 293024; -.
KEGG; rno:293024; -.
UCSC; RGD:727893; rat.
CTD; 11214; -.
RGD; 727893; Akap13.
eggNOG; ENOG410IR0Y; Eukaryota.
eggNOG; ENOG410XT68; LUCA.
GeneTree; ENSGT00760000119193; -.
KO; K16529; -.
OMA; QQLMKTN; -.
OrthoDB; EOG091G00G7; -.
TreeFam; TF325887; -.
Reactome; R-RNO-193648; NRAGE signals death through JNK.
Reactome; R-RNO-194840; Rho GTPase cycle.
Reactome; R-RNO-416482; G alpha (12/13) signalling events.
PRO; PR:F1M3G7; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000010964; -.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:InterPro.
GO; GO:0005078; F:MAP-kinase scaffold activity; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051018; F:protein kinase A binding; IMP:RGD.
GO; GO:0032947; F:protein-containing complex scaffold activity; IMP:RGD.
GO; GO:0017048; F:Rho GTPase binding; IPI:RGD.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0086023; P:adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; ISS:UniProtKB.
GO; GO:0071875; P:adrenergic receptor signaling pathway; IMP:UniProtKB.
GO; GO:0060348; P:bone development; ISS:UniProtKB.
GO; GO:0055007; P:cardiac muscle cell differentiation; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0051168; P:nuclear export; IMP:RGD.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
GO; GO:0008104; P:protein localization; TAS:RGD.
GO; GO:0010611; P:regulation of cardiac muscle hypertrophy; IMP:RGD.
GO; GO:1900169; P:regulation of glucocorticoid mediated signaling pathway; IEA:Ensembl.
GO; GO:0045859; P:regulation of protein kinase activity; IMP:RGD.
GO; GO:0060297; P:regulation of sarcomere organization; ISS:UniProtKB.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR028852; AKAP13.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR13944:SF18; PTHR13944:SF18; 1.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00109; C1; 1.
SMART; SM00233; PH; 1.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Cytoplasm;
Guanine-nucleotide releasing factor; Membrane; Metal-binding;
Methylation; Nucleus; Phosphoprotein; Reference proteome; Zinc;
Zinc-finger.
CHAIN 1 2760 A-kinase anchor protein 13.
/FTId=PRO_0000436320.
DOMAIN 1956 2153 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 2176 2280 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 1753 1800 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 482 504 Important for interaction with PRKAR2A.
{ECO:0000250|UniProtKB:Q12802}.
REGION 1213 1228 Important for interaction with PRKAR2A.
{ECO:0000269|PubMed:11696353}.
REGION 1546 1695 Important for interaction with MAP2K3.
{ECO:0000250|UniProtKB:Q12802}.
REGION 1881 2760 Interaction with ESR1.
{ECO:0000250|UniProtKB:Q12802}.
COILED 2292 2329 {ECO:0000255}.
COILED 2516 2632 {ECO:0000255}.
COMPBIAS 1432 1435 Poly-Ser. {ECO:0000255}.
COMPBIAS 1493 1498 Poly-Glu. {ECO:0000255}.
COMPBIAS 2725 2737 Poly-Lys. {ECO:0000255}.
MOD_RES 776 776 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 801 801 Phosphothreonine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 932 932 Phosphothreonine.
{ECO:0000250|UniProtKB:E9Q394}.
MOD_RES 962 962 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1450 1450 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1468 1468 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1501 1501 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1526 1526 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1585 1585 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1625 1625 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1628 1628 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1630 1630 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1654 1654 N6-methyllysine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1838 1838 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1857 1857 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1891 1891 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1892 1892 Phosphothreonine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 1894 1894 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1907 1907 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2292 2292 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2345 2345 Phosphoserine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 2415 2415 Phosphothreonine.
{ECO:0000250|UniProtKB:Q12802}.
MOD_RES 2511 2511 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2514 2514 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q394}.
MOD_RES 2676 2676 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 1348 1348 V -> A (in Ref. 3; AAL40924).
{ECO:0000305}.
CONFLICT 1542 1559 Missing (in Ref. 3; AAL40924).
{ECO:0000305}.
CONFLICT 1745 1747 EKD -> KKK (in Ref. 3; AAL40924).
{ECO:0000305}.
