AP2A_MOUSE
ID AP2A_MOUSE Reviewed; 437 AA.
AC P34056; Q60740; Q60741; Q60742; Q60743; Q62067; Q62068; Q62069; Q91VX0;
AC Q9CRY4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Transcription factor AP-2-alpha;
DE Short=AP2-alpha;
DE AltName: Full=AP-2 transcription factor;
DE AltName: Full=Activating enhancer-binding protein 2-alpha;
DE AltName: Full=Activator protein 2;
DE Short=AP-2;
GN Name=Tfap2a; Synonyms=Ap2tf, Tcfap2a;
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].
RC STRAIN=NIH Swiss;
RX PubMed=8233835; DOI=10.1093/nar/21.20.4844;
RA Moser M., Pscherer A., Bauer R., Imhof A., Seegers S., Kerscher M.,
RA Buettner R.;
RT "The complete murine cDNA sequence of the transcription factor AP-2.";
RL Nucleic Acids Res. 21:4844-4844(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-279, AND ALTERNATIVE
RP SPLICING.
RC STRAIN=129/4, and ICR; TISSUE=Embryo;
RX PubMed=7750631; DOI=10.1006/dbio.1995.1121;
RA Meier P., Koedood M., Philipp J., Fontana A., Mitchell P.J.;
RT "Alternative mRNAs encode multiple isoforms of transcription factor AP-2
RT during murine embryogenesis.";
RL Dev. Biol. 169:1-14(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-437.
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 259-437.
RX PubMed=1989904; DOI=10.1101/gad.5.1.105;
RA Mitchell P.J., Timmons P.M., Hebert J.M., Rigby P.W.J., Tjian R.;
RT "Transcription factor AP-2 is expressed in neural crest cell lineages
RT during mouse embryogenesis.";
RL Genes Dev. 5:105-119(1991).
RN [6]
RP INTERACTION WITH CITED4.
RX PubMed=12504852; DOI=10.1006/geno.2002.7005;
RA Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T.,
RA Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S.,
RA Shioda T.;
RT "Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding
RT transcriptional coactivators: induced expression in mammary epithelial
RT cells.";
RL Genomics 80:601-613(2002).
RN [7]
RP FUNCTION, ASSOCIATION WITH CHROMATIN, AND DEVELOPMENTAL STAGE.
RX PubMed=15475956; DOI=10.1038/ng1446;
RA Bamforth S.D., Braganca J., Farthing C.R., Schneider J.E., Broadbent C.,
RA Michell A.C., Clarke K., Neubauer S., Norris D., Brown N.A., Anderson R.H.,
RA Bhattacharya S.;
RT "Cited2 controls left-right patterning and heart development through a
RT Nodal-Pitx2c pathway.";
RL Nat. Genet. 36:1189-1196(2004).
CC -!- FUNCTION: Sequence-specific DNA-binding protein that interacts with
CC inducible viral and cellular enhancer elements to regulate
CC transcription of selected genes. AP-2 factors bind to the consensus
CC sequence 5'-GCCNNNGGC-3' and activate genes involved in a large
CC spectrum of important biological functions including proper eye, face,
CC body wall, limb and neural tube development. They also suppress a
CC number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha
CC is the only AP-2 protein required for early morphogenesis of the lens
CC vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1
CC promoter transcription activation. Associates with chromatin to the
CC PITX2 P1 promoter region. {ECO:0000269|PubMed:15475956}.
CC -!- SUBUNIT: Binds DNA as a dimer. Can form homodimers or heterodimers with
CC other AP-2 family members. Interacts with WWOX. Interacts with UBE2I.
CC Interacts with RALBP1 in a complex also containing EPN1 and NUMB during
CC interphase and mitosis (By similarity). Interacts with CITED4.
