MAZ_HUMAN
ID MAZ_HUMAN Reviewed; 477 AA.
AC P56270; A8QJL9; C6G496; G5E927; H3BQD6; Q15703; Q8NFN7; Q99443;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Myc-associated zinc finger protein;
DE Short=MAZI;
DE AltName: Full=Pur-1;
DE AltName: Full=Purine-binding transcription factor;
DE AltName: Full=Serum amyloid A-activating factor-1;
DE Short=SAF-1;
DE AltName: Full=Transcription factor Zif87;
DE AltName: Full=ZF87;
DE AltName: Full=Zinc finger protein 801;
GN Name=MAZ; Synonyms=ZNF801;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=1502157; DOI=10.1073/pnas.89.16.7452;
RA Bossone S.A., Asselin C., Patel A.J., Marcu K.B.;
RT "MAZ, a zinc finger protein, binds to c-MYC and C2 gene sequences
RT regulating transcriptional initiation and termination.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:7452-7456(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Carcinoma;
RX PubMed=1567856; DOI=10.1021/bi00131a029;
RA Pyrc J.J., Moberg K.H., Hall D.J.;
RT "Isolation of a novel cDNA encoding a zinc-finger protein that binds to two
RT sites within the c-myc promoter.";
RL Biochemistry 31:4102-4110(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=8831693; DOI=10.1006/bbrc.1996.1432;
RA Tsutsui H., Sakatsume O., Itakura K., Yokoyama K.K.;
RT "Members of the MAZ family: a novel cDNA clone for MAZ from human
RT pancreatic islet cells.";
RL Biochem. Biophys. Res. Commun. 226:801-809(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8626793; DOI=10.1074/jbc.271.8.4417;
RA Parks C.L., Shenk T.;
RT "The serotonin 1a receptor gene contains a TATA-less promoter that responds
RT to MAZ and Sp1.";
RL J. Biol. Chem. 271:4417-4430(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lymphoblastoma;
RX PubMed=9685418; DOI=10.1074/jbc.273.32.20603;
RA Song J., Murakami H., Tsutsui H., Tang X., Matsumura M., Itakura K.,
RA Kanazawa I., Sun K., Yokoyama K.K.;
RT "Genomic organization and expression of a human gene for Myc-associated
RT zinc finger protein (MAZ).";
RL J. Biol. Chem. 273:20603-20614(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, FUNCTION, AND
RP SUBUNIT.
RX PubMed=12270922; DOI=10.1074/jbc.m206299200;
RA Ray B.K., Murphy R., Ray P., Ray A.;
RT "SAF-2, a splice variant of SAF-1, acts as a negative regulator of
RT transcription.";
RL J. Biol. Chem. 277:46822-46830(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bae J.S., Kim S.H., Park H.S.;
RT "Human Myc-associated zinc finger protein (MAZ).";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION BY CYTOKINES AND GROWTH FACTORS.
RX PubMed=19583771; DOI=10.1111/j.1742-4658.2009.07136.x;
RA Ray A., Dhar S., Shakya A., Ray P., Okada Y., Ray B.K.;
RT "SAF-3, a novel splice variant of the SAF-1/MAZ/Pur-1 family, is expressed
RT during inflammation.";
RL FEBS J. 276:4276-4286(2009).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP INTERACTION WITH BPTF, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10727212; DOI=10.1021/bi992211q;
RA Jordan-Sciutto K.L., Dragich J.M., Caltagarone J., Hall D.J., Bowser R.;
RT "Fetal Alz-50 clone 1 (FAC1) protein interacts with the Myc-associated zinc
RT finger protein (ZF87/MAZ) and alters its transcriptional activity.";
RL Biochemistry 39:3206-3215(2000).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Transcriptional regulator, potentially with dual roles in
CC transcription initiation and termination. {ECO:0000303|PubMed:1502157}.
CC -!- FUNCTION: [Isoform 1]: Binds DNA and functions as a transcriptional
CC activator (PubMed:12270922). Binds to two G/A-rich sites, ME1a1 and
CC ME1a2, within the MYC promoter having greater affinity for the former
CC (PubMed:1502157). Also binds to multiple G/C-rich sites within the
CC promoter of the Sp1 family of transcription factors (PubMed:1502157).
CC {ECO:0000269|PubMed:12270922, ECO:0000269|PubMed:1502157}.
CC -!- FUNCTION: [Isoform 2]: Binds DNA and functions as a transcriptional
CC activator (PubMed:12270922). Inhibits MAZ isoform 1-mediated
CC transcription (PubMed:12270922). {ECO:0000269|PubMed:12270922}.
CC -!- FUNCTION: [Isoform 3]: Binds DNA and functions as a transcriptional
CC activator. {ECO:0000269|PubMed:19583771}.
