SOX17_MOUSE
ID SOX17_MOUSE Reviewed; 419 AA.
AC Q61473; Q61472; Q62248;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Transcription factor SOX-17;
GN Name=Sox17; Synonyms=Sox-17;
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 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=8636240; DOI=10.1083/jcb.133.3.667;
RA Kanai Y., Kanai-Azuma M., Noce T., Saido T.C., Shiroishi T., Hayashi Y.,
RA Yazaki K.;
RT "Identification of two Sox17 messenger RNA isoforms, with and without the
RT high mobility group box region, and their differential expression in mouse
RT spermatogenesis.";
RL J. Cell Biol. 133:667-681(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-132 (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Heart muscle;
RA Layfield R., Mynett-Johnson L., Yarwood P.J., Muscat G.E.O., Koopman P.A.,
RA Hume D.A.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=11973269; DOI=10.1242/dev.129.10.2367;
RA Kanai-Azuma M., Kanai Y., Gad J.M., Tajima Y., Taya C., Kurohmaru M.,
RA Sanai Y., Yonekawa H., Yazaki K., Tam P.P., Hayashi Y.;
RT "Depletion of definitive gut endoderm in Sox17-null mutant mice.";
RL Development 129:2367-2379(2002).
RN [5]
RP FUNCTION.
RX PubMed=16895970; DOI=10.1242/jcs.03081;
RA Matsui T., Kanai-Azuma M., Hara K., Matoba S., Hiramatsu R., Kawakami H.,
RA Kurohmaru M., Koopman P., Kanai Y.;
RT "Redundant roles of Sox17 and Sox18 in postnatal angiogenesis in mice.";
RL J. Cell Sci. 119:3513-3526(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17655922; DOI=10.1016/j.cell.2007.06.011;
RA Kim I., Saunders T.L., Morrison S.J.;
RT "Sox17 dependence distinguishes the transcriptional regulation of fetal
RT from adult hematopoietic stem cells.";
RL Cell 130:470-483(2007).
RN [7]
RP FUNCTION, INTERACTION WITH CTNNB1; LEF1 AND TCF4, AND SUBCELLULAR LOCATION.
RX PubMed=20802155; DOI=10.1152/ajplung.00140.2010;
RA Liu X., Luo M., Xie W., Wells J.M., Goodheart M.J., Engelhardt J.F.;
RT "Sox17 modulates Wnt3A/beta-catenin-mediated transcriptional activation of
RT the Lef-1 promoter.";
RL Am. J. Physiol. 299:L694-L710(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=24153254; DOI=10.1038/ncomms3609;
RA Corada M., Orsenigo F., Morini M.F., Pitulescu M.E., Bhat G., Nyqvist D.,
RA Breviario F., Conti V., Briot A., Iruela-Arispe M.L., Adams R.H.,
RA Dejana E.;
RT "Sox17 is indispensable for acquisition and maintenance of arterial
RT identity.";
RL Nat. Commun. 4:2609-2609(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 66-144 IN COMPLEX WITH TARGET
RP DNA, AND FUNCTION.
RX PubMed=19328208; DOI=10.1016/j.jmb.2009.03.055;
RA Palasingam P., Jauch R., Ng C.K., Kolatkar P.R.;
RT "The structure of Sox17 bound to DNA reveals a conserved bending topology
RT but selective protein interaction platforms.";
RL J. Mol. Biol. 388:619-630(2009).
CC -!- FUNCTION: Acts as transcription regulator that binds target promoter
CC DNA and bends the DNA (PubMed:8636240, PubMed:24153254,
CC PubMed:19328208). Binds to the sequences 5'-AACAAT-'3 or 5'-AACAAAG-3'
CC (PubMed:8636240). Modulates transcriptional regulation via WNT3A.
CC Inhibits Wnt signaling. Promotes degradation of activated CTNNB1. Plays
CC a key role in the regulation of embryonic development (PubMed:11973269,
CC PubMed:17655922, PubMed:24153254). Required for normal development of
CC the definitive gut endoderm (PubMed:11973269). Required for normal
CC looping of the embryonic heart tube. Plays an important role in
CC embryonic and postnatal vascular development, including development of
CC arteries (PubMed:24153254). Plays an important role in postnatal
CC angiogenesis, where it is functionally redundant with SOX18
CC (PubMed:16895970). Required for the generation and maintenance of fetal
CC hematopoietic stem cells, and for fetal hematopoiesis
CC (PubMed:17655922). Probable transcriptional activator in the premeiotic
CC germ cells. {ECO:0000269|PubMed:11973269, ECO:0000269|PubMed:16895970,
CC ECO:0000269|PubMed:17655922, ECO:0000269|PubMed:19328208,
CC ECO:0000269|PubMed:20802155, ECO:0000269|PubMed:24153254,
CC ECO:0000269|PubMed:8636240}.
