CDC14_CAEEL
ID CDC14_CAEEL Reviewed; 709 AA.
AC P81299; A0A0K3AQY3; A0A0K3ATW0; P81300; Q09955; Q09976; Q6DLY2; Q6DLY3;
AC Q6DLY4; Q6DLY5; Q6DLY6; Q8MQD6;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Tyrosine-protein phosphatase cdc-14;
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:12213836};
DE AltName: Full=Cell division cycle-related protein 14;
GN Name=cdc-14 {ECO:0000303|PubMed:12213836, ECO:0000303|PubMed:15247923,
GN ECO:0000312|WormBase:C17G10.4h};
GN ORFNames=C17G10.4 {ECO:0000312|WormBase:C17G10.4h};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C; D AND E), FUNCTION, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 446-GLN--SER-709.
RX PubMed=15247923; DOI=10.1038/ncb1154;
RA Saito R.M., Perreault A., Peach B., Satterlee J.S., van den Heuvel S.;
RT "The CDC-14 phosphatase controls developmental cell-cycle arrest in C.
RT elegans.";
RL Nat. Cell Biol. 6:777-783(2004).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RA Ernsting B.R., Li L., Wishart M.J., Dixon J.E.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-295.
RX PubMed=12213836; DOI=10.1083/jcb.200202054;
RA Gruneberg U., Glotzer M., Gartner A., Nigg E.A.;
RT "The CeCDC-14 phosphatase is required for cytokinesis in the Caenorhabditis
RT elegans embryo.";
RL J. Cell Biol. 158:901-914(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION (ISOFORM C), DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, NUCLEAR EXPORT SIGNAL, NUCLEAR LOCALIZATION SIGNAL, AND
RP MUTAGENESIS OF 366-LYS--ARG-371 AND 372-LEU--LEU-381.
RX PubMed=21723944; DOI=10.1016/j.mod.2011.06.001;
RA Roy S.H., Clayton J.E., Holmen J., Beltz E., Saito R.M.;
RT "Control of Cdc14 activity coordinates cell cycle and development in
RT Caenorhabditis elegans.";
RL Mech. Dev. 128:317-326(2011).
CC -!- FUNCTION: Protein phosphatase that negatively regulates the G1-to-S
CC phase transition to inhibit the cell cycle and establish quiescence in
CC cells of multiple lineages including vulval, hypodermal and intestinal
CC (PubMed:15247923, PubMed:21723944). Promotes nuclear accumulation and
CC activity of the cyclin-dependent kinase inhibitor cki-1 which leads to
CC inhibition of G1 progression during vulval tissue development
CC (PubMed:15247923). Has been shown to not be required for cytokinesis
CC (PubMed:15247923). However, in the embryo, in a contrasting study, has
CC been shown to act as a regulator of central spindle formation and
CC cytokinesis, and may be required for localization of the spindle
CC component zen-4, and its interacting partner air-2 at the spindle
CC during late cell divisions (PubMed:12213836).
CC {ECO:0000269|PubMed:12213836, ECO:0000269|PubMed:15247923,
CC ECO:0000269|PubMed:21723944}.
CC -!- FUNCTION: [Isoform c]: Main regulator of cell cycle arrest in vulval
CC precursor cells. {ECO:0000269|PubMed:21723944}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:12213836};
CC -!- ACTIVITY REGULATION: Inhibited by sodium orthovanadate. Weakly
CC inhibited by sodium fluoride and okadaic acid.
CC {ECO:0000269|PubMed:12213836}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12213836,
CC ECO:0000269|PubMed:15247923}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:15247923}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:12213836,
CC ECO:0000269|PubMed:15247923}. Midbody {ECO:0000269|PubMed:12213836}.
CC Nucleus {ECO:0000269|PubMed:15247923}. Note=Localizes to the cytoplasm
CC throughout interphase (PubMed:15247923). As cells enter prophase,
CC accumulates at the centrosomes (PubMed:15247923). During metaphase and
CC anaphase, localizes to the spindle, in particular spindle asters and
CC the spindle mid zone (PubMed:15247923, PubMed:12213836). During late
CC telophase, localizes to cytoplasmic aggregates (PubMed:15247923). In
CC some studies, localizes to the midbody during late telophase
CC (PubMed:12213836). Localizes to the cytoplasm in G1-arrested cells
CC (PubMed:15247923). Localizes to the nucleus or nucleolus in postmitotic
CC cells (PubMed:15247923). Some studies report no localization to
CC centrosomes or nuclei (PubMed:12213836). Co-localizes with zen-4 at the
CC spindle, and localization may be dependent on each other
CC (PubMed:12213836). {ECO:0000269|PubMed:12213836,
CC ECO:0000269|PubMed:15247923}.
