ARI4A_MOUSE
ID ARI4A_MOUSE Reviewed; 1261 AA.
AC F8VPQ2; B2RXT8; B2RY61; Q05CI2; Q6PE90;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=AT-rich interactive domain-containing protein 4A {ECO:0000303|PubMed:15922553, ECO:0000312|MGI:MGI:2444354};
DE Short=ARID domain-containing protein 4A;
DE AltName: Full=Retinoblastoma-binding protein 1 {ECO:0000303|PubMed:15922553};
GN Name=Arid4a {ECO:0000303|PubMed:15922553, ECO:0000312|MGI:MGI:2444354};
GN Synonyms=Rbbp1 {ECO:0000303|PubMed:15922553},
GN Rbp1 {ECO:0000303|PubMed:15922553};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000312|EMBL:AAI58110.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI58110.1};
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] {ECO:0000305}
RP NOMENCLATURE.
RX PubMed=15922553; DOI=10.1016/j.ygeno.2005.03.013;
RA Wilsker D., Probst L., Wain H.M., Maltais L., Tucker P.W., Moran E.;
RT "Nomenclature of the ARID family of DNA-binding proteins.";
RL Genomics 86:242-251(2005).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ARID4B, AND DISRUPTION PHENOTYPE.
RX PubMed=17043311; DOI=10.1101/gad.1452206;
RA Wu M.Y., Tsai T.F., Beaudet A.L.;
RT "Deficiency of Rbbp1/Arid4a and Rbbp1l1/Arid4b alters epigenetic
RT modifications and suppresses an imprinting defect in the PWS/AS domain.";
RL Genes Dev. 20:2859-2870(2006).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18728284; DOI=10.1093/jnci/djn253;
RA Wu M.Y., Eldin K.W., Beaudet A.L.;
RT "Identification of chromatin remodeling genes Arid4a and Arid4b as leukemia
RT suppressor genes.";
RL J. Natl. Cancer Inst. 100:1247-1259(2008).
RN [6] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH AR, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23487765; DOI=10.1073/pnas.1218318110;
RA Wu R.C., Jiang M., Beaudet A.L., Wu M.Y.;
RT "ARID4A and ARID4B regulate male fertility, a functional link to the AR and
RT RB pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:4616-4621(2013).
CC -!- FUNCTION: DNA-binding protein which modulates activity of several
CC transcription factors including RB1 (retinoblastoma-associated protein)
CC and AR (androgen receptor) (PubMed:17043311, PubMed:23487765). May
CC function as part of an mSin3A repressor complex (By similarity). Has no
CC intrinsic transcriptional activity (PubMed:23487765). Plays a role in
CC the regulation of epigenetic modifications at the PWS/AS imprinting
CC center near the SNRPN promoter, where it might function as part of a
CC complex with RB1 and ARID4B (PubMed:17043311). Involved in
CC spermatogenesis, together with ARID4B, where it acts as a
CC transcriptional coactivator for AR and enhances expression of genes
CC required for sperm maturation (PubMed:23487765). Regulates expression
CC of the tight junction protein CLDN3 in the testis, which is important
CC for integrity of the blood-testis barrier (PubMed:23487765). Plays a
CC role in myeloid homeostasis where it regulates the histone methylation
CC state of bone marrow cells and expression of various genes involved in
CC hematopoiesis (PubMed:18728284). May function as a leukemia suppressor
CC (PubMed:18728284). {ECO:0000250|UniProtKB:P29374,
CC ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:18728284,
CC ECO:0000269|PubMed:23487765}.
CC -!- SUBUNIT: Identified in mSin3A corepressor complexes together with
CC SIN3A, SIN3B, RBBP4, RBBP7, SAP30, BRMS1, HDAC1 and HDAC2 (By
CC similarity). Interacts with BRMS1 (By similarity). Interacts with RB1
CC (By similarity). Interacts with ARID4B (PubMed:17043311). Interacts
CC with AR (PubMed:23487765). {ECO:0000250|UniProtKB:P29374,
CC ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:23487765}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255,
CC ECO:0000305|PubMed:17043311, ECO:0000305|PubMed:23487765}.
CC -!- TISSUE SPECIFICITY: Expressed in Sertoli cells of the testis.
CC {ECO:0000269|PubMed:23487765}.
CC -!- DOMAIN: The function of the Tudor-knot domain, also named chromodomain-
CC like, is uncertain. One study suggests that it mediates binding to
CC lysine-methylated histone tails, with strongest affinity for H4K20me3
CC and H3K36me3. However, another study failed to find any interaction
CC between this domain and histone H4K20me3 peptide.