CC -!- FUNCTION: [Isoform 2]: Has no DNA-binding activity, and does not
CC function as transcriptional activator. {ECO:0000269|PubMed:8636240}.
CC -!- SUBUNIT: Interacts with CTNNB1, LEF1 and TCF4.
CC {ECO:0000269|PubMed:20802155}.
CC -!- INTERACTION:
CC Q61473; P26233: ctnnb1; Xeno; NbExp=3; IntAct=EBI-9106822, EBI-7373758;
CC Q61473; Q01978: tcf3; Xeno; NbExp=3; IntAct=EBI-9106822, EBI-9106902;
CC Q61473; P15884: TCF4; Xeno; NbExp=5; IntAct=EBI-9106822, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:20802155, ECO:0000269|PubMed:24153254,
CC ECO:0000269|PubMed:8636240}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61473-1; Sequence=Displayed;
CC Name=2; Synonyms=T-SOX17;
CC IsoId=Q61473-2; Sequence=VSP_002204;
CC -!- TISSUE SPECIFICITY: Detected in lung and testis (PubMed:8636240).
CC Detected in endothelial cells around small and large arteries in
CC newborns and adults, but is barely detectable in veins (at protein
CC level) (PubMed:24153254). Detected in lung and testis (PubMed:8636240).
CC {ECO:0000269|PubMed:24153254, ECO:0000269|PubMed:8636240}.
CC -!- DEVELOPMENTAL STAGE: Detected in the extraembryonic region of the
CC visceral endoderm of pre-streak and early-streak embryos. Detected in
CC the extraembryonic region of the visceral endoderm and in the
CC definitive endoderm at 7.5 dpc. By the seven to eight somite stage,
CC detected in the posterior endoderm, mainly in the endoderm of the
CC midgut and hindgut invagination. Expressed in spermatogonia. The
CC expression clearly declines from the early pachytene spermatocyte stage
CC onward. In contrast, expression of isoform 2 (T-SOX17) begins at the
CC pachytene spermatocyte stage and is highly accumulated in round
CC spermatids (PubMed:11973269). Detected in arterial endothelium in
CC embryos and yolk sac at 10.5 dpc (PubMed:24153254).
CC {ECO:0000269|PubMed:11973269, ECO:0000269|PubMed:24153254}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:Q9H6I2}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal due to defects in the
CC development of the definite gut endoderm, aberrant heart looping and
CC severe defects in vascular development and remodeling, including a lack
CC of artery formation. Embryos die at about 10.5 dpc (PubMed:11973269,
CC PubMed:17655922, PubMed:24153254). Besides, mutant embryos display a
CC severe defect in fetal hematopoiesis (PubMed:17655922).
CC {ECO:0000269|PubMed:11973269, ECO:0000269|PubMed:17655922,
CC ECO:0000269|PubMed:24153254}.
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DR EMBL; D49474; BAA08444.1; -; mRNA.
DR EMBL; D49473; BAA08443.1; -; mRNA.
DR EMBL; AK004781; BAB23559.1; -; mRNA.
DR EMBL; L29085; AAA56843.1; -; mRNA.
DR CCDS; CCDS14805.1; -. [Q61473-1]
DR CCDS; CCDS78538.1; -. [Q61473-2]
DR RefSeq; NP_001276393.1; NM_001289464.1. [Q61473-1]
DR RefSeq; NP_001276394.1; NM_001289465.1.
DR RefSeq; NP_001276396.1; NM_001289467.1. [Q61473-2]
DR RefSeq; NP_035571.1; NM_011441.5. [Q61473-1]
DR RefSeq; XP_006495537.1; XM_006495474.2. [Q61473-1]
DR RefSeq; XP_006495538.1; XM_006495475.3.
DR RefSeq; XP_011236666.1; XM_011238364.2.
DR PDB; 3F27; X-ray; 2.75 A; D=66-144.
DR PDB; 6L6Y; X-ray; 3.00 A; D/F=66-144.
DR PDBsum; 3F27; -.
DR PDBsum; 6L6Y; -.
DR AlphaFoldDB; Q61473; -.
DR SMR; Q61473; -.
DR BioGRID; 203403; 16.
DR IntAct; Q61473; 8.
DR STRING; 10090.ENSMUSP00000027035; -.
DR iPTMnet; Q61473; -.
DR PhosphoSitePlus; Q61473; -.
DR MaxQB; Q61473; -.
DR PaxDb; Q61473; -.
DR PRIDE; Q61473; -.
DR ProteomicsDB; 261478; -. [Q61473-1]
DR ProteomicsDB; 261479; -. [Q61473-2]
DR Antibodypedia; 11698; 468 antibodies from 42 providers.
DR DNASU; 20671; -.
