PEG3_MOUSE
ID PEG3_MOUSE Reviewed; 1571 AA.
AC Q3URU2; O54978; Q3TQ69; Q5EBP7; Q61138; Q6GQS0; Q80U47; Q8R5N0; Q9QX53;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Paternally-expressed gene 3 protein;
DE AltName: Full=ASF-1;
GN Name=Peg3; Synonyms=Kiaa0287, Pw1;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8563758; DOI=10.1038/ng0296-186;
RA Kuroiwa Y., Kaneko-Ishino T., Kagitani F., Kohda T., Li L.-L., Tada M.,
RA Suzuki R., Yokoyama M., Shiroishi T., Wakana S., Barton S.C., Ishino F.,
RA Surani M.A.;
RT "Peg3 imprinted gene on proximal chromosome 7 encodes for a zinc finger
RT protein.";
RL Nat. Genet. 12:186-190(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=B6C3H F1;
RX PubMed=11260267; DOI=10.1046/j.1365-2443.2001.00412.x;
RA Kohda T., Asai A., Kuroiwa Y., Kobayashi S., Aisaka K., Nagashima G.,
RA Yoshida M.C., Kondo Y., Kagiyama N., Kirino T., Kaneko-Ishino T.,
RA Ishino F.;
RT "Tumour suppressor activity of human imprinted gene PEG3 in a glioma cell
RT line.";
RL Genes Cells 6:237-247(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Head;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-352 (ISOFORM 1).
RX PubMed=10704281; DOI=10.1006/geno.1999.6103;
RA Li L.-L., Szeto I.Y.-Y., Cattanach B.M., Ishino F., Surani M.A.;
RT "Organization and parent-of-origin-specific methylation of imprinted Peg3
RT gene on mouse proximal chromosome 7.";
RL Genomics 63:333-340(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-1571 (ISOFORM 1), SUBCELLULAR
RP LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129/Sv; TISSUE=Limb bud;
RX PubMed=8806818; DOI=10.1006/dbio.1996.0172;
RA Relaix F., Weng X., Marazzi G., Yang E., Copeland N.G., Jenkins N.,
RA Spence S.E., Sassoon D.;
RT "Pw1, a novel zinc finger gene implicated in the myogenic and neuronal
RT lineages.";
RL Dev. Biol. 177:383-396(1996).
RN [8]
RP FUNCTION, AND INTERACTION WITH TRAF2.
RX PubMed=9500555; DOI=10.1038/ng0398-287;
RA Relaix F., Wei X.-J., Wu X., Sassoon D.A.;
RT "Peg3/Pw1 is an imprinted gene involved in the TNF-NFkappaB signal
RT transduction pathway.";
RL Nat. Genet. 18:287-291(1998).
RN [9]
RP FUNCTION.
RX PubMed=10195900; DOI=10.1126/science.284.5412.330;
RA Li L.-L., Keverne E.B., Aparicio S.A., Ishino F., Barton S.C., Surani M.A.;
RT "Regulation of maternal behavior and offspring growth by paternally
RT expressed Peg3.";
RL Science 284:330-333(1999).
RN [10]
RP FUNCTION, INDUCTION, AND INTERACTION WITH SIAH1A AND SIAH2.
RX PubMed=10681424; DOI=10.1073/pnas.040378897;
RA Relaix F., Wei X., Li W., Pan J., Lin Y., Bowtell D.D., Sassoon D.A.,
RA Wu X.;
RT "Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in
RT p53-mediated apoptosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:2105-2110(2000).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=11331620; DOI=10.1093/hmg/10.10.1093;
RA Hiby S.E., Lough M., Keverne E.B., Surani M.A., Loke Y.W., King A.;
RT "Paternal monoallelic expression of PEG3 in the human placenta.";
RL Hum. Mol. Genet. 10:1093-1100(2001).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=11943780; DOI=10.1074/jbc.m201907200;
RA Johnson M.D., Wu X., Aithmitti N., Morrison R.S.;
RT "Peg3/Pw1 is a mediator between p53 and Bax in DNA damage-induced neuronal
RT death.";
RL J. Biol. Chem. 277:23000-23007(2002).
