GenomeNet

Database: UniProt
Entry: Q60636
LinkDB: Q60636
Original site: Q60636 
ID   PRDM1_MOUSE             Reviewed;         856 AA.
AC   Q60636; A2VDE8; Q3UET9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-FEB-2019, entry version 163.
DE   RecName: Full=PR domain zinc finger protein 1;
DE            EC=2.1.1.-;
DE   AltName: Full=B lymphocyte-induced maturation protein 1;
DE            Short=Blimp-1;
DE   AltName: Full=Beta-interferon gene positive regulatory domain I-binding factor;
DE   AltName: Full=PR domain-containing protein 1;
GN   Name=Prdm1; Synonyms=Blimp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=B-cell;
RX   PubMed=8168136; DOI=10.1016/0092-8674(94)90321-2;
RA   Turner C.A., Mack D.H., Davis M.M.;
RT   "Blimp-1, a novel zinc finger-containing protein that can drive the
RT   maturation of B lymphocytes into immunoglobulin-secreting cells.";
RL   Cell 77:297-306(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1
RP   AND 5), AND TISSUE SPECIFICITY.
RC   STRAIN=129;
RX   PubMed=11121475; DOI=10.1093/nar/28.24.4846;
RA   Tunyaplin C., Shapiro M.A., Calame K.L.;
RT   "Characterization of the B lymphocyte-induced maturation protein-1
RT   (Blimp-1) gene, mRNA isoforms and basal promoter.";
RL   Nucleic Acids Res. 28:4846-4855(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 1-253 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Retina;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH PRMT5.
RX   PubMed=16699504; DOI=10.1038/ncb1413;
RA   Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,
RA   Kouzarides T., Surani M.A.;
RT   "Blimp1 associates with Prmt5 and directs histone arginine methylation
RT   in mouse germ cells.";
RL   Nat. Cell Biol. 8:623-630(2006).
RN   [6]
RP   ALTERNATIVE PROMOTER USAGE (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING
RP   (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   TISSUE=Embryo, Placenta, and Yolk sac;
RX   PubMed=19737919; DOI=10.1128/MCB.00670-09;
RA   Morgan M.A., Magnusdottir E., Kuo T.C., Tunyaplin C., Harper J.,
RA   Arnold S.J., Calame K., Robertson E.J., Bikoff E.K.;
RT   "Blimp-1/Prdm1 alternative promoter usage during mouse development and
RT   plasma cell differentiation.";
RL   Mol. Cell. Biol. 29:5813-5827(2009).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN LYMPHOCYTE T
RP   CELLS, TISSUE SPECIFICITY, AND INDUCTION (MICROBIAL INFECTION).
RX   PubMed=27102484; DOI=10.1126/science.aad2035;
RA   Mackay L.K., Minnich M., Kragten N.A., Liao Y., Nota B., Seillet C.,
RA   Zaid A., Man K., Preston S., Freestone D., Braun A., Wynne-Jones E.,
RA   Behr F.M., Stark R., Pellicci D.G., Godfrey D.I., Belz G.T.,
RA   Pellegrini M., Gebhardt T., Busslinger M., Shi W., Carbone F.R.,
RA   van Lier R.A., Kallies A., van Gisbergen K.P.;
RT   "Hobit and Blimp1 instruct a universal transcriptional program of
RT   tissue residency in lymphocytes.";
RL   Science 352:459-463(2016).
CC   -!- FUNCTION: Transcription factor that mediates a transcriptional
CC       program in various innate and adaptive immune tissue-resident
CC       lymphocyte T cell types such as tissue-resident memory T (Trm),
CC       natural killer (trNK) and natural killer T (NKT) cells and
CC       negatively regulates gene expression of proteins that promote the
CC       egress of tissue-resident T-cell populations from non-lymphoid
CC       organs (PubMed:27102484). Plays a role in the development,
CC       retention and long-term establishment of adaptive and innate
CC       tissue-resident lymphocyte T cell types in non-lymphoid organs,
CC       such as the skin and gut, but also in other nonbarrier tissues
CC       like liver and kidney, and therefore may provide immediate
CC       immunological protection against reactivating infections or viral
CC       reinfection (PubMed:27102484). Binds specifically to the PRDI
CC       element in the promoter of the beta-interferon gene (By
CC       similarity). Drives the maturation of B-lymphocytes into Ig
CC       secreting cells (By similarity). Associates with the
CC       transcriptional repressor ZNF683 to chromatin at gene promoter
CC       regions (PubMed:27102484). {ECO:0000250|UniProtKB:O75626,
CC       ECO:0000269|PubMed:27102484}.