DR Ensembl; ENSMUST00000027035; ENSMUSP00000027035; ENSMUSG00000025902. [Q61473-1]
DR Ensembl; ENSMUST00000116652; ENSMUSP00000112351; ENSMUSG00000025902. [Q61473-1]
DR Ensembl; ENSMUST00000195555; ENSMUSP00000141894; ENSMUSG00000025902. [Q61473-2]
DR GeneID; 20671; -.
DR KEGG; mmu:20671; -.
DR UCSC; uc007aey.1; mouse. [Q61473-1]
DR CTD; 64321; -.
DR MGI; MGI:107543; Sox17.
DR VEuPathDB; HostDB:ENSMUSG00000025902; -.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000156694; -.
DR HOGENOM; CLU_044994_0_1_1; -.
DR InParanoid; Q61473; -.
DR OrthoDB; 1042753at2759; -.
DR PhylomeDB; Q61473; -.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR BioGRID-ORCS; 20671; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sox17; mouse.
DR PRO; PR:Q61473; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61473; protein.
DR Bgee; ENSMUSG00000025902; Expressed in brain blood vessel and 221 other tissues.
DR ExpressionAtlas; Q61473; baseline and differential.
DR Genevisible; Q61473; MM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IGI:MGI.
DR GO; GO:0060913; P:cardiac cell fate determination; ISO:MGI.
DR GO; GO:0003142; P:cardiogenic plate morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IDA:MGI.
DR GO; GO:0061009; P:common bile duct development; IMP:MGI.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:BHF-UCL.
DR GO; GO:0035050; P:embryonic heart tube development; IGI:MGI.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:BHF-UCL.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0060956; P:endocardial cell differentiation; IGI:MGI.
DR GO; GO:0060214; P:endocardium formation; IGI:MGI.
DR GO; GO:0007492; P:endoderm development; IMP:UniProtKB.
DR GO; GO:0001706; P:endoderm formation; ISO:MGI.
DR GO; GO:0035987; P:endodermal cell differentiation; IDA:MGI.
DR GO; GO:0007493; P:endodermal cell fate determination; IDA:MGI.
DR GO; GO:0001714; P:endodermal cell fate specification; IMP:BHF-UCL.
DR GO; GO:0061031; P:endodermal digestive tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0061010; P:gall bladder development; IMP:MGI.
DR GO; GO:0007369; P:gastrulation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0001947; P:heart looping; IMP:UniProtKB.
DR GO; GO:0001828; P:inner cell mass cellular morphogenesis; IMP:MGI.
DR GO; GO:0001656; P:metanephros development; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0003308; P:negative regulation of Wnt signaling pathway involved in heart development; IMP:BHF-UCL.
DR GO; GO:0003151; P:outflow tract morphogenesis; IGI:BHF-UCL.
DR GO; GO:1903226; P:positive regulation of endodermal cell differentiation; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:2000043; P:regulation of cardiac cell fate specification; IMP:BHF-UCL.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:MGI.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:2000035; P:regulation of stem cell division; IMP:MGI.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0021903; P:rostrocaudal neural tube patterning; IMP:MGI.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IDA:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR GO; GO:0048866; P:stem cell fate specification; IDA:MGI.
DR GO; GO:0072189; P:ureter development; ISO:MGI.
DR GO; GO:0001570; P:vasculogenesis; IGI:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR033392; Sox7/17/18_central.
DR InterPro; IPR021934; Sox_C.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF12067; Sox17_18_mid; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS51516; SOX_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Wnt signaling pathway.
FT CHAIN 1..419
FT /note="Transcription factor SOX-17"
FT /id="PRO_0000048766"
FT DOMAIN 278..418
FT /note="Sox C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00849"
FT DNA_BIND 68..136
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 366..374
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q9H6I2"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8636240"
FT /id="VSP_002204"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:3F27"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3F27"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:3F27"
FT HELIX 111..131
FT /evidence="ECO:0007829|PDB:3F27"
SQ SEQUENCE 419 AA; 44646 MW; 14233EED2CCDD69D CRC64;
MSSPDAGYAS DDQSQPRSAQ PAVMAGLGPC PWAESLSPLG DVKVKGEVVA SSGAPAGTSG
RAKAESRIRR PMNAFMVWAK DERKRLAQQN PDLHNAELSK MLGKSWKALT LAEKRPFVEE
AERLRVQHMQ DHPNYKYRPR RRKQVKRMKR VEGGFLHALV EPQAGALGPE GGRVAMDGLG
LPFPEPGYPA GPPLMSPHMG PHYRDCQGLG APALDGYPLP TPDTSPLDGV EQDPAFFAAP
LPGDCPAAGT YTYAPVSDYA VSVEPPAGPM RVGPDPSGPA MPGILAPPSA LHLYYGAMGS
PAASAGRGFH AQPQQPLQPQ APPPPPQQQH PAHGPGQPSP PPEALPCRDG TESNQPTELL
GEVDRTEFEQ YLPFVYKPEM GLPYQGHDCG VNLSDSHGAI SSVVSDASSA VYYCNYPDI