CC Interacts with KCTD1; this interaction represses transcription
CC activation. Interacts (via C-terminus) with CITED2 (via C-terminus);
CC the interaction stimulates TFAP2A-transcriptional activation. Interacts
CC (via N-terminus) with EP300 (via N-terminus); the interaction requires
CC CITED2 (By similarity). Interacts with KCTD15; this interaction
CC inhibits TFAP2A transcriptional activation (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P34056-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P34056-2; Sequence=VSP_006404;
CC Name=3;
CC IsoId=P34056-3; Sequence=VSP_006402;
CC Name=4;
CC IsoId=P34056-4; Sequence=VSP_006403;
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic heart. Expressed from
CC embryo day 9.5 to birth. At day 12.5, expressed in the midbrain,
CC hindbrain, spinal cord, sensory ganglia, epidermis, nephric system and
CC limbs. At mid-embryogenesis, isoform 3 is the most abundant form in the
CC nervous system and total embryo, but the least abundant form in the
CC epidermis. In adults, AP-2A is expressed in the eye, skin, kidney,
CC prostate, thymus, skeletal muscle and very weakly, in the brain.
CC Highest expression found in skin and eye.
CC {ECO:0000269|PubMed:15475956}.
CC -!- INDUCTION: All isoforms are induced during retinoic acid-mediated
CC differentiation and by cAMP stimulation of primary astrocytes. Isoform
CC 3 is most strongly induced in the former case, isoform 1 in the latter
CC case.
CC -!- DOMAIN: The PPxY motif mediates interaction with WWOX. {ECO:0000250}.
CC -!- PTM: Sumoylated on Lys-10; which inhibits transcriptional activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AP-2 family. {ECO:0000305}.
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DR EMBL; X74216; CAA52292.1; -; mRNA.
DR EMBL; BC018226; AAH18226.1; -; mRNA.
DR EMBL; BC007471; AAH07471.1; -; mRNA.
DR EMBL; U17285; AAA85681.1; -; mRNA.
DR EMBL; U17291; AAA85678.1; -; Genomic_DNA.
DR EMBL; U17289; AAA85678.1; JOINED; Genomic_DNA.
DR EMBL; U17286; AAA85682.1; -; mRNA.
DR EMBL; U17287; AAA85683.1; -; mRNA.
DR EMBL; U17291; AAA85679.1; -; Genomic_DNA.
DR EMBL; U17290; AAA85679.1; JOINED; Genomic_DNA.
DR EMBL; U17288; AAA85684.1; -; mRNA.
DR EMBL; U17291; AAA85680.1; -; Genomic_DNA.
DR EMBL; AK013900; BAB29047.1; -; mRNA.
DR EMBL; X57012; CAA40331.1; -; mRNA.
DR CCDS; CCDS49243.1; -. [P34056-3]
DR PIR; S42111; S42111.
DR RefSeq; NP_001288603.1; NM_001301674.1.
DR RefSeq; NP_035677.2; NM_011547.4.
DR AlphaFoldDB; P34056; -.
DR BioGRID; 204011; 7.
DR CORUM; P34056; -.
DR IntAct; P34056; 1.
DR STRING; 10090.ENSMUSP00000105822; -.
DR iPTMnet; P34056; -.
DR PhosphoSitePlus; P34056; -.
DR MaxQB; P34056; -.
DR PaxDb; P34056; -.
DR PeptideAtlas; P34056; -.
DR PRIDE; P34056; -.
DR ProteomicsDB; 296054; -. [P34056-1]
DR ProteomicsDB; 296055; -. [P34056-2]
DR ProteomicsDB; 296056; -. [P34056-3]
DR ProteomicsDB; 296057; -. [P34056-4]
DR DNASU; 21418; -.
DR GeneID; 21418; -.
DR KEGG; mmu:21418; -.
DR UCSC; uc007qei.1; mouse. [P34056-4]
DR UCSC; uc011yyq.1; mouse. [P34056-2]
DR CTD; 7020; -.
DR MGI; MGI:104671; Tfap2a.
DR eggNOG; KOG3811; Eukaryota.
DR InParanoid; P34056; -.
DR PhylomeDB; P34056; -.
DR TreeFam; TF313718; -.
DR Reactome; R-MMU-8864260; Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors.
DR Reactome; R-MMU-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors.