CC   -!- SUBUNIT: Interacts with PRMT5 (PubMed:16699504). Interacts with
CC       FBXO10 (By similarity). Interacts with FBXO11 (By similarity).
CC       {ECO:0000250|UniProtKB:O75626, ECO:0000269|PubMed:16699504}.
CC   -!- INTERACTION:
CC       P63165:SUMO1 (xeno); NbExp=3; IntAct=EBI-7000804, EBI-80140;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8168136}.
CC       Cytoplasm {ECO:0000250|UniProtKB:O75626}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q60636-1; Sequence=Displayed;
CC         Note=Produced by alternative splicing.;
CC       Name=2; Synonyms=1A;
CC         IsoId=Q60636-2; Sequence=VSP_039189;
CC         Note=Produced by alternative splicing of isoform 1.;
CC       Name=3; Synonyms=1B;
CC         IsoId=Q60636-3; Sequence=VSP_041570;
CC         Note=Produced by alternative promoter usage of isoform 2.;
CC       Name=4; Synonyms=1C;
CC         IsoId=Q60636-4; Sequence=VSP_041571;
CC         Note=Produced by alternative promoter usage of isoform 2.;
CC       Name=5; Synonyms=delta exon 7;
CC         IsoId=Q60636-5; Sequence=VSP_041572;
CC         Note=Produced by alternative splicing of isoform 1. Does not
CC         bind DNA.;
CC   -!- TISSUE SPECIFICITY: Expressed in innate lymphocytes, including
CC       tissue-resident conventional natural killer (cNK) cells in liver
CC       (PubMed:27102484). Expressed also weakly in tissue-resident
CC       natural killer (trNK) and natural killer T (NKT) cells in liver
CC       (PubMed:27102484). Isoform 1 is detected in bone marrow, spleen
CC       and lymph node but not in brain, heart, kidney, liver, ovary or
CC       muscle. Weak expression detected in the lung. Isoform 3 is
CC       detected only in yolk sac. Isoform 4 is detected in embryo, yolk
CC       sac, placenta, splenocytes, and activated T-cells.
CC       {ECO:0000269|PubMed:11121475, ECO:0000269|PubMed:19737919,
CC       ECO:0000269|PubMed:27102484, ECO:0000269|PubMed:8168136}.
CC   -!- INDUCTION: By lymphokines, specifically IL-2 and IL-5. Up-
CC       regulated during dendritic cell maturation.
CC   -!- INDUCTION: (Microbial infection) Up-regulated in response to
CC       Herpes simplex virus (HSV) infection in skin and spleen memory
CC       CD8(+) T cells. {ECO:0000269|PubMed:27102484}.
CC   -!- INDUCTION: (Microbial infection) Up-regulated in response to
CC       Lymphocytic choriomeningitis virus (LCMV) in memory CD8(+) T
CC       cells. {ECO:0000269|PubMed:27102484}.
CC   -!- PTM: Sumoylation at Lys-847 by PIAS1 augments transcriptional
CC       repressor activity, and is critical for plasma cell
CC       differentiation. {ECO:0000250|UniProtKB:O75626}.
CC   -!- PTM: Ubiquitinated by SCF(FBXO11), leading to its degradation by
CC       the proteasome. {ECO:0000250|UniProtKB:O75626}.
CC   -!- DISRUPTION PHENOTYPE: Early embryonic lethality (PubMed:19737919).
CC       Compound heterozygotes display germ cell defects and a rudimentary
CC       or missing fifth digit of the forelimb (PubMed:19737919).
CC       Conditional knockout in lymphocyte T cells show a weak reduction
CC       in tissue-resident memory T (Trm) cell population maintenance in
CC       the skin, gut, liver and kidney but not of splenic T cells
CC       (PubMed:27102484). Double knockouts for PRDM1/BLIMP1 and ZNF683
CC       result in a strong inhibition of Trm cell population maintenance
CC       but not of circulating memory cells (PubMed:27102484). Display an
CC       enhancement of natural killer T (NKT) cells migration
CC       preferentially to the white pulp of the spleen in response to
CC       chemotactic stimuli (PubMed:27102484).
