PO2F1_MOUSE
ID PO2F1_MOUSE Reviewed; 770 AA.
AC P25425; Q61994; Q63891; Q6Y681; Q7TSD0; Q8BT04; Q8K570; Q99JH0; Q9WTZ4;
AC Q9WTZ5; Q9WTZ6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=POU domain, class 2, transcription factor 1;
DE AltName: Full=NF-A1;
DE AltName: Full=Octamer-binding protein 1;
DE Short=Oct-1;
DE AltName: Full=Octamer-binding transcription factor 1;
DE Short=OTF-1;
GN Name=Pou2f1; Synonyms=Oct-1, Otf-1, Otf1;
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] (ISOFORMS 1; 2 AND 3).
RX PubMed=8441632; DOI=10.1093/nar/21.2.245;
RA Suzuki N., Peter W., Ciesiolka T., Gruss P., Schoeler H.R.;
RT "Mouse Oct-1 contains a composite homeodomain of human Oct-1 and Oct-2.";
RL Nucleic Acids Res. 21:245-252(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=1561098; DOI=10.1093/nar/20.6.1419;
RA Stepchenko A.G.;
RT "The nucleotide sequence of mouse OCT-1 cDNA.";
RL Nucleic Acids Res. 20:1419-1419(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND TISSUE SPECIFICITY.
RX PubMed=11683265; DOI=10.1007/s004380100549;
RA Pankratova E.V., Deyev I.E., Zhenilo S.V., Polanovsky O.L.;
RT "Tissue-specific isoforms of the ubiquitous transcription factor Oct-1.";
RL Mol. Genet. Genomics 266:239-245(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C3H/HeN; TISSUE=Mammary gland;
RX PubMed=12151092; DOI=10.1016/s0167-4781(02)00402-5;
RA Zhao F.-Q., Adachi K., Oka T.;
RT "Involvement of Oct-1 in transcriptional regulation of beta-casein gene
RT expression in mouse mammary gland.";
RL Biochim. Biophys. Acta 1577:27-37(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=14729276; DOI=10.1016/j.gene.2003.10.023;
RA Zhao F.-Q., Zheng Y., Dong B., Oka T.;
RT "Cloning, genomic organization, expression, and effect on beta-casein
RT promoter activity of a novel isoform of the mouse Oct-1 transcription
RT factor.";
RL Gene 326:175-187(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11).
RC STRAIN=BALB/cJ; TISSUE=Myeloma;
RA Deyev I.E., Zhenilo S.V., Pankratova E.V., Polanovsky O.L.;
RT "Novel isoforms of mRNA of gene oct-1.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-770.
RX PubMed=8376772;
RA Lerner A., D'Adamio L., Diener A.C., Clayton L.K., Reinherz E.L.;
RT "CD3 zeta/eta/theta locus is colinear with and transcribed antisense to the
RT gene encoding the transcription factor Oct-1.";
RL J. Immunol. 151:3152-3162(1993).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-770 (ISOFORMS 2 AND 6), AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6 X DBA/20; TISSUE=Lymphoid tissue;
RX PubMed=7711063; DOI=10.1016/0167-4781(94)00246-y;
RA Jaffe J., Hochberg M., Riss J., Hasin T., Reich L., Laskov R.;
RT "Cloning, sequencing and expression of two isoforms of the murine oct-1
RT transcription factor.";
RL Biochim. Biophys. Acta 1261:201-209(1995).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 305-426.
RC TISSUE=Testis;
RX PubMed=1970171; DOI=10.1093/nar/18.6.1634;
RA Goldsborough A., Ashworth A., Willison K.R.;
RT "Cloning and sequencing of POU-boxes expressed in mouse testis.";
RL Nucleic Acids Res. 18:1634-1634(1990).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 669-770 (ISOFORMS 7; 8 AND 9), AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=10023087; DOI=10.1016/s0167-4781(98)00280-2;
RA Riss J., Laskov R.;
RT "Expression of novel alternatively spliced isoforms of the oct-1
RT transcription factor.";
RL Biochim. Biophys. Acta 1444:295-298(1999).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Spleen;
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).
CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'-
CC ATTTGCAT-3') and activates the promoters of the genes for some small
CC nuclear RNAs (snRNA) and of genes such as those for histone H2B and
CC immunoglobulins. Modulates transcription transactivation by NR3C1, AR
CC and PGR. {ECO:0000250|UniProtKB:P14859}.
CC -!- SUBUNIT: Interacts with POU2AF1; the interaction increases POU2F1
CC transactivation activity. Interacts with NR3C1, AR, PGR and HCFC1.
CC {ECO:0000250|UniProtKB:P14859}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=1; Synonyms=OCT-1A;
CC IsoId=P25425-1; Sequence=Displayed;
CC Name=2; Synonyms=OCT-1B;
CC IsoId=P25425-2; Sequence=VSP_002321;
CC Name=3; Synonyms=OCT-1C;
CC IsoId=P25425-3; Sequence=VSP_002321, VSP_002322, VSP_002323;
CC Name=4; Synonyms=OCT-1R;
CC IsoId=P25425-4; Sequence=VSP_007271, VSP_007272, VSP_002321,
CC VSP_007273;
CC Name=5; Synonyms=OCT-1L;
CC IsoId=P25425-5; Sequence=VSP_007271, VSP_002321;
CC Name=6;
CC IsoId=P25425-6; Sequence=VSP_007278;
CC Name=7;
CC IsoId=P25425-7; Sequence=VSP_007276, VSP_007277;
CC Name=8;
CC IsoId=P25425-8; Sequence=VSP_007278, VSP_002322, VSP_002323;
CC Name=9;
CC IsoId=P25425-9; Sequence=VSP_007274, VSP_007275;
CC Name=10; Synonyms=OCT-1Z;
CC IsoId=P25425-10; Sequence=VSP_013404, VSP_013405;
CC Name=11;
CC IsoId=P25425-11; Sequence=VSP_007271, VSP_007273;
CC Name=12;
CC IsoId=P25425-12; Sequence=VSP_013403;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. However, isoforms 4 and 5
CC are only expressed in lymphocytes. {ECO:0000269|PubMed:10023087,
CC ECO:0000269|PubMed:11683265, ECO:0000269|PubMed:14729276,
CC ECO:0000269|PubMed:7711063}.
CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2
CC subfamily. {ECO:0000305}.
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DR EMBL; X68362; CAA48422.1; -; mRNA.
DR EMBL; X68363; CAA48423.1; -; mRNA.
DR EMBL; X68364; CAA48424.1; -; mRNA.
DR EMBL; X56230; CAA39679.1; -; mRNA.
DR EMBL; AJ296212; CAC34943.1; -; mRNA.
DR EMBL; AF508939; AAM34281.1; -; mRNA.
DR EMBL; AY177625; AAO45298.1; -; mRNA.
DR EMBL; AJ489474; CAD35743.1; -; mRNA.
DR EMBL; AK028237; BAC25832.1; -; mRNA.
DR EMBL; S65461; AAB28234.1; -; mRNA.
DR EMBL; X70324; CAA49791.1; -; mRNA.
DR EMBL; X70325; CAA49792.1; -; mRNA.
DR EMBL; X51958; CAA36217.1; -; mRNA.
DR EMBL; AF095458; AAD25325.1; -; mRNA.
DR EMBL; AF095459; AAD25326.1; -; mRNA.
DR EMBL; AF095460; AAD25327.1; -; mRNA.
DR CCDS; CCDS15444.1; -. [P25425-5]
DR PIR; I56187; I56187.
DR PIR; S30293; S30293.
DR RefSeq; NP_035267.2; NM_011137.3.
DR RefSeq; NP_945151.2; NM_198933.3. [P25425-5]
DR RefSeq; XP_006496767.1; XM_006496704.2. [P25425-1]
DR RefSeq; XP_011237069.1; XM_011238767.2. [P25425-1]
DR RefSeq; XP_011237071.1; XM_011238769.2.
DR RefSeq; XP_017174849.1; XM_017319360.1. [P25425-2]
DR AlphaFoldDB; P25425; -.
DR SMR; P25425; -.
DR BioGRID; 202301; 16.
