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Transcription factor Maf (Proto-oncogene c-Maf) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog)

 MAF_HUMAN               Reviewed;         373 AA.
O75444; Q66I47; Q9UP93;
11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 2.
27-SEP-2017, entry version 151.
RecName: Full=Transcription factor Maf;
AltName: Full=Proto-oncogene c-Maf;
AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog;
Name=MAF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
ALTERNATIVE SPLICING.
PubMed=9616139;
Chesi M., Bergsagel P.L., Shonukan O.O., Martelli M.L., Brents L.A.,
Chen T., Schrock E., Ried T., Kuehl W.M.;
"Frequent dysregulation of the c-maf proto-oncogene at 16q23 by
translocation to an Ig locus in multiple myeloma.";
Blood 91:4457-4463(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBUNIT, INDUCTION, AND DNA-BINDING.
PubMed=12149651; DOI=10.1038/sj.onc.1205642;
Dhakshinamoorthy S., Jaiswal A.K.;
"c-Maf negatively regulates ARE-mediated detoxifying enzyme genes
expression and anti-oxidant induction.";
Oncogene 21:5301-5312(2002).
[5]
FUNCTION.
PubMed=14998494; DOI=10.1016/S1535-6108(04)00019-4;
Hurt E.M., Wiestner A., Rosenwald A., Shaffer A.L., Campo E.,
Grogan T., Bergsagel P.L., Kuehl W.M., Staudt L.M.;
"Overexpression of c-maf is a frequent oncogenic event in multiple
myeloma that promotes proliferation and pathological interactions with
bone marrow stroma.";
Cancer Cell 5:191-199(2004).
[6]
FUNCTION.
PubMed=15007382; DOI=10.1038/sj.onc.1207474;
Watson J.E., Doggett N.A., Albertson D.G., Andaya A., Chinnaiyan A.,
van Dekken H., Ginzinger D., Haqq C., James K., Kamkar S., Kowbel D.,
Pinkel D., Schmitt L., Simko J.P., Volik S., Weinberg V.K.,
Paris P.L., Collins C.;
"Integration of high-resolution array comparative genomic
hybridization analysis of chromosome 16q with expression array data
refines common regions of loss at 16q23-qter and identifies underlying
candidate tumor suppressor genes in prostate cancer.";
Oncogene 23:3487-3494(2004).
[7]
PHOSPHORYLATION.
PubMed=15963504; DOI=10.1016/j.febslet.2005.04.086;
Sii-Felice K., Pouponnot C., Gillet S., Lecoin L., Girault J.-A.,
Eychene A., Felder-Schmittbuhl M.-P.;
"MafA transcription factor is phosphorylated by p38 MAP kinase.";
FEBS Lett. 579:3547-3554(2005).
[8]
UBIQUITINATION.
PubMed=17875808; DOI=10.1182/blood-2007-05-088666;
Mao X., Stewart A.K., Hurren R., Datti A., Zhu X., Zhu Y., Shi C.,
Lee K., Tiedemann R., Eberhard Y., Trudel S., Liang S., Corey S.J.,
Gillis L.C., Barber D.L., Wrana J.L., Ezzat S., Schimmer A.D.;
"A chemical biology screen identifies glucocorticoids that regulate c-
maf expression by increasing its proteasomal degradation through up-
regulation of ubiquitin.";
Blood 110:4047-4054(2007).
[9]
FUNCTION.
PubMed=16247450; DOI=10.1038/sj.onc.1209171;
Pouponnot C., Sii-Felice K., Hmitou I., Rocques N., Lecoin L.,
Druillennec S., Felder-Schmittbuhl M.-P., Eychene A.;
"Cell context reveals a dual role for Maf in oncogenesis.";
Oncogene 25:1299-1310(2006).
[10]
TISSUE SPECIFICITY.
PubMed=17897790; DOI=10.1016/j.gene.2007.08.010;
Mahoney K.M., Petrovic N., Schacke W., Shapiro L.H.;
"CD13/APN transcription is regulated by the proto-oncogene c-Maf via
an atypical response element.";
Gene 403:178-187(2007).