CC       {ECO:0000269|PubMed:19737919, ECO:0000269|PubMed:27102484}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI29802.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; U08185; AAA19252.1; -; mRNA.
DR   EMBL; AF305539; AAG42212.1; -; Genomic_DNA.
DR   EMBL; AF305534; AAG42212.1; JOINED; Genomic_DNA.
DR   EMBL; AF305535; AAG42212.1; JOINED; Genomic_DNA.
DR   EMBL; AF305536; AAG42212.1; JOINED; Genomic_DNA.
DR   EMBL; AF305537; AAG42212.1; JOINED; Genomic_DNA.
DR   EMBL; AF305538; AAG42212.1; JOINED; Genomic_DNA.
DR   EMBL; AK077622; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK149344; BAE28822.1; -; mRNA.
DR   EMBL; BC129801; AAI29802.1; ALT_INIT; mRNA.
DR   CCDS; CCDS23825.2; -. [Q60636-2]
DR   PIR; A53503; A53503.
DR   RefSeq; NP_031574.2; NM_007548.4. [Q60636-2]
DR   RefSeq; XP_006512565.1; XM_006512502.3. [Q60636-4]
DR   RefSeq; XP_006512566.1; XM_006512503.2. [Q60636-3]
DR   RefSeq; XP_006512568.1; XM_006512505.2. [Q60636-1]
DR   RefSeq; XP_011241411.1; XM_011243109.1. [Q60636-3]
DR   UniGene; Mm.4800; -.
DR   ProteinModelPortal; Q60636; -.
DR   SMR; Q60636; -.
DR   BioGrid; 198355; 9.
DR   IntAct; Q60636; 1.
DR   MINT; Q60636; -.
DR   STRING; 10090.ENSMUSP00000101129; -.
DR   iPTMnet; Q60636; -.
DR   PhosphoSitePlus; Q60636; -.
DR   PaxDb; Q60636; -.
DR   PeptideAtlas; Q60636; -.
DR   PRIDE; Q60636; -.
DR   DNASU; 12142; -.
DR   Ensembl; ENSMUST00000039174; ENSMUSP00000039248; ENSMUSG00000038151. [Q60636-1]
DR   Ensembl; ENSMUST00000105490; ENSMUSP00000101129; ENSMUSG00000038151. [Q60636-2]
DR   Ensembl; ENSMUST00000218369; ENSMUSP00000151237; ENSMUSG00000038151. [Q60636-4]
DR   GeneID; 12142; -.
DR   KEGG; mmu:12142; -.
DR   UCSC; uc007ezu.3; mouse. [Q60636-1]
DR   UCSC; uc007ezv.3; mouse. [Q60636-2]
DR   CTD; 639; -.
DR   MGI; MGI:99655; Prdm1.
DR   eggNOG; KOG2461; Eukaryota.
DR   eggNOG; ENOG410ZFVU; LUCA.
DR   GeneTree; ENSGT00940000154798; -.
DR   HOGENOM; HOG000059670; -.
DR   HOVERGEN; HBG053670; -.
DR   InParanoid; Q60636; -.
DR   OMA; HCHKSYI; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q60636; -.
DR   TreeFam; TF316545; -.
DR   PRO; PR:Q60636; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   Bgee; ENSMUSG00000038151; Expressed in 205 organ(s), highest expression level in testis.
DR   Genevisible; Q60636; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0042826; F:histone deacetylase binding; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0035904; P:aorta development; IMP:MGI.
DR   GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR   GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR   GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR   GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR   GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR   GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR   GO; GO:0007281; P:germ cell development; IGI:MGI.
DR   GO; GO:0003170; P:heart valve development; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0060576; P:intestinal epithelial cell development; IMP:MGI.
DR   GO; GO:0001893; P:maternal placenta development; IMP:MGI.
DR   GO; GO:0001763; P:morphogenesis of a branching structure; IMP:MGI.
DR   GO; GO:0030889; P:negative regulation of B cell proliferation; IDA:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; IDA:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0033082; P:regulation of extrathymic T cell differentiation; IMP:UniProtKB.