DR IntAct; P25425; 7.
DR STRING; 10090.ENSMUSP00000107056; -.
DR iPTMnet; P25425; -.
DR PhosphoSitePlus; P25425; -.
DR jPOST; P25425; -.
DR MaxQB; P25425; -.
DR PaxDb; P25425; -.
DR PeptideAtlas; P25425; -.
DR PRIDE; P25425; -.
DR ProteomicsDB; 289847; -. [P25425-1]
DR ProteomicsDB; 289848; -. [P25425-2]
DR ProteomicsDB; 289849; -. [P25425-3]
DR ProteomicsDB; 289850; -. [P25425-4]
DR ProteomicsDB; 289851; -. [P25425-5]
DR ProteomicsDB; 289852; -. [P25425-6]
DR ProteomicsDB; 289853; -. [P25425-7]
DR ProteomicsDB; 289854; -. [P25425-8]
DR ProteomicsDB; 289855; -. [P25425-9]
DR ProteomicsDB; 289856; -. [P25425-10]
DR ProteomicsDB; 289857; -. [P25425-11]
DR ProteomicsDB; 289858; -. [P25425-12]
DR Antibodypedia; 3616; 662 antibodies from 45 providers.
DR DNASU; 18986; -.
DR Ensembl; ENSMUST00000069609; ENSMUSP00000064000; ENSMUSG00000026565. [P25425-5]
DR Ensembl; ENSMUST00000111429; ENSMUSP00000107057; ENSMUSG00000026565. [P25425-2]
DR Ensembl; ENSMUST00000184643; ENSMUSP00000138962; ENSMUSG00000026565. [P25425-3]
DR GeneID; 18986; -.
DR KEGG; mmu:18986; -.
DR UCSC; uc007djv.1; mouse. [P25425-6]
DR UCSC; uc007djx.2; mouse. [P25425-5]
DR UCSC; uc007dkb.2; mouse. [P25425-4]
DR UCSC; uc007dkc.2; mouse. [P25425-11]
DR UCSC; uc007dke.1; mouse. [P25425-10]
DR CTD; 5451; -.
DR MGI; MGI:101898; Pou2f1.
DR VEuPathDB; HostDB:ENSMUSG00000026565; -.
DR eggNOG; KOG3802; Eukaryota.
DR GeneTree; ENSGT00940000157831; -.
DR HOGENOM; CLU_013065_4_0_1; -.
DR InParanoid; P25425; -.
DR OrthoDB; 873012at2759; -.
DR PhylomeDB; P25425; -.
DR TreeFam; TF316413; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 18986; 6 hits in 77 CRISPR screens.
DR ChiTaRS; Pou2f1; mouse.
DR PRO; PR:P25425; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P25425; protein.
DR Bgee; ENSMUSG00000026565; Expressed in rostral migratory stream and 254 other tissues.
DR ExpressionAtlas; P25425; baseline and differential.
DR Genevisible; P25425; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0060235; P:lens induction in camera-type eye; IGI:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030910; P:olfactory placode formation; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR045703; POU2F1_C.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR000972; TF_octamer.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR Pfam; PF19536; POU2F1_C; 2.