CC -!- FUNCTION: Induces apoptosis in cooperation with SIAH1A. Acts as a
CC mediator between p53/TP53 and BAX in a neuronal death pathway that is
CC activated by DNA damage. Acts synergistically with TRAF2 and inhibits
CC TNF induced apoptosis through activation of NF-kappa-B. Plays a role in
CC regulating maternal behavior and offspring growth.
CC {ECO:0000269|PubMed:10195900, ECO:0000269|PubMed:10681424,
CC ECO:0000269|PubMed:11943780, ECO:0000269|PubMed:9500555}.
CC -!- SUBUNIT: Homodimer. Interacts with SIAH1A and SIAH2. Interacts with
CC TRAF2. {ECO:0000269|PubMed:10681424, ECO:0000269|PubMed:8806818,
CC ECO:0000269|PubMed:9500555}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3URU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3URU2-2; Sequence=VSP_020375, VSP_020376, VSP_020377;
CC -!- TISSUE SPECIFICITY: Brain, glial cells, neurons, skeletal muscle,
CC uterus and placenta. In the placenta it found in all trophoblast cells.
CC {ECO:0000269|PubMed:11260267, ECO:0000269|PubMed:11331620,
CC ECO:0000269|PubMed:8563758, ECO:0000269|PubMed:8806818}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed upon gastrulation and
CC subsequently becomes restricted to skeletal muscle and subregions of
CC the CNS. At 9.5 dpc, expressed in the branchial arches, somites and gut
CC but little in the heart and neural tissues. At 12.5 dpc strongly
CC expressed in the cranial skeleton, tongue, vertebral cartilage,
CC pituitary and the luminal epithelium. {ECO:0000269|PubMed:8563758,
CC ECO:0000269|PubMed:8806818}.
CC -!- INDUCTION: Induced during p53/TP53 mediated apoptosis. Up-regulated by
CC DNA damage in cortical neurons in the presence of p53/TP53.
CC {ECO:0000269|PubMed:10681424, ECO:0000269|PubMed:11943780}.
CC -!- DOMAIN: The SCAN domain enables PEG3 homo- or heterodimerization to
CC control gene expression in a combinatorial fashion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52770.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB85589.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC65520.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF038939; AAB96922.1; -; mRNA.
DR EMBL; AB003040; BAB85589.1; ALT_FRAME; mRNA.
DR EMBL; AK141217; BAE24595.1; -; mRNA.
DR EMBL; AK163845; BAE37516.1; -; mRNA.
DR EMBL; AK122238; BAC65520.2; ALT_INIT; Transcribed_RNA.
DR EMBL; BC072661; AAH72661.1; -; mRNA.
DR EMBL; BC085183; AAH85183.1; -; mRNA.
DR EMBL; BC089344; AAH89344.1; -; mRNA.
DR EMBL; AF105266; AAF16868.1; -; Genomic_DNA.
DR EMBL; AF105264; AAF16868.1; JOINED; Genomic_DNA.
DR EMBL; AF105265; AAF16868.1; JOINED; Genomic_DNA.
DR EMBL; U48804; AAC52770.1; ALT_FRAME; Genomic_DNA.
DR CCDS; CCDS20783.1; -. [Q3URU2-1]
DR PIR; T14155; T14155.
DR PIR; T30173; T30173.
DR RefSeq; NP_032843.2; NM_008817.2. [Q3URU2-1]
DR RefSeq; XP_017177520.1; XM_017322031.1. [Q3URU2-1]
DR RefSeq; XP_017177521.1; XM_017322032.1.
DR AlphaFoldDB; Q3URU2; -.
DR BioGRID; 202106; 3.
DR IntAct; Q3URU2; 1.
DR MINT; Q3URU2; -.
DR STRING; 10090.ENSMUSP00000050750; -.
DR iPTMnet; Q3URU2; -.
DR PhosphoSitePlus; Q3URU2; -.
DR MaxQB; Q3URU2; -.
DR PaxDb; Q3URU2; -.
