PKN2_RAT
ID PKN2_RAT Reviewed; 985 AA.
AC O08874;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Serine/threonine-protein kinase N2;
DE EC=2.7.11.13;
DE AltName: Full=Cardiolipin-activated protein kinase Pak2;
DE AltName: Full=PKN gamma;
DE AltName: Full=Protease-activated kinase 2;
DE Short=PAK-2;
DE AltName: Full=Protein kinase C-like 2;
DE AltName: Full=Protein-kinase C-related kinase 2;
DE AltName: Full=p140 kinase;
GN Name=Pkn2; Synonyms=Pak2, Prk2, Prkcl2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-979, PARTIAL PROTEIN SEQUENCE, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver, and Myeloma;
RX PubMed=9092545; DOI=10.1074/jbc.272.15.9683;
RA Yu W., Liu J., Morrice N.A., Wettenhall R.E.H.;
RT "Isolation and characterization of a structural homologue of human PRK2
RT from rat liver: distinguishing substrate and lipid activator
RT specificities.";
RL J. Biol. Chem. 272:10030-10034(1997).
RN [3]
RP PROTEIN SEQUENCE OF 34-44 AND 255-266, AUTOPHOSPHORYLATION,
RP PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=9121475; DOI=10.1128/mcb.17.4.2247;
RA Vincent S., Settleman J.;
RT "The PRK2 kinase is a potential effector target of both Rho and Rac GTPases
RT and regulates actin cytoskeletal organization.";
RL Mol. Cell. Biol. 17:2247-2256(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584 AND THR-959, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: PKC-related serine/threonine-protein kinase and Rho/Rac
CC effector protein that participates in specific signal transduction
CC responses in the cell. Plays a role in the regulation of cell cycle
CC progression, actin cytoskeleton assembly, cell migration, cell
CC adhesion, tumor cell invasion and transcription activation signaling
CC processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and
CC hence decreases CTTN ability to associate with filamentous actin.
CC Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct
CC RhoA target required for the regulation of the maturation of primordial
CC junctions into apical junction formation in bronchial epithelial cells.
CC Required for G2/M phases of the cell cycle progression and abscission
CC during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase
CC activity that is required for establishment of skin cell-cell adhesion
CC during keratinocytes differentiation. Regulates epithelial bladder
CC cells speed and direction of movement during cell migration and tumor
CC cell invasion. Inhibits Akt pro-survival-induced kinase activity.
CC Mediates Rho protein-induced transcriptional activation via the c-fos
CC serum response factor (SRF). Involved in the negative regulation of
CC ciliogenesis. {ECO:0000250|UniProtKB:Q16513}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13;
CC -!- ACTIVITY REGULATION: Kinase activity is activated upon binding to GTP-
CC bound Rho1/Rac1 GTPases. Activated by caspase-3 (CASP3) cleavage during
CC apoptosis. Activated by lipids, particularly cardiolipin and to a
CC lesser extent by other acidic phospholipids and unsaturated fatty
CC acids. Two specific sites, Thr-817 (activation loop of the kinase
CC domain) and Thr-959 (turn motif), need to be phosphorylated for its
CC full activation (By similarity). {ECO:0000250|UniProtKB:Q16513}.
CC -!- SUBUNIT: Interacts (via the REM repeats) with RHOA (GTP-bound form
CC preferentially) and interacts (via the REM repeats) with RAC1 (GTP-
CC bound form preferentially); the interactions induce its
CC autophosphorylation (By similarity). Interacts with RHOC (By
CC similarity). Interacts with NCK1 (via SH3 domains) and NCK2 (By
CC similarity). Interacts with CD44 (By similarity). Interacts (via C-
CC terminal kinase domain) with PDPK1; the interaction stimulates PDPK1
CC kinase activity (By similarity). Interacts with MAP3K2; the interaction
CC activates PRK2 kinase activity in a MAP3K2-independent kinase activity
CC (By similarity). Interacts (via C-terminal domain) with AKT1; the
CC interaction occurs with the C-terminal cleavage product of PRK2 in
CC apoptotic cells (By similarity). Interacts (via C-terminus) with PTPN13
CC (via PDZ 3 domain) (By similarity). Interacts with CDK10 (By
CC similarity). {ECO:0000250|UniProtKB:Q16513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16513}. Nucleus
CC {ECO:0000250|UniProtKB:Q16513}. Membrane
CC {ECO:0000250|UniProtKB:Q8BWW9}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q16513}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q16513}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q16513}. Midbody {ECO:0000250|UniProtKB:Q16513}.
CC Cell junction {ECO:0000250|UniProtKB:Q16513}. Note=Colocalizes with
CC PTPN13 in lamellipodia-like structures, regions of large actin
CC turnover. Accumulates during telophase at the cleavage furrow and
CC concentrates finally around the midbody in cytokinesis. Recruited to
CC nascent cell-cell contacts at the apical surface of cells.
CC {ECO:0000250|UniProtKB:Q16513}.
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
CC {ECO:0000269|PubMed:9092545, ECO:0000269|PubMed:9121475}.
CC -!- DOMAIN: The N-terminal regioninterferes with the interaction between
CC AKT1 and the C-terminal regionof PKN2. {ECO:0000250}.
CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC -!- DOMAIN: The apoptotic C-terminal cleavage product inhibits EGF-induced
CC kinase activity of AKT1 phosphorylation at 'Thr-308' and 'Ser-473'
CC sites, PDPK1 autophosphorylation and kinases PRKCD and PRKCZ
CC phosphorylations. {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis (By similarity). Autophosphorylated.
CC Phosphorylated. Binding to Rho and Rac promotes autophosphorylation and
CC phosphorylation on serine and threonine residues. Phosphorylated by
CC CDK10 (By similarity). {ECO:0000250|UniProtKB:Q16513,
CC ECO:0000269|PubMed:9121475}.
CC -!- PTM: Proteolytically cleaved by caspase-3 during the induction of
CC apoptotic cell death (By similarity). Activated by limited proteolysis
CC with trypsin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; AABR03012350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03012657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U75358; AAB53364.1; -; mRNA.
DR AlphaFoldDB; O08874; -.
DR SMR; O08874; -.
DR IntAct; O08874; 2.
DR MINT; O08874; -.
DR STRING; 10116.ENSRNOP00000034133; -.
DR iPTMnet; O08874; -.
DR PhosphoSitePlus; O08874; -.
DR jPOST; O08874; -.
DR PaxDb; O08874; -.
DR PRIDE; O08874; -.
DR UCSC; RGD:620146; rat.
DR RGD; 620146; Pkn2.
DR eggNOG; KOG0694; Eukaryota.
DR InParanoid; O08874; -.
DR PhylomeDB; O08874; -.
DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:O08874; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043296; C:apical junction complex; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0043297; P:apical junction assembly; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11622; HR1_PKN_1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037784; C2_PKN.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00742; Hr1; 3.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 3.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; ATP-binding; Cell adhesion; Cell cycle;
KW Cell division; Cell junction; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..985
FT /note="Serine/threonine-protein kinase N2"
FT /id="PRO_0000055724"
FT DOMAIN 33..109
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 121..204
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 207..286
FT /note="REM-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 354..474
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 658..917
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 918..985
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 111..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..464
FT /note="Necessary to rescue apical junction formation"
FT /evidence="ECO:0000250"
FT REGION 570..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..978
FT /note="Necessary for the catalytic activity"
FT /evidence="ECO:0000250"
FT REGION 979..985
FT /note="Negatively regulates the responsiveness of the
FT catalytic activity by cardiolipin and is required for
FT optimal activation by the GTP-bound RhoA"
FT /evidence="ECO:0000250"
FT COMPBIAS 120..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 783
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 664..672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 687
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 117..118
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT SITE 701..702
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWW9"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWW9"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 817
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16513"
FT MOD_RES 959
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 985 AA; 112069 MW; AE71D30379715C3D CRC64;
MASNPDRGEI LLTELQVDSR PLPFSENVSA VQKLDFSDTI VQQKLDDVKD RIKREIRKEL
KIKEGAENLR KVTTDKKNLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDYTDCPR
TPDTPNSDSR SSTSNNRRLM ALQKQLDIEL KVKQGAENMI QMYSNGPSKD RKLHGTAQQL
LQDNKTKIEV IRMHILQAVL TNELAFDNAK PVISPLELRN GRIIEHHFRI EFAVAEGAKN
VMKLLGSGKV TDRKALSEAQ ARFNESSQKL DLLKYSLEQR LNELPKNHPK SSVVIEELSL
VASPTLSPRQ SMLSTQNQYS TLSKPAALTG TLEVRLWGAK ISWENVPGRS KATSVALPGW
SPSENRSSFM SRTSKSKSGS SRNLLKTDDL SNDVCAVLKL DNTVVGQTIW KPISNQSWDQ
KFTLELDRSR ELEISVYWRD WRSLCAVKFL RLEDFLDNQR HGMALYLEPQ GTLFAEVTFF
NPVIERRPKL QRQKKIFSKQ QGKTFLRAPQ MNINIATWGR LVRRAIPTVN HSGTFSPQTP
VPATVPVVDA RTPELAPPAS DSTVTKLDFD LEPEAPPAPP RASSLGEIDD SSELRVLDIP
GQGSETVFDI ENDRNNMRPK SKSEYELNIP DSSRSCWSVG ELEDKRSQQR FQFNLQDFRC
CAVLGRGHFG KVLLAEYKHT NEMFAIKALK KGDIVARDEV DSLMCEKRIF ETVNSVRHPF
LVNLFACFQT KEHVCFVMEY AAGGDLMMHI HTDVFSEPRA VFYAACVVLG LQYLHEHKIV
YRDLKLDNLL LDTEASVKIA DFGLCKEGMG YGDRTSTFCG TPEFLAPEVL TETSYTRAVD
WWGLGVLIYE MLVGESPFPG DDEEEVFDSI VNDEVRYPRF LSTEAISIMR RLLRRNPERR
LGAGEKDAED VKKHPFFRLT DWSALLDKKV KPPFVPTIRG REDVSNFDDE FTSEAPILTP
PREPRILLEE EQEMFRDFDY VADWC