CC {ECO:0000250|UniProtKB:P29374}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile, although females have reduced
CC fertility (PubMed:17043311, PubMed:18728284). At two months of age,
CC animals show abnormal blood cell production accompanied by mild anemia,
CC leukopenia and thrombocytopenia. Hematologic abnormalities become
CC progressively more severe with age (PubMed:18728284). Monocytosis is
CC observed at 5 months onwards, along with splenomegaly and hepatomegaly
CC (PubMed:18728284). Approximately 12% of animals develop acute myeloid
CC leukemia (AML) and/or myeloid sarcoma (PubMed:18728284). Mortality
CC increases rapidly from age 6 months onwards, with no survival past 22
CC months (PubMed:18728284). Expansion of hematopoietic stem cell and
CC common myeloid progenitor cell populations, and their downstream
CC lineage, is observed in bone marrow and spleen; the effect is most
CC significant in spleen (PubMed:18728284). Bone marrow cells show altered
CC patterns of histone methylation and significantly increased levels of
CC both H3K4me3 and H3K9me3 (PubMed:18728284). Expression of HOXB3, HOXB5,
CC HOXB6, HOXB8 and PITX2 in bone marrow cells is reduced
CC (PubMed:18728284). No effect on histone methylation at the PWS/AS
CC imprinting center (PubMed:17043311). Double knockouts with ARID4B
CC heterozygotes show a more severe hematologic phenotype with 83% of
CC animals progressing to AML, and with earlier age of onset
CC (PubMed:18728284). In bone marrow cells, expression of FOXP3 is
CC significantly reduced (PubMed:18728284). Males show progressive
CC reduction in fertility from 2 months of age onwards, with reduced
CC testis size and variable defects in seminal vesicle formation
CC (PubMed:23487765). Spermatogenesis is partially blocked from the meiois
CC II stage onwards leading to reduced numbers of mature spermatozoa
CC (PubMed:23487765). Expression in testis of CLDN3, an androgen receptor-
CC regulated gene, is significantly reduced (PubMed:23487765). Expression
CC of PTGDS is also reduced, whereas expression of INHA and EMB is
CC moderately increased (PubMed:23487765). Maternal-specific
CC trimethylation of H4K20 and H3K9 at the PWS/AS imprinting center is
CC significantly reduced (PubMed:17043311). {ECO:0000269|PubMed:17043311,
CC ECO:0000269|PubMed:18728284, ECO:0000269|PubMed:23487765}.
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DR EMBL; AC112794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025436; AAH25436.1; -; mRNA.
DR EMBL; BC058209; AAH58209.1; -; mRNA.
DR EMBL; BC157975; AAI57976.1; -; mRNA.
DR EMBL; BC158109; AAI58110.1; -; mRNA.
DR CCDS; CCDS36471.1; -.
DR RefSeq; NP_001074664.1; NM_001081195.1.
DR RefSeq; XP_017170546.1; XM_017315057.1.
DR AlphaFoldDB; F8VPQ2; -.
DR SMR; F8VPQ2; -.
DR ComplexPortal; CPX-3441; SIN3A histone deacetylase complex, ES cell-specific variant.
DR ComplexPortal; CPX-3443; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3444; SIN3B histone deacetylase complex.
DR STRING; 10090.ENSMUSP00000035512; -.
DR iPTMnet; F8VPQ2; -.
DR PhosphoSitePlus; F8VPQ2; -.
DR EPD; F8VPQ2; -.
DR jPOST; F8VPQ2; -.
DR MaxQB; F8VPQ2; -.
DR PaxDb; F8VPQ2; -.
DR PRIDE; F8VPQ2; -.
DR ProteomicsDB; 313983; -.
DR Antibodypedia; 11317; 60 antibodies from 19 providers.
DR DNASU; 238247; -.
DR Ensembl; ENSMUST00000046305; ENSMUSP00000035512; ENSMUSG00000048118.
DR GeneID; 238247; -.
DR KEGG; mmu:238247; -.
DR UCSC; uc007nud.1; mouse.
DR CTD; 5926; -.
DR MGI; MGI:2444354; Arid4a.
DR VEuPathDB; HostDB:ENSMUSG00000048118; -.
DR eggNOG; KOG2744; Eukaryota.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00940000156159; -.
DR HOGENOM; CLU_007419_1_0_1; -.
DR InParanoid; F8VPQ2; -.
DR OMA; MSPHIKD; -.
DR OrthoDB; 329541at2759; -.
DR PhylomeDB; F8VPQ2; -.
DR TreeFam; TF106427; -.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR BioGRID-ORCS; 238247; 12 hits in 78 CRISPR screens.
DR ChiTaRS; Arid4a; mouse.