CC -!- SUBCELLULAR LOCATION: [Isoform c]: Cytoplasm
CC {ECO:0000269|PubMed:21723944}. Nucleus {ECO:0000269|PubMed:21723944}.
CC Note=Localizes to the cytoplasm during interphase, but localizes to the
CC nucleus during cell cycle arrest. {ECO:0000269|PubMed:21723944}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=h {ECO:0000312|WormBase:C17G10.4h};
CC IsoId=P81299-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C17G10.4a};
CC IsoId=P81299-2; Sequence=VSP_059807, VSP_059811;
CC Name=c {ECO:0000312|WormBase:C17G10.4c};
CC IsoId=P81299-3; Sequence=VSP_059807, VSP_059808;
CC Name=d {ECO:0000312|WormBase:C17G10.4d};
CC IsoId=P81299-4; Sequence=VSP_059807;
CC Name=e {ECO:0000312|WormBase:C17G10.4e};
CC IsoId=P81299-5; Sequence=VSP_059811;
CC Name=g {ECO:0000312|WormBase:C17G10.4g};
CC IsoId=P81299-7; Sequence=VSP_059809, VSP_059810;
CC -!- DEVELOPMENTAL STAGE: Expressed in the soma during early embryogenesis,
CC and widely expressed after hatching. Isoform C: Expressed in the soma
CC during early embryogenesis, but after hatching, expression in larvae is
CC restricted to V and P lineages, the postembryonic lineages that
CC contribute to the seam cells and vulval precursor cells, respectively.
CC {ECO:0000269|PubMed:21723944}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in extra cell
CC divisions in the vulval lineage, but does not result in defects in
CC cytokinesis (PubMed:15247923, PubMed:21723944). RNAi-mediated knockdown
CC decreases cki-1 expression in the nucleus of vulval precursor cells
CC (PubMed:15247923). In contrasting studies RNAi-mediated knockdown
CC results in embryonic lethality with the production of multinucleated
CC embryos that exhibit cytokinesis failure during telophase, no central
CC spindle formation, and failed localization of the spindle component
CC zen-4 and its interacting partner air-2 at the spindle in either
CC anaphase or telophase (PubMed:12213836). {ECO:0000269|PubMed:12213836,
CC ECO:0000269|PubMed:15247923, ECO:0000269|PubMed:21723944}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class CDC14 subfamily. {ECO:0000305}.
CC -!- CAUTION: Has been shown in one report to not be localized to
CC centrosomes or nuclei, and based on RNAi-mediated knockdown studies,
CC has been shown to play a role in cytokinesis (PubMed:12213836).
CC However, has also been reported to localize to centrosomes and nuclei
CC and to have no role in cytokinesis, based on results obtained using the
CC cdc-14 he118 mutant and RNAi-mediated knockdown (PubMed:15247923).
CC {ECO:0000269|PubMed:12213836, ECO:0000269|PubMed:15247923}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT74543.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AY661743; AAT74542.1; -; mRNA.
DR EMBL; AY661744; AAT74543.1; ALT_SEQ; mRNA.
DR EMBL; AY661745; AAT74544.1; -; mRNA.
DR EMBL; AY661746; AAT74545.1; -; mRNA.
DR EMBL; AY661747; AAT74546.1; -; mRNA.
DR EMBL; AF000363; AAB94407.1; -; mRNA.
DR EMBL; BX284602; CCD64951.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD64953.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD64954.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD64955.1; -; Genomic_DNA.
DR EMBL; BX284602; CTQ86448.1; -; Genomic_DNA.
DR EMBL; BX284602; CTQ86449.1; -; Genomic_DNA.
DR PIR; E88158; E88158.
DR PIR; T34097; T34097.
DR RefSeq; NP_001021969.1; NM_001026798.5. [P81299-5]
DR RefSeq; NP_001300509.1; NM_001313580.1.