CC -!- SUBUNIT: Interacts with BPTF. {ECO:0000269|PubMed:10727212}.
CC -!- SUBUNIT: [Isoform 1]: Forms a heterodimer with MAZ isoform 2; the
CC interaction inhibits MAZ isoform 1-mediated transcription activation.
CC {ECO:0000269|PubMed:12270922}.
CC -!- SUBUNIT: [Isoform 2]: Forms a heterodimer with MAZ isoform 1; the
CC interaction inhibits MAZ isoform 1-mediated transcription activation.
CC {ECO:0000269|PubMed:12270922}.
CC -!- INTERACTION:
CC P56270; P43146: DCC; NbExp=4; IntAct=EBI-1809742, EBI-1222919;
CC P56270; P70211: Dcc; Xeno; NbExp=2; IntAct=EBI-1809742, EBI-1798863;
CC P56270; Q91562: dcc.L; Xeno; NbExp=2; IntAct=EBI-1809742, EBI-1809954;
CC P56270-2; P42858: HTT; NbExp=3; IntAct=EBI-12068586, EBI-466029;
CC P56270-2; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-12068586, EBI-10172052;
CC P56270-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12068586, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:10727212}. Note=In
CC brains of Alzheimer disease patients, present in a plaque-like
CC structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=SAF-1;
CC IsoId=P56270-1; Sequence=Displayed;
CC Name=2; Synonyms=SAF-2;
CC IsoId=P56270-2; Sequence=VSP_044561;
CC Name=3; Synonyms=SAF-3;
CC IsoId=P56270-3; Sequence=VSP_047560;
CC Name=4;
CC IsoId=P56270-4; Sequence=VSP_055108;
CC -!- TISSUE SPECIFICITY: Present in kidney, liver and brain. In the brain,
CC highest levels are found in motor cortex and midfrontal cortex (at
CC protein level). {ECO:0000269|PubMed:10727212}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in the heart, brain,
CC placenta, lung, liver, skeletal muscle and weakly expressed in the
CC kidney (PubMed:1502157). Expressed in the joint synovium
CC (PubMed:19583771). {ECO:0000269|PubMed:1502157,
CC ECO:0000269|PubMed:19583771}.
CC -!- INDUCTION: [Isoform 3]: Induced by cytokine and growth factor
CC stimulation. {ECO:0000269|PubMed:19583771}.
CC -!- MISCELLANEOUS: [Isoform 2]: May act as a dominant negative of isoform
CC 1. Reduced expression during inflammatory conditions. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: The transactivation potential of isoform 3
CC is much greater than that of the predominantly expressed isoform 1.
CC {ECO:0000269|PubMed:19583771}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB04121.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA12728.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M94046; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M93339; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; D85131; BAA12728.1; ALT_INIT; mRNA.
DR EMBL; U33819; AAB04121.1; ALT_INIT; mRNA.
DR EMBL; AB017335; BAA33064.1; -; Genomic_DNA.
DR EMBL; AF489858; AAN03800.1; -; mRNA.
DR EMBL; EF059746; ABN80996.1; -; mRNA.
DR EMBL; FJ532357; ACS26236.1; -; mRNA.
DR EMBL; AC009133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471238; EAW79996.1; -; Genomic_DNA.
DR EMBL; CH471238; EAW79997.1; -; Genomic_DNA.
DR CCDS; CCDS42143.1; -. [P56270-1]
DR CCDS; CCDS42144.1; -. [P56270-2]
DR CCDS; CCDS61902.1; -. [P56270-3]
DR CCDS; CCDS61903.1; -. [P56270-4]
DR PIR; A42170; A42170.
DR PIR; JC5076; JC5076.
DR RefSeq; NP_001036004.1; NM_001042539.2. [P56270-2]
DR RefSeq; NP_001263204.1; NM_001276275.1. [P56270-3]
DR RefSeq; NP_001263205.1; NM_001276276.1. [P56270-4]
DR RefSeq; NP_002374.2; NM_002383.3. [P56270-1]
DR AlphaFoldDB; P56270; -.
DR SMR; P56270; -.
DR BioGRID; 110320; 73.
DR CORUM; P56270; -.
DR IntAct; P56270; 32.
DR MINT; P56270; -.
DR STRING; 9606.ENSP00000219782; -.
DR iPTMnet; P56270; -.
DR PhosphoSitePlus; P56270; -.
DR SwissPalm; P56270; -.
DR BioMuta; MAZ; -.
DR DMDM; 3024110; -.
DR EPD; P56270; -.
DR jPOST; P56270; -.
DR MassIVE; P56270; -.
DR MaxQB; P56270; -.
DR PaxDb; P56270; -.
DR PeptideAtlas; P56270; -.
DR PRIDE; P56270; -.
DR ProteomicsDB; 33810; -.
