PCNA_MOUSE
ID PCNA_MOUSE Reviewed; 261 AA.
AC P17918;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Proliferating cell nuclear antigen;
DE Short=PCNA;
DE AltName: Full=Cyclin;
GN Name=Pcna;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lymphoid tissue;
RX PubMed=1726365; DOI=10.3109/10425179109039688;
RA Shipman-Appasamy P.M., Cohen K.S., Prystowsky M.B.;
RT "Nucleotide sequence of murine PCNA: interspecies comparison of the cDNA
RT and the 5' flanking region of the gene.";
RL DNA Seq. 2:181-191(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=1674997; DOI=10.1093/nar/19.9.2403;
RA Yamaguchi M., Hayashi Y., Hirose F., Matsuoka S., Moriuchi T.,
RA Shiroishi T., Moriwaki K., Matsukage A.;
RT "Molecular cloning and structural analysis of mouse gene and pseudogenes
RT for proliferating cell nuclear antigen.";
RL Nucleic Acids Res. 19:2403-2410(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-42.
RC TISSUE=T-cell;
RX PubMed=2906640; DOI=10.1002/jcb.240380306;
RA Shipman P.M., Sabath D.E., Fischer A.H., Comber P.G., Sullivan K.,
RA Tan E.M., Prystowsky M.B.;
RT "Cyclin mRNA and protein expression in recombinant interleukin 2-stimulated
RT cloned murine T lymphocytes.";
RL J. Cell. Biochem. 38:189-198(1988).
RN [5]
RP INTERACTION WITH PPP1R15A AND HHV-1 ICP34.5.
RX PubMed=9371605; DOI=10.1128/jvi.71.12.9442-9449.1997;
RA Brown S.M., MacLean A.R., McKie E.A., Harland J.;
RT "The herpes simplex virus virulence factor ICP34.5 and the cellular protein
RT MyD116 complex with proliferating cell nuclear antigen through the 63-
RT amino-acid domain conserved in ICP34.5, MyD116, and GADD34.";
RL J. Virol. 71:9442-9449(1997).
RN [6]
RP INTERACTION WITH APEX2.
RX PubMed=12573260; DOI=10.1016/s0888-7543(02)00009-5;
RA Ide Y., Tsuchimoto D., Tominaga Y., Iwamoto Y., Nakabeppu Y.;
RT "Characterization of the genomic structure and expression of the mouse
RT Apex2 gene.";
RL Genomics 81:47-57(2003).
RN [7]
RP PHOSPHORYLATION AT TYR-211.
RX PubMed=17115032; DOI=10.1038/ncb1501;
RA Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C.,
RA McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.;
RT "Tyrosine phosphorylation controls PCNA function through protein
RT stability.";
RL Nat. Cell Biol. 8:1359-1368(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH RTEL1, AND SUBCELLULAR LOCATION.
RX PubMed=24115439; DOI=10.1126/science.1241779;
RA Vannier J.B., Sandhu S., Petalcorin M.I., Wu X., Nabi Z., Ding H.,
RA Boulton S.J.;
RT "RTEL1 is a replisome-associated helicase that promotes telomere and
RT genome-wide replication.";
RL Science 342:239-242(2013).
CC -!- FUNCTION: Auxiliary protein of DNA polymerase delta and is involved in
CC the control of eukaryotic DNA replication by increasing the
CC polymerase's processibility during elongation of the leading strand.
CC Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-
CC phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease,
CC APEX2 activities. Has to be loaded onto DNA in order to be able to
CC stimulate APEX2. Plays a key role in DNA damage response (DDR) by being
CC conveniently positioned at the replication fork to coordinate DNA
CC replication with DNA repair and DNA damage tolerance pathways. Acts as
CC a loading platform to recruit DDR proteins that allow completion of DNA
CC replication after DNA damage and promote postreplication repair:
CC Monoubiquitinated PCNA leads to recruitment of translesion (TLS)
CC polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is
CC involved in error-free pathway and employs recombination mechanisms to
CC synthesize across the lesion (By similarity).
CC {ECO:0000250|UniProtKB:P12004}.