[11]
PHOSPHORYLATION.
PubMed=18042454; DOI=10.1016/j.molcel.2007.11.009;
Rocques N., Abou Zeid N., Sii-Felice K., Lecoin L.,
Felder-Schmittbuhl M.-P., Eychene A., Pouponnot C.;
"GSK-3-mediated phosphorylation enhances Maf-transforming activity.";
Mol. Cell 28:584-597(2007).
[12]
INVOLVEMENT IN CTRCT21, AND VARIANT CTRCT21 LEU-303.
PubMed=24664492; DOI=10.1002/ajmg.a.36433;
Narumi Y., Nishina S., Tokimitsu M., Aoki Y., Kosaki R., Wakui K.,
Azuma N., Murata T., Takada F., Fukushima Y., Kosho T.;
"Identification of a novel missense mutation of MAF in a Japanese
family with congenital cataract by whole exome sequencing: a clinical
report and review of literature.";
Am. J. Med. Genet. A 164A:1272-1276(2014).
[13]
INVOLVEMENT IN AYGRP, AND VARIANTS AYGRP LEU-54; ALA-58; ILE-58;
HIS-59; LEU-59; ARG-62 AND ARG-69.
PubMed=25865493; DOI=10.1016/j.ajhg.2015.03.001;
Niceta M., Stellacci E., Gripp K.W., Zampino G., Kousi M., Anselmi M.,
Traversa A., Ciolfi A., Stabley D., Bruselles A., Caputo V.,
Cecchetti S., Prudente S., Fiorenza M.T., Boitani C., Philip N.,
Niyazov D., Leoni C., Nakane T., Keppler-Noreuil K., Braddock S.R.,
Gillessen-Kaesbach G., Palleschi A., Campeau P.M., Lee B.H.,
Pouponnot C., Stella L., Bocchinfuso G., Katsanis N., Sol-Church K.,
Tartaglia M.;
"Mutations impairing GSK3-mediated MAF phosphorylation cause cataract,
deafness, intellectual disability, seizures, and a Down syndrome-like
facies.";
Am. J. Hum. Genet. 96:816-825(2015).
[14]
REVIEW, AND FUNCTION.
PubMed=19143053; DOI=10.1038/nrc2460;
Eychene A., Rocques N., Pouponnot C.;
"A new MAFia in cancer.";
Nat. Rev. Cancer 8:683-693(2008).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29; LYS-33 AND LYS-331,
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-379 (ISOFORM 1), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[17]
VARIANT CTRCT21 PRO-288.
PubMed=11772997; DOI=10.1093/hmg/11.1.33;
Jamieson R.V., Perveen R., Kerr B., Carette M., Yardley J., Heon E.,
Wirth M.G., van Heyningen V., Donnai D., Munier F., Black G.C.;
"Domain disruption and mutation of the bZIP transcription factor, MAF,
associated with cataract, ocular anterior segment dysgenesis and
coloboma.";
Hum. Mol. Genet. 11:33-42(2002).
[18]
VARIANT CTRCT21 ARG-297.
PubMed=16470690; DOI=10.1002/ajmg.a.31126;
Vanita V., Singh D., Robinson P.N., Sperling K., Singh J.R.;
"A novel mutation in the DNA-binding domain of MAF at 16q23.1
associated with autosomal dominant 'cerulean cataract' in an Indian
family.";
Am. J. Med. Genet. A 140:558-566(2006).
-!- FUNCTION: Acts as a transcriptional activator or repressor.
Involved in embryonic lens fiber cell development. Recruits the
transcriptional coactivators CREBBP and/or EP300 to crystallin
promoters leading to up-regulation of crystallin gene during lens
fiber cell differentiation. Activates the expression of IL4 in T
helper 2 (Th2) cells. Increases T-cell susceptibility to apoptosis
by interacting with MYB and decreasing BCL2 expression. Together
with PAX6, transactivates strongly the glucagon gene promoter
through the G1 element. Activates transcription of the CD13
proximal promoter in endothelial cells. Represses transcription of
the CD13 promoter in early stages of myelopoiesis by affecting the
ETS1 and MYB cooperative interaction. Involved in the initial
chondrocyte terminal differentiation and the disappearance of
hypertrophic chondrocytes during endochondral bone development.