DR ProteomicsDB; 41756; -.
DR ProteomicsDB; 56907; -. [P56270-1]
DR ProteomicsDB; 7603; -.
DR Antibodypedia; 26824; 328 antibodies from 30 providers.
DR DNASU; 4150; -.
DR Ensembl; ENST00000219782.10; ENSP00000219782.6; ENSG00000103495.15. [P56270-2]
DR Ensembl; ENST00000322945.11; ENSP00000313362.6; ENSG00000103495.15. [P56270-1]
DR Ensembl; ENST00000545521.5; ENSP00000443956.1; ENSG00000103495.15. [P56270-3]
DR Ensembl; ENST00000562337.5; ENSP00000455726.1; ENSG00000103495.15. [P56270-4]
DR GeneID; 4150; -.
DR KEGG; hsa:4150; -.
DR MANE-Select; ENST00000322945.11; ENSP00000313362.6; NM_002383.4; NP_002374.2.
DR UCSC; uc002dtx.5; human. [P56270-1]
DR CTD; 4150; -.
DR DisGeNET; 4150; -.
DR GeneCards; MAZ; -.
DR HGNC; HGNC:6914; MAZ.
DR HPA; ENSG00000103495; Low tissue specificity.
DR MIM; 600999; gene.
DR neXtProt; NX_P56270; -.
DR OpenTargets; ENSG00000103495; -.
DR PharmGKB; PA30657; -.
DR VEuPathDB; HostDB:ENSG00000103495; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158525; -.
DR HOGENOM; CLU_042232_0_0_1; -.
DR InParanoid; P56270; -.
DR OMA; HVNQEGQ; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P56270; -.
DR TreeFam; TF331686; -.
DR PathwayCommons; P56270; -.
DR SignaLink; P56270; -.
DR SIGNOR; P56270; -.
DR BioGRID-ORCS; 4150; 28 hits in 1105 CRISPR screens.
DR ChiTaRS; MAZ; human.
DR GeneWiki; MAZ_(gene); -.
DR GenomeRNAi; 4150; -.
DR Pharos; P56270; Tbio.
DR PRO; PR:P56270; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P56270; protein.
DR Bgee; ENSG00000103495; Expressed in ventricular zone and 197 other tissues.
DR ExpressionAtlas; P56270; baseline and differential.
DR Genevisible; P56270; HS.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:ARUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:ARUK-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IDA:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..477
FT /note="Myc-associated zinc finger protein"
FT /id="PRO_0000047215"
FT ZN_FING 190..212
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..301
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 307..329
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..360
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..413
FT /note="C2H2-type 6; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..34
FT /note="MFPVFPCTLLAPPFPVLGLDSRGVGGLMNSFPPP -> MDPSNWSSFIF
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19583771"
FT /id="VSP_047560"
FT VAR_SEQ 65..369
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_055108"
FT VAR_SEQ 428..477
FT /note="TGEVCPMAAAAAAAAAAAAAAVAAPPTAVGSLSGAEGVPVSSQPLPSQPW
FT -> FTTAAYLRIHAVKDHGLQAPRADRILCKLCSVHCKTPAQLAGHMQTHLGGAAPPVP
FT GDAPQPQPTC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12270922"
FT /id="VSP_044561"
FT CONFLICT 259
FT /note="Missing (in Ref. 3; BAA12728)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="E -> K (in Ref. 6; AAN03800)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..396
FT /note="HV -> PW (in Ref. 6; AAN03800)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="L -> M (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 443..447
FT /note="Missing (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 48608 MW; C04C80F32C3C6825 CRC64;
MFPVFPCTLL APPFPVLGLD SRGVGGLMNS FPPPQGHAQN PLQVGAELQS RFFASQGCAQ
SPFQAAPAPP PTPQAPAAEP LQVDLLPVLA AAQESAAAAA AAAAAAAAVA AAPPAPAAAS
TVDTAALKQP PAPPPPPPPV SAPAAEAAPP ASAATIAAAA ATAVVAPTST VAVAPVASAL
EKKTKSKGPY ICALCAKEFK NGYNLRRHEA IHTGAKAGRV PSGAMKMPTM VPLSLLSVPQ
LSGAGGGGGE AGAGGGAAAV AAGGVVTTTA SGKRIRKNHA CEMCGKAFRD VYHLNRHKLS
HSDEKPYQCP VCQQRFKRKD RMSYHVRSHD GAVHKPYNCS HCGKSFSRPD HLNSHVRQVH
STERPFKCEK CEAAFATKDR LRAHTVRHEE KVPCHVCGKM LSSAYISDHM KVHSQGPHHV
CELCNKGTGE VCPMAAAAAA AAAAAAAAVA APPTAVGSLS GAEGVPVSSQ PLPSQPW