CC -!- SUBUNIT: Homotrimer. Interacts with p300/EP300; the interaction occurs
CC on chromatin in UV-irradiated damaged cells. Interacts with CREBBP (via
CC transactivation domain and C-terminus); the interaction occurs on
CC chromatin in UV-irradiated damaged cells. Directly interacts with
CC POLD1, POLD3 and POLD4 subunits of the DNA polymerase delta complex,
CC POLD3 being the major interacting partner; the interaction with POLD3
CC is inhibited by CDKN1A/p21(CIP1). Forms a complex with activator 1
CC heteropentamer in the presence of ATP. Interacts with EXO1, POLH, POLK,
CC DNMT1, ERCC5, FEN1, CDC6 and POLDIP2 (By similarity). Interacts with
CC APEX2; this interaction is triggered by reactive oxygen species and
CC increased by misincorporation of uracil in nuclear DNA
CC (PubMed:12573260). Forms a ternary complex with DNTTIP2 and core
CC histone (By similarity). Interacts with KCTD10 (By similarity).
CC Interacts with PPP1R15A (PubMed:9371605). Interacts with SMARCA5/SNF2H
CC (By similarity). Interacts with BAZ1B/WSTF; the interaction is direct
CC and is required for BAZ1B/WSTF binding to replication foci during S
CC phase (By similarity). Interacts with HLTF and SHPRH. Interacts with
CC NUDT15; this interaction is disrupted in response to UV irradiation and
CC acetylation. Interacts with CDKN1A/p21(CIP1) and CDT1; interacts via
CC their PIP-box which also recruits the DCX(DTL) complex. The interaction
CC with CDKN1A inhibits POLD3 binding. Interacts with DDX11. Interacts
CC with EGFR; positively regulates PCNA. Interacts with PARPBP. Interacts
CC (when ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA
CC ubiquitination. Interacts (when polyubiquitinated) with ZRANB3.
CC Interacts with SMARCAD1. Interacts with CDKN1C. Interacts with PCLAF
CC (via PIP-box) (By similarity). Interacts with RTEL1 (via PIP-box); the
CC interaction is direct and essential for the suppression of telomere
CC fragility (PubMed:24115439). Interacts with FAM111A (via PIP-box); the
CC interaction is direct and required for PCNA loading on chromatin
CC binding. Interacts with LIG1. Interacts with SETMAR. Interacts with
CC ANKRD17. Interacts with FBXO18/FBH1 (via PIP-box); the interaction
CC recruits the DCX(DTL) complex and promotes ubiquitination and
CC degradation of FBXO18/FBH1. Interacts with POLN (By similarity).
CC Interacts with SDE2 (via PIP-box); the interaction is direct and
CC prevents ultraviolet light induced monoubiquitination (By similarity).
CC Component of the replisome complex composed of at least DONSON, MCM2,
CC MCM7, PCNA and TICRR; interaction at least with PCNA occurs during DNA
CC replication (By similarity). Interacts with MAPK15; the interaction is
CC chromatin binding dependent and prevents MDM2-mediated PCNA destruction
CC by inhibiting the association of PCNA with MDM2. Interacts with PARP10
CC (via PIP-box) (By similarity). Interacts with DDI2 (By similarity).
CC Interacts with HMCES (via PIP-box) (By similarity). Interacts with
CC TRAIP (via PIP-box) (By similarity). Interacts with UHRF2 (By
CC similarity). Interacts with ALKBH2; this interaction is enhanced during
CC the S-phase of the cell cycle. Interacts with ATAD5; the interaction
CC promotes USP1-mediated PCNA deubiquitination (By similarity).
CC {ECO:0000250|UniProtKB:P04961, ECO:0000250|UniProtKB:P12004,
CC ECO:0000269|PubMed:12573260, ECO:0000269|PubMed:24115439,
CC ECO:0000269|PubMed:9371605}.
CC -!- INTERACTION:
CC P17918; P39689: Cdkn1a; NbExp=2; IntAct=EBI-1173716, EBI-1174103;
CC P17918; Q9Z111: Gadd45g; NbExp=2; IntAct=EBI-1173716, EBI-1173616;
CC P17918; P62137: Ppp1ca; NbExp=2; IntAct=EBI-1173716, EBI-357187;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24115439}.