Binds to the sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7
promoter. Binds to the T-MARE (Maf response element) sites of
lens-specific alpha- and beta-crystallin gene promoters. Binds
element G1 on the glucagon promoter. Binds an AT-rich region
adjacent to the TGC motif (atypical Maf response element) in the
CD13 proximal promoter in endothelial cells (By similarity). When
overexpressed, represses anti-oxidant response element (ARE)-
mediated transcription. Involved either as an oncogene or as a
tumor suppressor, depending on the cell context. Binds to the ARE
sites of detoxifying enzyme gene promoters. {ECO:0000250,
ECO:0000269|PubMed:12149651, ECO:0000269|PubMed:14998494,
ECO:0000269|PubMed:15007382, ECO:0000269|PubMed:16247450,
ECO:0000269|PubMed:19143053}.
-!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip
transcription factors. Binds DNA as a homodimer or as a
heterodimer. Heterotetramer of two MAF and two USF2. Interacts
with PAX6; the interaction is direct. Interacts with MYB;
interaction takes place weakly in normal T-cells and increases in
T-cells following stimulation through the TCR engagement.
Interacts with MYB; the ternary complex formed with MYB and the
CD13 promoter is regulated in response to differentiating signals.
Interacts with USF2; the interaction inhibits its DNA-binding
activity on the L7 promoter. Interacts with CREBBP, EP300 and ETS1
(By similarity). {ECO:0000250}.
-!- INTERACTION:
O14867:BACH1; NbExp=2; IntAct=EBI-2805091, EBI-1263541;
P0C746:HBZ (xeno); NbExp=2; IntAct=EBI-2805091, EBI-10890294;
Q9Y5Q3:MAFB; NbExp=2; IntAct=EBI-2805091, EBI-3649340;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=Short;
IsoId=O75444-2; Sequence=Displayed;
Name=1; Synonyms=Long;
IsoId=O75444-1; Sequence=VSP_000583;
Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
with G-Cter in SUMO2) at position 379.
{ECO:0000244|PubMed:28112733};
-!- TISSUE SPECIFICITY: Expressed in endothelial cells.
{ECO:0000269|PubMed:17897790}.
-!- INDUCTION: Up-regulated with tert-butyl hydroquinone (t-BHQ).
{ECO:0000269|PubMed:12149651}.
-!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
Ubiquitination is triggered by glucocorticoids.
{ECO:0000269|PubMed:17875808}.
-!- PTM: Phosphorylated by GSK3 and MAPK13 on serine and threonine
residues (Probable). The phosphorylation status can serve to
either stimulate or inhibit transcription.
{ECO:0000269|PubMed:15963504, ECO:0000269|PubMed:18042454,
ECO:0000305}.
-!- DISEASE: Note=A chromosomal aberration involving MAF is found in
some forms of multiple myeloma (MM). Translocation
t(14;16)(q32.3;q23) with an IgH locus.
-!- DISEASE: Cataract 21, multiple types (CTRCT21) [MIM:610202]: An
opacification of the crystalline lens of the eye that frequently
results in visual impairment or blindness. Opacities vary in
morphology, are often confined to a portion of the lens, and may
be static or progressive. In general, the more posteriorly located
and dense an opacity, the greater the impact on visual function.
CTRCT21 includes cerulean and pulverulent cataracts. Cerulean
cataracts are characterized by peripheral bluish and white
opacifications organized in concentric layers with occasional
central lesions arranged radially. The opacities are observed in
the superficial layers of the fetal nucleus as well as the adult
nucleus of the lens. Involvement is usually bilateral. Visual
acuity is only mildly reduced in childhood. In adulthood, the
opacifications may progress, making lens extraction necessary.