DR RefSeq; NP_001300510.1; NM_001313581.1. [P81299-1]
DR RefSeq; NP_495085.2; NM_062684.5.
DR RefSeq; NP_495086.1; NM_062685.3.
DR RefSeq; NP_740991.1; NM_170993.4.
DR AlphaFoldDB; P81299; -.
DR SMR; P81299; -.
DR BioGRID; 39287; 7.
DR DIP; DIP-25903N; -.
DR STRING; 6239.C17G10.4b.2; -.
DR iPTMnet; P81299; -.
DR EPD; P81299; -.
DR PaxDb; P81299; -.
DR PeptideAtlas; P81299; -.
DR EnsemblMetazoa; C17G10.4a.1; C17G10.4a.1; WBGene00000383. [P81299-2]
DR EnsemblMetazoa; C17G10.4c.1; C17G10.4c.1; WBGene00000383. [P81299-3]
DR EnsemblMetazoa; C17G10.4d.1; C17G10.4d.1; WBGene00000383. [P81299-4]
DR EnsemblMetazoa; C17G10.4e.1; C17G10.4e.1; WBGene00000383. [P81299-5]
DR EnsemblMetazoa; C17G10.4g.1; C17G10.4g.1; WBGene00000383. [P81299-7]
DR EnsemblMetazoa; C17G10.4h.1; C17G10.4h.1; WBGene00000383. [P81299-1]
DR GeneID; 173945; -.
DR UCSC; C17G10.4b; c. elegans. [P81299-1]
DR CTD; 173945; -.
DR WormBase; C17G10.4a; CE30868; WBGene00000383; cdc-14. [P81299-2]
DR WormBase; C17G10.4c; CE08288; WBGene00000383; cdc-14. [P81299-3]
DR WormBase; C17G10.4d; CE06845; WBGene00000383; cdc-14. [P81299-4]
DR WormBase; C17G10.4e; CE36916; WBGene00000383; cdc-14. [P81299-5]
DR WormBase; C17G10.4g; CE50122; WBGene00000383; cdc-14. [P81299-7]
DR WormBase; C17G10.4h; CE01789; WBGene00000383; cdc-14. [P81299-1]
DR eggNOG; KOG1720; Eukaryota.
DR GeneTree; ENSGT00940000170847; -.
DR HOGENOM; CLU_288890_0_0_1; -.
DR InParanoid; P81299; -.
DR OMA; MQKFCWS; -.
DR OrthoDB; 1357618at2759; -.
DR Reactome; R-CEL-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR PRO; PR:P81299; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000383; Expressed in embryo and 4 other tissues.
DR GO; GO:0000235; C:astral microtubule; IDA:WormBase.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:1902636; C:kinociliary basal body; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IDA:WormBase.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:WormBase.
DR GO; GO:0005730; C:nucleolus; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IDA:WormBase.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IDA:WormBase.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:WormBase.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:WormBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:WormBase.
DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:WormBase.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:1903452; P:positive regulation of G1 to G0 transition; IMP:WormBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:WormBase.
DR GO; GO:0060284; P:regulation of cell development; IMP:UniProtKB.
DR GO; GO:0007096; P:regulation of exit from mitosis; IBA:GO_Central.
DR GO; GO:0040028; P:regulation of vulval development; IMP:UniProtKB.
DR CDD; cd14499; CDC14_C; 1.
DR CDD; cd17657; CDC14_N; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR026070; CDC14.
DR InterPro; IPR044506; CDC14_C.