DR PeptideAtlas; Q3URU2; -.
DR PRIDE; Q3URU2; -.
DR ProteomicsDB; 287822; -. [Q3URU2-1]
DR ProteomicsDB; 287823; -. [Q3URU2-2]
DR Antibodypedia; 19625; 182 antibodies from 24 providers.
DR DNASU; 18616; -.
DR Ensembl; ENSMUST00000051209; ENSMUSP00000050750; ENSMUSG00000002265. [Q3URU2-1]
DR GeneID; 18616; -.
DR KEGG; mmu:18616; -.
DR UCSC; uc009fbw.1; mouse. [Q3URU2-1]
DR CTD; 5178; -.
DR MGI; MGI:104748; Peg3.
DR VEuPathDB; HostDB:ENSMUSG00000002265; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162525; -.
DR HOGENOM; CLU_005305_0_0_1; -.
DR InParanoid; Q3URU2; -.
DR PhylomeDB; Q3URU2; -.
DR TreeFam; TF337075; -.
DR BioGRID-ORCS; 18616; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Peg3; mouse.
DR PRO; PR:Q3URU2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3URU2; protein.
DR Bgee; ENSMUSG00000002265; Expressed in humerus cartilage element and 269 other tissues.
DR ExpressionAtlas; Q3URU2; baseline and differential.
DR Genevisible; Q3URU2; MM.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 12.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1571
FT /note="Paternally-expressed gene 3 protein"
FT /id="PRO_0000249229"
FT REPEAT 942..946
FT /note="1-1"
FT REPEAT 967..971
FT /note="1-2"
FT REPEAT 987..991
FT /note="2-1"
FT REPEAT 992..996
FT /note="1-3"
FT REPEAT 997..1001
FT /note="2-2"
FT REPEAT 1002..1006
FT /note="1-4"
FT REPEAT 1007..1011
FT /note="2-3"
FT REPEAT 1012..1016
FT /note="1-5"
FT REPEAT 1017..1021
FT /note="1-6"
FT REPEAT 1022..1026
FT /note="1-7"
FT REPEAT 1027..1031
FT /note="1-8"
FT REPEAT 1032..1036
FT /note="1-9"
FT REPEAT 1047..1051
FT /note="1-10"
FT ZN_FING 325..347
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..400
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 436..458
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 520..542
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 850..872
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1091..1113
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1147..1169
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1209..1231
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1266..1289
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1317..1339
FT /note="C2H2-type 10; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1488..1510
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1547..1569
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..265
FT /note="10 X 5 AA repeat of P-H-X-X-E"
FT REGION 199..265
FT /note="3 X 5 AA repeat of P-H-D-D-K"
FT REGION 456..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1420
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1483
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 989..1048
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020375"
FT VAR_SEQ 1202..1254
FT /note="PAVSGSAIRCRQCGQGFIHSSALNEHMRQHRDNEIMEQSELSDEIFIQGLAL
FT T -> ASSLPNSSGTTTPKFTRMSPMSMGPPTPMPPFSPSPSGSTSHCTNAKIAASPS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020376"
FT VAR_SEQ 1255..1571
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020377"
FT CONFLICT 5
FT /note="E -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="T -> A (in Ref. 1; AAB96922)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="G -> W (in Ref. 2; BAB85589)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="N -> T (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..371