DR PRO; PR:F8VPQ2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; F8VPQ2; protein.
DR Bgee; ENSMUSG00000048118; Expressed in animal zygote and 223 other tissues.
DR ExpressionAtlas; F8VPQ2; baseline and differential.
DR Genevisible; F8VPQ2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0097368; P:establishment of Sertoli cell barrier; IGI:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:MGI.
DR GO; GO:0036124; P:histone H3-K9 trimethylation; IMP:MGI.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR012603; RBB1NT.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR025995; Tudor-knot.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF08169; RBB1NT; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Differentiation; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1261
FT /note="AT-rich interactive domain-containing protein 4A"
FT /id="PRO_0000444995"
FT DOMAIN 309..401
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 579..631
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT REGION 4..121
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT REGION 142..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..968
FT /note="Retinoblastoma protein binding"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT REGION 1067..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT CROSSLNK 723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT CROSSLNK 743
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P29374"
FT CONFLICT 419..420
FT /note="EE -> KK (in Ref. 2; AAH25436)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="D -> E (in Ref. 2; AAI58110)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="Missing (in Ref. 2; AAI57976)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="I -> K (in Ref. 2; AAH58209)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="A -> G (in Ref. 2; AAI57976)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="F -> L (in Ref. 2; AAI57976)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="T -> S (in Ref. 2; AAI57976)"
FT /evidence="ECO:0000305"
FT CONFLICT 1138
FT /note="S -> P (in Ref. 2; AAI57976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1261 AA; 142055 MW; 4392BF421E3A00B8 CRC64;
MKAADEPAYL TVGTDVSAKY RGAFCEAKIK TVKRLVKVKV LLKQDNTTQL VQDDQVKGPL
RVGAIVETRT SDGSIQEAII SKLTDASWYT VVFDDGDERT LRRTSLCLKG ERHFAESETL
DQLPLTNPEH FGTPVIAKKT NRGRRSSLPI TEDEKEEESS EEEDEDKRRL NDELLGKVVS
VASTAESTGW YPALVVSPSC NDDVTVKKDQ CLVRSFIDSK FYSIARKDIK ELDILTLPES
ELCARPGLRR ASVFLKGRIV PDNWKMDISE ILESSSSDDE ECPAEEHEEE KEKEAKKEEE
ELPEEELDPE ERDNFLQQLY KFMEDRGTPI NKPPVLGYKD LNLFKLFRLV YHQGGCGNID
SGAVWKQIYM DLGIPILNSA ASYNVKTAYR KYLYGFEEYC RSANIQFRTI HHHEPKVKEE
KKDFEDSMDE ALKEAPEMPL LDVKSEPEEN TDSNSESDRE DTELKSPRGR RKIVRDANCI
KKEIEEEKIE DKFLRDDLEN KDAGDDDDDG DPAAKREHEL LFGRKSTPKN KEKKIKKPED
SERDSDEEEE KSQEREETES RCDSEGEDEE DDTEPCLTGT KVKVKYGRGK TQKIYEASIK
STEMDDGEIL YLVHYYGWNV RYDEWVKADR IIWPLDKGGP KKKQKKKVKN KEDSEKDEKR
DEERQKSKRG RPPLKSTFSP NMPYSLSKTS NSEGKSDSCS SDSEADDQLE KSSGGEDLSP
DVKEELEKNE NAHDDKLDEE NPKIVHISKE NDRTQAQPSD TLTVEAGDSD QIVHIFGDKV
DQVEEFKKQV EKSPKGKGRR SKTKDLSLEL IKISPFGQEE AGSEAHGDVH SLEFSSLECK
NFSSTEDDID PYEKEKKLKR KILGQQSPEK KLRLDNGMEM TTGVSQERSD DGAGAEGMKG
AHVEQHFETE GEGMPSLTAE PDQGLQELTS EKSDSPAEEE PVHTPLKEEE DAMPLIGPET
LVCHEVDLDD LDEKDKTSIE DVVVEGSESN SLASVPPALP PVAQHNFSVA SPLTLSQDES
RSIKSESDIT IEVDSIAEES QEGLCERESA NGFEASVASG ACSIIAHERE SREKGQKRPS
DGNSGLIAKK QKRTPKRTSA AAKTEKNGAG QSSDSEDLPA MDSSSNCTPV KRLTLPKSQK
LPRSPARTSP HIKDAEKEKH REKHPNSSPR TYKWSFQLNE LDNMNSTERI SFLQEKLQEI
RKYYMSLKSE VATIDRRRKR LKKKDREVSH AGASMSSASS DTGMSPSSSS PPQNVLAVEC
R