Histologically the lesions are described as fusiform cavities
between lens fibers which contain a deeply staining granular
material. Although the lesions may take on various colors, a dull
blue is the most common appearance and is responsible for the
designation cerulean cataract. Pulverulent cataracts are
characterized by a dust-like, 'pulverised' appearance of the
opacities which can be found in any part of the lens. In some
cases cataract is associated with microcornea without any other
systemic anomaly or dysmorphism. Microcornea is defined by a
corneal diameter inferior to 10 mm in both meridians in an
otherwise normal eye. {ECO:0000269|PubMed:11772997,
ECO:0000269|PubMed:16470690, ECO:0000269|PubMed:24664492}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Ayme-Gripp syndrome (AYGRP) [MIM:601088]: A multisystem
disorder characterized by congenital cataracts, sensorineural
deafness, intellectual disability, seizures, brachycephaly,
distinctive flat facial appearance, skeletal anomalies, mammary
gland hypoplasia, and reduced growth.
{ECO:0000269|PubMed:25865493}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the bZIP family. Maf subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAFID41234ch16q23.html";
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EMBL; AF055376; AAC27037.1; -; mRNA.
EMBL; AF055377; AAC27038.1; -; mRNA.
EMBL; AF055378; AAC27039.1; -; Genomic_DNA.
EMBL; AC009159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC081542; AAH81542.1; -; mRNA.
CCDS; CCDS10928.1; -. [O75444-1]
CCDS; CCDS42198.1; -. [O75444-2]
RefSeq; NP_001026974.1; NM_001031804.2. [O75444-2]
RefSeq; NP_005351.2; NM_005360.4. [O75444-1]
UniGene; Hs.134859; -.
ProteinModelPortal; O75444; -.
SMR; O75444; -.
BioGrid; 110269; 22.
ELM; O75444; -.
IntAct; O75444; 6.
STRING; 9606.ENSP00000327048; -.
iPTMnet; O75444; -.
PhosphoSitePlus; O75444; -.
BioMuta; MAF; -.
PaxDb; O75444; -.
PeptideAtlas; O75444; -.
PRIDE; O75444; -.
Ensembl; ENST00000326043; ENSP00000327048; ENSG00000178573. [O75444-1]
Ensembl; ENST00000393350; ENSP00000377019; ENSG00000178573. [O75444-2]
GeneID; 4094; -.
KEGG; hsa:4094; -.
UCSC; uc002ffm.4; human. [O75444-2]
CTD; 4094; -.
DisGeNET; 4094; -.
EuPathDB; HostDB:ENSG00000178573.6; -.
GeneCards; MAF; -.
H-InvDB; HIX0173268; -.
HGNC; HGNC:6776; MAF.
HPA; CAB010296; -.
HPA; HPA028289; -.
MalaCards; MAF; -.
MIM; 177075; gene.
MIM; 601088; phenotype.
MIM; 610202; phenotype.
neXtProt; NX_O75444; -.
OpenTargets; ENSG00000178573; -.
Orphanet; 1377; Cataract-microcornea syndrome.
Orphanet; 98989; Cerulean cataract.
Orphanet; 98984; Pulverulent cataract.
PharmGKB; PA30534; -.
eggNOG; KOG4196; Eukaryota.
eggNOG; ENOG410YCYQ; LUCA.
GeneTree; ENSGT00550000074549; -.
HOGENOM; HOG000261683; -.
HOVERGEN; HBG000313; -.
InParanoid; O75444; -.
KO; K09035; -.
OMA; GTVHPHM; -.
OrthoDB; EOG091G0H46; -.
PhylomeDB; O75444; -.
TreeFam; TF325689; -.
SignaLink; O75444; -.
SIGNOR; O75444; -.
GeneWiki; MAF_(gene); -.
GenomeRNAi; 4094; -.
PRO; PR:O75444; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000178573; -.
CleanEx; HS_MAF; -.
ExpressionAtlas; O75444; baseline and differential.
Genevisible; O75444; HS.
GO; GO:0000785; C:chromatin; TAS:ProtInc.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
GO; GO:0048468; P:cell development; IEA:Ensembl.
GO; GO:0001816; P:cytokine production; IEA:Ensembl.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0070306; P:lens fiber cell differentiation; IBA:GO_Central.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0032330; P:regulation of chondrocyte differentiation; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
InterPro; IPR004827; bZIP.