DR   GO; GO:0032823; P:regulation of natural killer cell differentiation; IMP:UniProtKB.
DR   GO; GO:0051136; P:regulation of NK T cell differentiation; IMP:UniProtKB.
DR   GO; GO:1990654; P:sebum secreting cell proliferation; IDA:MGI.
DR   GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
DR   GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Alternative promoter usage; Alternative splicing;
KW   Complete proteome; Cytoplasm; Developmental protein; DNA-binding;
KW   Immunity; Innate immunity; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    856       PR domain zinc finger protein 1.
FT                                /FTId=PRO_0000047758.
FT   DOMAIN      115    233       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     606    628       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     634    656       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     662    684       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     690    712       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      558    605       Interaction with PIAS1. {ECO:0000250}.
FT   COMPBIAS    351    394       Glu/Pro/Ser/Thr-rich.
FT   CROSSLNK    847    847       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:O75626}.
FT   CROSSLNK    847    847       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:O75626}.
FT   VAR_SEQ       1     67       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_041570.
FT   VAR_SEQ       1     47       MREAYLRCWIFSWKNVWVRPCQRLHFKTVLLQGSLLYTALD
FT                                SYSTVQ -> MLDLLLEKRVGTTL (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_039189.
FT   VAR_SEQ       1     47       MREAYLRCWIFSWKNVWVRPCQRLHFKTVLLQGSLLYTALD
FT                                SYSTVQ -> MTPGVPGHRTQQRPQHISALSDKAKDCSK
FT                                (in isoform 4). {ECO:0000305}.
FT                                /FTId=VSP_041571.
FT   VAR_SEQ     624    666       Missing (in isoform 5). {ECO:0000305}.
FT                                /FTId=VSP_041572.
FT   CONFLICT    155    155       N -> K (in Ref. 4; AAI29802).
FT                                {ECO:0000305}.
FT   CONFLICT    205    205       L -> M (in Ref. 3; AK077622).
FT                                {ECO:0000305}.
SQ   SEQUENCE   856 AA;  95836 MW;  B9AC6FC2E29ECF4A CRC64;
     MREAYLRCWI FSWKNVWVRP CQRLHFKTVL LQGSLLYTAL DSYSTVQAAP KSSSGSVKFQ
     GLAETGIMKM DMEDADMTLW TEAEFEEKCT YIVNDHPWDS GADGGTSVQA EASLPRNLLF
     KYAANNSKEV IGVVSKEYIP KGTRFGPLIG EVYTNDTVPK NANRKYFWRI YSREEFHHFI
     DGFNEEKSNW MRYVNPAHSA REQNLAACQN GMNIYFYTIK PIPANQELLV WYCRDFAERL
     HYPYPGELTV INLTQTESNP KQYSSEKNEL YPKSVPKREY SVKEILKLDS NPSKRKDIYR
     SNISPFTLEK DMDGFRKNGS PDMPFYPRVV YPIRAPLPED FLKASLAYGM ERPTYITHSP
     LPSSTTPSPP ASSSPEQSLK SSSPHSSPGN TVSPLAPGLP EHRDSYSYLN VSYGSEGLGS
     YPGYAPAPHL PPAFIPSYNA HYPKFLLPPY GISSNGLSTM NNINGINNFS LFPRLYPVYS
     NLLSGSSLPH PMLNPASLPS SLPTDGARRL LPPEHPKEVL IPAPHSAFSL TGAAASMKDE
     SSPPSGSPTA GTAATSEHVV QPKATSSVMA APSTDGAMNL IKNKRNMTGY KTLPYPLKKQ
     NGKIKYECNV CAKTFGQLSN LKVHLRVHSG ERPFKCQTCN KGFTQLAHLQ KHYLVHTGEK
     PHECQVCHKR FSSTSNLKTH LRLHSGEKPY QCKVCPAKFT QFVHLKLHKR LHTRERPHKC
     AQCHKSYIHL CSLKVHLKGN CPAGPAAGLP LEDLTRINEE IERFDISDNA DRLEDMEDSV
     DVTSMVEKEI LAVVRKEKEE TSLKVSLQRN MGNGLLSSGC SLYESSDLSL MKLPHSNPLP
     LVPVKVKQET VEPMDP
//
DBGET integrated database retrieval system