DR PRINTS; PR00029; OCTAMER.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Homeobox; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..770
FT /note="POU domain, class 2, transcription factor 1"
FT /id="PRO_0000100708"
FT DOMAIN 281..355
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 382..441
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14859"
FT VAR_SEQ 1
FT /note="M -> MADGGAASQDESSAAAAAAADSR (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013403"
FT VAR_SEQ 1
FT /note="M -> MLDCSDCVLDSRM (in isoform 4, isoform 5 and
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:11683265,
FT ECO:0000303|PubMed:1561098, ECO:0000303|Ref.6"
FT /id="VSP_007271"
FT VAR_SEQ 54..71
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:1561098"
FT /id="VSP_007272"
FT VAR_SEQ 499..522
FT /note="DQDLRRGCSWEVLRSLPDRVTTTA -> GKQQPAYRLVSTVPVRFLWRTARS
FT (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14729276"
FT /id="VSP_013404"
FT VAR_SEQ 499..522
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:11683265,
FT ECO:0000303|PubMed:12151092, ECO:0000303|PubMed:1561098,
FT ECO:0000303|PubMed:7711063, ECO:0000303|PubMed:8441632"
FT /id="VSP_002321"
FT VAR_SEQ 523..770
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14729276"
FT /id="VSP_013405"
FT VAR_SEQ 639..770
FT /note="Missing (in isoform 4 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:1561098, ECO:0000303|Ref.6"
FT /id="VSP_007273"
FT VAR_SEQ 639..647
FT /note="GALLSLSPG -> IASWIGELS (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:10023087"
FT /id="VSP_007274"
FT VAR_SEQ 639..641
FT /note="GAL -> SCF (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:10023087"
FT /id="VSP_007276"
FT VAR_SEQ 642..770
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:10023087"
FT /id="VSP_007277"
FT VAR_SEQ 648..770
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:10023087"
FT /id="VSP_007275"
FT VAR_SEQ 668..691
FT /note="Missing (in isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10023087,
FT ECO:0000303|PubMed:7711063"
FT /id="VSP_007278"
FT VAR_SEQ 717..725
FT /note="VSLVSAAAA -> DCFMDWRTF (in isoform 3 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10023087,
FT ECO:0000303|PubMed:8441632"
FT /id="VSP_002322"
FT VAR_SEQ 726..770
FT /note="Missing (in isoform 3 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10023087,
FT ECO:0000303|PubMed:8441632"
FT /id="VSP_002323"
FT CONFLICT 43
FT /note="Q -> L (in Ref. 2; CAA39679)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="V -> I (in Ref. 3; CAC34943)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="A -> P (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> C (in Ref. 6; CAD35743)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="L -> H (in Ref. 3; CAC34943)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="Q -> R (in Ref. 3; CAC34943)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="L -> W (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="D -> G (in Ref. 3; CAC34943)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="A -> D (in Ref. 10)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="N -> D (in Ref. 3; CAC34943)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="S -> G (in Ref. 3; CAC34943)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="G -> D (in Ref. 3; CAC34943)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="A -> G (in Ref. 1; CAA48422/CAA48423/CAA48424)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="Q -> R (in Ref. 3; CAC34943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 770 AA; 79547 MW; B45CDBE632853FE9 CRC64;
MNNPSETNKS SMESEDASTG TQTNGLDFQK QPVPVGGAIS TAQAQAFLGH LHQVQLAGTS
LQAAAQSLNV QSKSSEESGD SQQSSQPSSQ PPSVQSAIPQ TQLMLAGGQI TGLTLTPAQQ
QLLLQQAQAQ AQLLAAAVQQ HSASQQHSAA GATISASAAT PMTQIPLSQP IQIAQDLQQL
QQLQQQNLNL QQFVLVHPTT NLQPAQFIIS QTPQGQQGLL QAQNLLTQLP QQSQANLLQP
QPSITLTSQP TTPTRTIAAA SVQTLPQSQS TPKRIDTPSL EEPSDLEELE QFAKTFKQRR
IKLGFTQGDV GLAMGKLYGN DFSQTTISRF EALNLSFKNM CKLKPLLEKW LNDAENLSSD
STASSPSALN SPGLGAEGLN RRRKKRTSIE TNIRVALEKS FMENQKPTSE DITLIAEQLN
MEKEVIRVWF CNRRQKEKRI NPPSSGGTSS SPIKAIFPSP ASLVATTPSL VTSSTATTLT
VNPVLPLTSA AVTNLSLTDQ DLRRGCSWEV LRSLPDRVTT TAGTTDSTSN NNTATVISTA
PPASSAVTSP SLSPSPSASA STSEASSASE TNTTQTTSTP LPSPLGASQV MVTTPGLQTA
AAALQGAAQL PANASLAAMA AAAGLSPGLM APSQFAAGGA LLSLSPGTLG SALSPALMSN
STLATIQALA SSGSLPITSL DATGNLVFAN AGGAPNIVTA PLFLNPQNLS LLTSNPVSLV
SAAAASTGNS APTASLHASS TSTESIQSSL FTVASASGPA STTTAASKAQ