FT /note="KG -> RS (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="E -> V (in Ref. 2; BAB85589)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="E -> R (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..568
FT /note="Missing (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="K -> E (in Ref. 2; BAB85589)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="R -> G (in Ref. 2; BAB85589)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="F -> S (in Ref. 2; BAB85589)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="K -> E (in Ref. 2; BAB85589)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="F -> L (in Ref. 1; AAB96922)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="Y -> C (in Ref. 1; AAB96922)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="G -> A (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="E -> K (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 736..737
FT /note="ND -> MN (in Ref. 2; BAB85589)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="G -> R (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="D -> V (in Ref. 1; AAB96922)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="K -> E (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="E -> Q (in Ref. 5; AAH89344)"
FT /evidence="ECO:0000305"
FT CONFLICT 1123
FT /note="E -> G (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 1171
FT /note="Missing (in Ref. 3; BAC65520)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181
FT /note="D -> Y (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1401
FT /note="N -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1571 AA; 178932 MW; 915E13EF0751C6EE CRC64;
MYHHEDDTNS DMNSDDDMSR SGRETPPPRP SHAFGSERDL ERRGRSRDVE PRDRWPYTRN
PRSRLPQRDL SLPVMSRPHF GLDRDDDRRS MDYESRSQDA ESYQNVVELK EDKKPQNPIQ
DNLENYRKLL SLGVQLAEDD RHSHMTQGHS SRSKRTAYPS TSRGLKPMPE AKKPSHRRGI
CEDESSHGVI MEKFIKDVAR NPKSGRAREL NERPPPRFPR PNDNWKDSSS SRRESVIQER
GYEGSAFRGG FRFNADLASR SRALERKRRY HFDSDERGSG HEHKSCVRKK PFECGAEMRQ
AMSMGNLNSP SFSESQSIDF GANPYVCDEC GRQFSVISEF VEHQIMHTRE NLYEYGESFI
HSVAVNEVQK GQGGGKRFEC KECGETFSRS AALAEHRQIH AREYLAECRD QEDEETIMPS
PTFSELQKMY GKDKFYECKV CKETFLHSSA LIEHQKIHGR GNSDDRDNER ERERDRLRAR
AREQRERERE RERERELGEP FLTCPNFNEF RKMYRKDKIY ECKVCGESFL HLSSLREHQK
IHTRGNPFEN KSRMCEETFV PSQSLRRRQK TYREKLFDFN NARDALMGNS DSSEHQKNRS
RRNFFEGRGF EKPFVESQKS HTITRPPENK DDDKPFTISV NPNDKLKFPI MENGSQGKSY
ERSVIHSLGS AEAQKSHGGL GFSKPRPVAE SSTQSSSSIY YPRAHSGGNT YEGKEYKDSI
IHSLPAPRPL KRHRANDHIQ CDEGGESSIY IPDIINKGRK IPAREDAYEG SSSSNYHTPN
VSRAEPPSLS GESHDSKQDV TFSVPSSSVR EHQKARAKKK YIEPRNNETS VIHSLPFGEL
LAGHRRAKFF ECQECGEAFA RRSELIEHQK IHDRERPSGS RHYERSVIRS LAPSDPQTSY
AQERFIQEQV RKFRAFGQRS TTSNNLSVQK IYAQETFNAE EPHDKETHGQ KIHDKEPYGK
EPSGKEPHGD EPQDKEPLDQ EMRSEEPHDD KPHGQEPHDD KPHGQEPHDD KPHGQEPHGD
EPHGQEPHGD EPHDKEPIDQ EMRSEEPHSE ESHGDEPHGE ESHGQEKVED ATIQASVSEE
HQKDDAGDAI YECQDCGLGF TDLNDLTSHQ DTHSRKALVD SREYAHSEVH AHSVSEFEKK
CSGEKLYECP KCGESFIHSS LLFEHQRVHE QDQLYSVKAC DDAFIALLPV RPRRNCTVER
NPAVSGSAIR CRQCGQGFIH SSALNEHMRQ HRDNEIMEQS ELSDEIFIQG LALTEYQGSE
TEEKLFECTI CGECFFTAKQ LGDHHTKVHK DEPYEYGPSY THASFLTEPL RKHIPLYECK
DCGQSFLDDT VIAERMVFHP EREGGSEIVA ATAQEVEANV LIPQEVLRIQ GSNAEAAEPE
VEAAEPEVEA AEPEVEAAEP NGEAEGPDGE AAEPDGEAEQ PNGEAEQPNG DADEPDGAGI
EDPEERADEP EEDVEEPEGD ADEPDGADIE DPEEEGEDQE IEVEEPYYNC HECAETFASS
SAFGEHLKSH ASVIIFEPAN APGECSGYIE RASTSAGGAE QADDKYFKCD VCGQLFNDRL
SLARHQNSHT G