CC Note=Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage
CC (By similarity). Forms nuclear foci representing sites of ongoing DNA
CC replication and vary in morphology and number during S phase. Together
CC with APEX2, is redistributed in discrete nuclear foci in presence of
CC oxidative DNA damaging agents. {ECO:0000250|UniProtKB:P12004}.
CC -!- INDUCTION: Induced in IL2-stimulated proliferating T-lymphocytes.
CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes
CC chromatin-associated PCNA (By similarity).
CC {ECO:0000250|UniProtKB:P12004}.
CC -!- PTM: Acetylated by CREBBP and p300/EP300; preferentially acetylated by
CC CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon
CC loading on chromatin in response to UV irradiation. Lysine acetylation
CC disrupts association with chromatin, hence promoting PCNA
CC ubiquitination and proteasomal degradation in response to UV damage in
CC a CREBBP- and EP300-dependent manner. Acetylation disrupts interaction
CC with NUDT15 and promotes degradation (By similarity).
CC {ECO:0000250|UniProtKB:P12004}.
CC -!- PTM: Ubiquitinated. Following DNA damage, can be either
CC monoubiquitinated to stimulate direct bypass of DNA lesions by
CC specialized DNA polymerases or polyubiquitinated to promote
CC recombination-dependent DNA synthesis across DNA lesions by template
CC switching mechanisms. Following induction of replication stress,
CC monoubiquitinated by the UBE2B-RAD18 complex on Lys-164, leading to
CC recruit translesion (TLS) polymerases, which are able to synthesize
CC across DNA lesions in a potentially error-prone manner. An error-free
CC pathway also exists and requires non-canonical polyubiquitination on
CC Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2
CC complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH. This
CC error-free pathway, also known as template switching, employs
CC recombination mechanisms to synthesize across the lesion, using as a
CC template the undamaged, newly synthesized strand of the sister
CC chromatid. Monoubiquitination at Lys-164 also takes place in undamaged
CC proliferating cells, and is mediated by the DCX(DTL) complex, leading
CC to enhance PCNA-dependent translesion DNA synthesis. Sumoylated during
CC S phase (By similarity). {ECO:0000250|UniProtKB:P12004}.
CC -!- PTM: Methylated on glutamate residues by ARMT1.
CC {ECO:0000250|UniProtKB:P12004}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}.
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DR EMBL; X53068; CAA37243.1; -; mRNA.
DR EMBL; X57800; CAA40938.1; -; Genomic_DNA.
DR EMBL; BC005778; AAH05778.1; -; mRNA.
DR EMBL; BC010343; AAH10343.1; -; mRNA.
DR CCDS; CCDS16771.1; -.
DR PIR; S15703; WMMS.
DR RefSeq; NP_035175.1; NM_011045.2.
DR AlphaFoldDB; P17918; -.
DR BMRB; P17918; -.
DR SMR; P17918; -.
DR BioGRID; 202049; 68.
DR ComplexPortal; CPX-541; PCNA homotrimer.
DR CORUM; P17918; -.
DR DIP; DIP-39409N; -.
DR IntAct; P17918; 39.
DR MINT; P17918; -.
DR STRING; 10090.ENSMUSP00000028817; -.
DR iPTMnet; P17918; -.
DR PhosphoSitePlus; P17918; -.
DR SwissPalm; P17918; -.
DR REPRODUCTION-2DPAGE; P17918; -.
DR EPD; P17918; -.
DR PaxDb; P17918; -.
DR PeptideAtlas; P17918; -.
DR PRIDE; P17918; -.
DR ProteomicsDB; 294031; -.
DR TopDownProteomics; P17918; -.
DR Antibodypedia; 3769; 2642 antibodies from 54 providers.
DR DNASU; 18538; -.
DR Ensembl; ENSMUST00000028817; ENSMUSP00000028817; ENSMUSG00000027342.
DR GeneID; 18538; -.
DR KEGG; mmu:18538; -.