DR InterPro; IPR029260; DSPn.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR23339:SF27; PTHR23339:SF27; 1.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF14671; DSPn; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Hydrolase; Microtubule; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..709
FT /note="Tyrosine-protein phosphatase cdc-14"
FT /id="PRO_0000094880"
FT DOMAIN 196..354
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 403..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 366..371
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:21723944"
FT MOTIF 372..381
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:21723944"
FT COMPBIAS 403..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 295
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 542..555
FT /note="Missing (in isoform a, isoform c and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_059807"
FT VAR_SEQ 620..709
FT /note="ITKCSLTAESKPPKRILSMPGTSKSTSSLKKIQVSRPRPYPSTGVRVELCAN
FT GKSYDIRPRKEAHVIPGAGLAANTEALLGVCKLVNTLS -> FGLVRVPPDSPHSIMAH
FT RPPPTTSSRAPLSPHNYSTTQGYSTSSRGLYGDKKPLARGSVSTSTLPSMYMTRSCERK
FT (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_059808"
FT VAR_SEQ 620..695
FT /note="ITKCSLTAESKPPKRILSMPGTSKSTSSLKKIQVSRPRPYPSTGVRVELCAN
FT GKSYDIRPRKEAHVIPGAGLAANT -> FGLVRVPPDSPHSIMAHRPPPTTSSRAPLSP
FT HNYSTTQGYSTSSRGLYGDKKPLARGSVSTSTLPSMYMTRSCERK (in isoform
FT g)"
FT /evidence="ECO:0000305"
FT /id="VSP_059809"
FT VAR_SEQ 696..709
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_059810"
FT VAR_SEQ 701..708
FT /note="VCKLVNTL -> KRRKTA (in isoform a and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_059811"
FT MUTAGEN 295
FT /note="C->S: Abolishes phosphatase activity."
FT /evidence="ECO:0000269|PubMed:12213836"
FT MUTAGEN 366..371
FT /note="KRNVRR->AANVAA: Disrupts nuclear localization.
FT Localizes to the cytoplasm; when associated with 372-A--A-
FT 381."
FT /evidence="ECO:0000269|PubMed:21723944"
FT MUTAGEN 372..381
FT /note="LVNQVDDINL->AVNQVDDANA: Impairs nuclear export
FT signal. Disrupts cytoplasmic localization, conferring
FT nuclear localization during interphase. Localizes to the
FT cytoplasm; when associated with 366-A--A-371."
FT /evidence="ECO:0000269|PubMed:21723944"
FT MUTAGEN 446..709
FT /note="Missing: In he118; no effect on viability,
FT embryogenesis or fertility. Disrupts cell cycle arrest of
FT vulval precursor, intestinal, and hypodermal cells, and of
FT precursor cells that give rise to male specific structures
FT during postembryonic development. Vulval precursor cells
FT undergo an extra round of cell division during the L2
FT larval stage of development, but the additional precursor
FT cells do not disrupt formation of the vulval structure and
FT animals undergo normal vulval morphogenesis during the L4
FT larval stage. Does not result in defects in cytokinesis.
FT Overexpression of the cyclin dependent kinase inhibitor
FT cki-1, or knockout with the G1/S-specific cyclin-E cye-1
FT (eh10), rescues the cell division phenotype."
FT /evidence="ECO:0000269|PubMed:15247923"
SQ SEQUENCE 709 AA; 79740 MW; AB5873D8C7FEDB0C CRC64;
MREDHSPRRN NTIENTLTEL LPNRLYFGCF PNPDAIDKSD KSVKKTCFIN INNKFHYEPF
YEDFGPWNLS VLYRLCVQVG KLLEVEEKRS RRVVLFCQDD GTGQYDKIRV NTAYVLGAYL
IIYQGFSADD AYLKVSSGET VKFVGFRDAS MGSPQYLLHL HDVLRGIEKA LKFGWLDFSD
FDYEEYEFYE RVENGDFNWI IPGKILSFCG PHNESREENG YPYHAPDVYF DYFRENKVST
IVRLNAKNYD ASKFTKAGFD HVDLFFIDGS TPSDEIMLKF IKVVDNTKGG VAVHCKAGLG
RTGTLIACWM MKEYGLTAGE CMGWLRVCRP GSVIGPQQPY LIEKQKFCWS LSQSNGVHLT
QNKEEKRNVR RLVNQVDDIN LGEERISPKS RENTRPNILR RRVQVQNGRS TAPVTIAPAG
TSESRRSTKP SRVVDETALD DQGRSQGDRL LQLKAKHQHE SETTSPNSSS SRRFVKSSTP
QMTVPSQAYL NRNREPIIVT PSKNGTSSGT SSRQLKTTPN GNVAYRTRNS SGNTTSTLTR
TGNESYRFHN SLFYEPASAV FPSMASRRSE TTRYLSPTTP IKPMSPSYTD GTSPRYKARL
RSENPIGSTT STPFSLQPQI TKCSLTAESK PPKRILSMPG TSKSTSSLKK IQVSRPRPYP
STGVRVELCA NGKSYDIRPR KEAHVIPGAG LAANTEALLG VCKLVNTLS