DR Reactome; R-MMU-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
DR BioGRID-ORCS; 21418; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Tfap2a; mouse.
DR PRO; PR:P34056; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P34056; protein.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; TAS:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0140536; F:nuclear receptor corepressor activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0021506; P:anterior neuropore closure; IMP:MGI.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071281; P:cellular response to iron ion; ISS:UniProtKB.
DR GO; GO:0061303; P:cornea development in camera-type eye; IMP:MGI.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:MGI.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:UniProtKB.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:UniProtKB.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IMP:UniProtKB.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0021884; P:forebrain neuron development; IMP:MGI.
DR GO; GO:0035136; P:forelimb morphogenesis; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR GO; GO:0003334; P:keratinocyte development; IGI:MGI.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0060235; P:lens induction in camera-type eye; IMP:MGI.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0072210; P:metanephric nephron development; IEP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:UniProtKB.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IEP:UniProtKB.
DR GO; GO:0014032; P:neural crest cell development; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR GO; GO:0021623; P:oculomotor nerve formation; IMP:UniProtKB.
DR GO; GO:0003409; P:optic cup structural organization; IMP:UniProtKB.
DR GO; GO:0003404; P:optic vesicle morphogenesis; IMP:UniProtKB.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0070172; P:positive regulation of tooth mineralization; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR GO; GO:0007423; P:sensory organ development; IEP:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0043588; P:skin development; IGI:MGI.
DR GO; GO:0048485; P:sympathetic nervous system development; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0021559; P:trigeminal nerve development; IMP:UniProtKB.
DR InterPro; IPR004979; TF_AP2.
DR InterPro; IPR008121; TF_AP2_alpha_N.
DR InterPro; IPR013854; TF_AP2_C.
DR PANTHER; PTHR10812; PTHR10812; 1.
DR Pfam; PF03299; TF_AP-2; 1.
DR PRINTS; PR01749; AP2ATNSCPFCT.
DR PRINTS; PR01748; AP2TNSCPFCT.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..437
FT /note="Transcription factor AP-2-alpha"
FT /id="PRO_0000184797"
FT REGION 14..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..410
FT /note="H-S-H (helix-span-helix), dimerization"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT REGION 414..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 57..62
FT /note="PPxY motif"
FT COMPBIAS 23..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 10
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P05549"
FT VAR_SEQ 1..15
FT /note="MLWKLTDNIKYEDCE -> MLVHSFSAM (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006402"
FT VAR_SEQ 1..15
FT /note="MLWKLTDNIKYEDCE -> MNSVVVDTPYFGGLPTLGLWNGFSRVVEALRLI
FT SSSPSRLAFFQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006403"
FT VAR_SEQ 16..160
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006404"
FT CONFLICT 38
FT /note="P -> S (in Ref. 2; AAH07471)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="A -> G (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 158..159
FT /note="DV -> RL (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="Missing (in Ref. 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 47971 MW; 901F456EE07AE69C CRC64;
MLWKLTDNIK YEDCEDRHDG TSNGTARLPQ LGTVGQSPYT SAPPLSHTPN ADFQPPYFPP
PYQPIYPQSQ DPYSHVNDPY SLNPLHAQPQ PQHPGWPGQR QSQESGLLHT HRGLPHQLSG
LDPRRDYRRH EDLLHGPHAL GSGLGDLPIH SLPHAIEDVP HVEDPGINIP DQTVIKKGPV
SLSKSNSNAV SAIPINKDNL FGGVVNPNEV FCSVPGRLSL LSSTSKYKVT VAEVQRRLSP
PECLNASLLG GVLRRAKSKN GGRSLREKLD KIGLNLPAGR RKAANVTLLT SLVEGEAVHL
ARDFGYVCET EFPAKAVAEF LNRQHSDPNE QVARKNMLLA TKQICKEFTD LLAQDRSPLG
NSRPNPILEP GIQSCLTHFN LISHGFGSPA VCAAVTALQN YLTEALKAMD KMYLSNNPNS
HTDNSAKSSD KEEKHRK