DR UCSC; uc008mml.1; mouse.
DR CTD; 5111; -.
DR MGI; MGI:97503; Pcna.
DR VEuPathDB; HostDB:ENSMUSG00000027342; -.
DR eggNOG; KOG1636; Eukaryota.
DR GeneTree; ENSGT00390000004965; -.
DR HOGENOM; CLU_043978_3_0_1; -.
DR InParanoid; P17918; -.
DR OMA; EMKLINM; -.
DR OrthoDB; 1012066at2759; -.
DR PhylomeDB; P17918; -.
DR TreeFam; TF313441; -.
DR Reactome; R-MMU-110312; Translesion synthesis by REV1.
DR Reactome; R-MMU-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-MMU-110320; Translesion Synthesis by POLH.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-MMU-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-MMU-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-MMU-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-MMU-5655862; Translesion synthesis by POLK.
DR Reactome; R-MMU-5656121; Translesion synthesis by POLI.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-MMU-69091; Polymerase switching.
DR Reactome; R-MMU-69166; Removal of the Flap Intermediate.
DR Reactome; R-MMU-69183; Processive synthesis on the lagging strand.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR BioGRID-ORCS; 18538; 56 hits in 103 CRISPR screens.
DR ChiTaRS; Pcna; mouse.
DR PRO; PR:P17918; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P17918; protein.
DR Bgee; ENSMUSG00000027342; Expressed in thymus and 75 other tissues.
DR ExpressionAtlas; P17918; baseline and differential.
DR Genevisible; P17918; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005652; C:nuclear lamina; IDA:MGI.
DR GO; GO:0043596; C:nuclear replication fork; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043626; C:PCNA complex; ISS:UniProtKB.
DR GO; GO:0070557; C:PCNA-p21 complex; ISS:UniProtKB.
DR GO; GO:0005657; C:replication fork; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:0032139; F:dinucleotide insertion or deletion binding; ISO:MGI.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0032405; F:MutLalpha complex binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IDA:MGI.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0006298; P:mismatch repair; ISO:MGI.
DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; IGI:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032077; P:positive regulation of deoxyribonuclease activity; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; ISO:MGI.
DR GO; GO:0031297; P:replication fork processing; IGI:BHF-UCL.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:1902065; P:response to L-glutamate; IEA:Ensembl.
DR GO; GO:0033993; P:response to lipid; ISO:MGI.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR InterPro; IPR000730; Pr_cel_nuc_antig.
DR InterPro; IPR022649; Pr_cel_nuc_antig_C.
DR InterPro; IPR022659; Pr_cel_nuc_antig_CS.
DR InterPro; IPR022648; Pr_cel_nuc_antig_N.
DR Pfam; PF02747; PCNA_C; 1.
DR Pfam; PF00705; PCNA_N; 1.
DR PRINTS; PR00339; PCNACYCLIN.
DR TIGRFAMs; TIGR00590; pcna; 1.
DR PROSITE; PS01251; PCNA_1; 1.
DR PROSITE; PS00293; PCNA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..261
FT /note="Proliferating cell nuclear antigen"
FT /id="PRO_0000149160"
FT DNA_BIND 61..80
FT /evidence="ECO:0000255"
FT MOD_RES 14
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12004"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12004"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12004"
FT MOD_RES 211
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000269|PubMed:17115032"
FT MOD_RES 248
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P12004"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P12004"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P12004"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P12004"
FT CONFLICT 3..5
FT /note="EAR -> LES (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="A -> T (in Ref. 2; CAA37243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 28785 MW; F705CCBDD3205986 CRC64;
MFEARLIQGS ILKKVLEALK DLINEACWDV SSGGVNLQSM DSSHVSLVQL TLRSEGFDTY
RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA LVFEAPNQEK VSDYEMKLMD
LDVEQLGIPE QEYSCVIKMP SGEFARICRD LSHIGDAVVI SCAKNGVKFS ASGELGNGNI
KLSQTSNVDK EEEAVTIEMN EPVHLTFALR YLNFFTKATP LSPTVTLSMS ADVPLVVEYK
IADMGHLKYY LAPKIEDEEA S