SEQUENCE 2760 AA; 301403 MW; DC1C4A92AF76188C CRC64;
MKLSPQQAPL YGDCVVTVLL AEEDKVEDDA IFYLIFSGST LYHCTSTRKV SSDTLETIAP
GHDCCETVKV LLCASKEGLP VFVVAEEDFH FVQDEAYDAA QFLATSAGNQ QALNFTRFLD
RSGPPSGDVN SLDEKVALAF RHLKLPAEWN VLGTDHTLHD GGPRETLMHF AVRLGLLRLT
WFLLQKPGGR GALSIHNKEG ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG
DYSVRHHREL DIYTLTSESE SHCEPHGDSC TGHISKLMNI QQQLMKTNLK QMDNLMPLMV
TTQDSSCVPC VPEPSDHQQL PFEETKSTVC CQGSPGRKDA SPCDLSSVVE EENLICSHKK
NKDTGRPGEG VEPASAVDSR SASHQDSCLQ SIPDCGVKGR EGLPSCGNRN EVTGTQYSGV
ATCQQPLSSE SSVPQDVLVT EPDARQHSSG RELPDSSSTD AGAPEKAGEL EHSLLTPDAT
TQNSKPQVGE SAKERLENSD ISSAEATAVQ ALREPKQKAD VTNHVFAARA AGADAPAEAS
PAWSPEEIPT GKPGMETQER GCEGGITSDQ SSQVLPAAAA ATENKVLDGL ELETLPACPC
ETASSLDLTV SGPRPDGMPK QNSESSAQHA QSLNSQAPLC SIAGAGTPSA ESACPQSTET
SSGGSVIEHG SGEASLPEST AAQPEPQGLC TAPCPEDPQA DTVTSDTAAH NQKSVGSCHL
CALDAKNQEK DLRQDTPSVN TLEDVPHLPS VVPQSEEKLE PDQVSPRGSS FSLASSPESE
SVTKDDVLSL VSSQKEKGTA TPQLHRAPAC SDGPDGRDLN DTDKVGDGAA SPPTPSAVEL
QTSMGNTSPV GVGEQEGSSL TATLEVLSDS LLQSVDKAAL VSDSLLPEEG GSIVVPESST
ALGQGGKDKA TKCPSVKEDV HSSEMSREDQ RTPPPGQEIS RLCEKPMSAL CAGEKALQHS
NSPDTPSACL QTETKHNKEV APQSSPLMKG GAVQNLVPPK TSLSADSEQK TSSTEQSGSS
LLPGGASEAL RCSQPSLSVS VESIQFQGKT SACKVSRNAM EDVTVADAFL ATAEPTKEDA
LHHVKDISDL LNQEKKTTPG LPEALLDKGV TDLQEVITPE IEPLDCKREK LEGTDLSCPT
SKSKETPNNE ETTQPPARDL PTETGLSAIN DNGPQADMKH VTQASVPGEE SNVTTVLGMV
STQAADGPPG ADSIEETATR IVEAVIKQIK ASNTLRTQVE IQNPPLSSSE IKEIENTGSE
SARVFLPGEP LQMENTQKET TGHCSVETEA PEKIILAVHR PEPAPEMPDT KTGGEVDLLS
KRSAASEEEA IGNGAATPKM KQAPGTQVIN RESWCAIEPC PEAASLLASK QSSECRSFID
VGLGTECATK EGVLQRESGS DSDLFHSPSD EMDSIIFSKP EEEQLLCDTT GSSSSTDDTA
SLDRHSSHGS DVSLPQTSKL NRSRNHQSSN GFFSHGVDPE SREGESEPAG SGEMEEEEMD
SITEVPANRS FLRNSMRSLS PFRRHSWGPG KNAASDAEMN QRSSMQVLGH VVRRPPIHRR
SMSWCPSGVQ YSAALNADFN IRSFSLEGLT GGGGVGNKPS SSLEISSANS SELRNPFSGE
EQRSSLMSLS EEHLEPDQRQ HHRMFDQQTC YRSKQQGFNY CTSAISSPLT KSISLMTISH
PGLDNSRPFH SASANLTESI TEENCNFLPP SPSKKSFEEK SGTKVSRTFS YIRNKMSSSK
KSKKEKDKKT LNGHTFSPIP IVGPINCSQC MKPFTNKDAY TCASCGAFVH KGCRENLASC
AKVKMKQPKG SLQAHDTSSL PTVIMRNKSS QPKERPRSAV LLAEEAIAAP MFTNRRSQQS
VSLSKSVSIQ NITGVGNDEN MSNTWKFLSH STDSLNKICK VNESTESLTD EGVGTDMNEG
QLMGDFESDS KQLEAESWSR TVDSKFLKQQ KKDVVKRQEV IYELMQTELH HIRTLKIMSD
VYSRGMMTDL LFEQQMVEKL FPCLDELISI HSQFFQRILE RKKESLVDKS EKNFLIKRIG
DVLVSQFSGE NAERLKKTYG KFCGQHNQSV NYFKDLYTKD KRFQAFVKKK MSSSVVRRLG
IPECILLVTQ RITKYPVLFQ RILQCTKDNE VEQEDLTQSL SLVKDVIGAV DSKVASYEKK
VRLGEIYTKT DSKSIMRMKS GQMFAKEDLR RKKLVRDGSV FLKSATGRLK EKDQKYVFAS
LDHKSTVISL KKLIVREVAH EEKGLFLISM GVKDPEMVEV HASSREERNS WIQIIQDTIN
SLNRDEDEGI PSENEEEKRL LDTKARELKE QLQQKDQQIL LLLEEKEMIF RDMTECSTPL
PEDCSPTHSP RMLFRSNTEE ALKGGPLMKS AISEVEILQG LVSGSLGGTL GQPISSPVEQ
EVMAGPISLP RRAETFGGFD CHQLNASKGG EKEEGDDGQD LRRTESDSGL KKGGNANLVF
MLKRNSEQVV QSIVHLHELL TMLQGVVLQQ DSYIEDQKLV LTEKVLTRSA SRPSSLIEQE
KQRSLEKQRQ DLANLQKQQA QHLEEKRRRE REWEARELEL RDREAKLAER EETVRRRQQD
LERDREELQQ KKGTYQCDLE RLRAAQKQLE REQEQLKRDA EQLSQRQMEQ DLCQVSNKHG
RLMRVPSFLP NSDEFSLLST PSITKSGSLD SELSVSPKRN SISRTQKDKG PFHILSSASQ
TKVPEGQSQA PSSTSTSTRL FGLSKPKEKK EKKKKSKGSR TQPGDGPAPE VPAEGEEIFC


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