InterPro; IPR004826; bZIP_Maf.
InterPro; IPR028573; Maf/V-MAF.
InterPro; IPR013592; Maf_TF_N.
InterPro; IPR008917; TF_DNA-bd.
InterPro; IPR024874; Transciption_factor_Maf_fam.
PANTHER; PTHR10129; PTHR10129; 1.
PANTHER; PTHR10129:SF35; PTHR10129:SF35; 1.
Pfam; PF03131; bZIP_Maf; 1.
Pfam; PF08383; Maf_N; 1.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Cataract; Chromosomal rearrangement;
Complete proteome; Disease mutation; DNA-binding; Dwarfism;
Isopeptide bond; Mental retardation; Nucleus; Proto-oncogene;
Reference proteome; Repressor; Transcription;
Transcription regulation; Tumor suppressor; Ubl conjugation.
CHAIN 1 373 Transcription factor Maf.
/FTId=PRO_0000076491.
DOMAIN 288 351 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 126 373 Represses ARE-mediated transcription.
REGION 288 313 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 316 337 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 126 254 Gly-rich.
COMPBIAS 132 252 Ala-rich.
COMPBIAS 180 194 His-rich.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 373 373 M -> ITEPTRKLEPSVGYATFWKPQHRVLTSVFTK (in
isoform 1). {ECO:0000303|PubMed:9616139}.
/FTId=VSP_000583.
VARIANT 54 54 S -> L (in AYGRP; dbSNP:rs727502766).
{ECO:0000269|PubMed:25865493}.
/FTId=VAR_073891.
VARIANT 58 58 T -> A (in AYGRP; dbSNP:rs727502767).
{ECO:0000269|PubMed:25865493}.
/FTId=VAR_073892.
VARIANT 58 58 T -> I (in AYGRP; dbSNP:rs727502769).
{ECO:0000269|PubMed:25865493}.
/FTId=VAR_073893.
VARIANT 59 59 P -> H (in AYGRP; dbSNP:rs727502770).
{ECO:0000269|PubMed:25865493}.
/FTId=VAR_073894.
VARIANT 59 59 P -> L (in AYGRP; dbSNP:rs727502770).
{ECO:0000269|PubMed:25865493}.
/FTId=VAR_073895.
VARIANT 62 62 T -> R (in AYGRP; dbSNP:rs727502771).
{ECO:0000269|PubMed:25865493}.
/FTId=VAR_073896.
VARIANT 69 69 P -> R (in AYGRP; dbSNP:rs727502768).
{ECO:0000269|PubMed:25865493}.
/FTId=VAR_073897.
VARIANT 288 288 R -> P (in CTRCT21; dbSNP:rs121917735).
{ECO:0000269|PubMed:11772997}.
/FTId=VAR_029369.
VARIANT 297 297 K -> R (in CTRCT21; dbSNP:rs121917736).
{ECO:0000269|PubMed:16470690}.
/FTId=VAR_029370.
VARIANT 303 303 Q -> L (in CTRCT21).
{ECO:0000269|PubMed:24664492}.
/FTId=VAR_073898.
SEQUENCE 373 AA; 38492 MW; 566C2BC3E4A62762 CRC64;
MASELAMSNS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI AGGSLSSTPM
STPCSSVPPS PSFSAPSPGS GSEQKAHLED YYWMTGYPQQ LNPEALGFSP EDAVEALISN
SHQLQGGFDG YARGAQQLAA AAGAGAGASL GGSGEEMGPA AAVVSAVIAA AAAQSGAGPH
YHHHHHHAAG HHHHPTAGAP GAAGSAAASA GGAGGAGGGG PASAGGGGGG GGGGGGGGAA
GAGGALHPHH AAGGLHFDDR FSDEQLVTMS VRELNRQLRG VSKEEVIRLK QKRRTLKNRG
YAQSCRFKRV QQRHVLESEK NQLLQQVDHL KQEISRLVRE RDAYKEKYEK LVSSGFRENG
SSSDNPSSPE FFM


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