BAZ1A_MOUSE
ID BAZ1A_MOUSE Reviewed; 1555 AA.
AC O88379; Q3TKK7; Q3UXF6;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 1A;
DE AltName: Full=Cbp146;
GN Name=Baz1a; Synonyms=Cbp146;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-382.
RC STRAIN=C57BL/6J; TISSUE=Blastocyst, and Egg;
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 18-361.
RX PubMed=9701556; DOI=10.1242/jcs.111.17.2575;
RA Tate P., Lee M., Tweedie S., Skarnes W.C., Bickmore W.A.;
RT "Capturing novel mouse genes encoding chromosomal and other nuclear
RT proteins.";
RL J. Cell Sci. 111:2575-2585(1998).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-732, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; THR-732; SER-962;
RP SER-963; SER-1339; SER-1352 AND SER-1412, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
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).
CC -!- FUNCTION: Regulatory subunit of the ATP-dependent ACF-1 and ACF-5 ISWI
CC chromatin remodeling complexes, which form ordered nucleosome arrays on
CC chromatin and slide edge- and center-positioned histone octamers away
CC from their original location on the DNA template to facilitate access
CC to DNA during DNA-templated processes such as DNA replication,
CC transcription, and repair (By similarity). Both complexes regulate the
CC spacing of nucleosomes along the chromatin and have the ability to
CC slide mononucleosomes to the center of a DNA template in an ATP-
CC dependent manner (By similarity). The ACF-1 ISWI chromatin remodeling
CC complex has a lower ATP hydrolysis rate than the ACF-5 ISWI chromatin
CC remodeling complex (By similarity). Has a role in sensing the length of
CC DNA which flank nucleosomes, which modulates the nucleosome spacing
CC activity of the ACF-5 ISWI chromatin remodeling complex (By
CC similarity). Involved in DNA replication and together with
CC SMARCA5/SNF2H is required for replication of pericentric
CC heterochromatin in S-phase (By similarity). May have a role in nuclear
CC receptor-mediated transcription repression (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRL2}.
CC -!- SUBUNIT: Component of the ACF-1 ISWI chromatin remodeling complex at
CC least composed of SMARCA1 and BAZ1A, which regulates the spacing of
CC histone octamers on the DNA template to facilitate access to DNA (By
CC similarity). Within the ACF-1 ISWI chromatin remodeling complex
CC interacts with SMARCA1; the interaction is direct (By similarity).
CC Component of the ACF-5 ISWI chromatin remodeling complex (also called
CC the ACF complex) at least composed of BAZ1A and SMARCA5/SNF2H, which
CC regulates the spacing of histone octamers on the DNA template to
CC facilitate access to DNA (By similarity). Within the ACF-5 ISWI
CC chromatin remodeling complex interacts with SMARCA5/SNF2H; the
CC interaction is direct (By similarity). Component of the CHRAC ISWI
CC chromatin remodeling complex at least composed of SMARCA5/SNF2H,
CC BAZ1A/ACF1, CHRAC1 and POLE3; the complex preferentially binds DNA
CC through the CHRAC1-POLE3 heterodimer and possesses ATP-dependent
CC nucleosome-remodeling activity (By similarity). Within the complex
CC interacts (via N-terminus) with POLE3-CHRAC1 heterodimer; the
CC interaction is direct and is required for the complex to preferentially
CC bind to DNA (By similarity). Within the complex interacts with
CC SMARCA5/SNF2H; the interaction is direct and promotes the interaction
CC with the POLE3-CHRAC1 heterodimer (By similarity). Interacts with NCOR1
CC (via its RD1 domain); the interaction corepresses a number of NCOR1-
CC regulated genes (By similarity). {ECO:0000250|UniProtKB:Q9NRL2}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Concentrated in pericentric to
CC heterochromatin.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22607.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC138767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK135668; BAE22607.1; ALT_INIT; mRNA.
DR EMBL; AK166955; BAE39138.1; -; mRNA.
DR EMBL; AF033664; AAC32043.1; -; mRNA.
DR AlphaFoldDB; O88379; -.
DR SMR; O88379; -.
DR ComplexPortal; CPX-444; ACF chromatin remodeling complex.
DR ComplexPortal; CPX-858; CHRAC chromatin remodeling complex.
DR IntAct; O88379; 2.
DR STRING; 10090.ENSMUSP00000039757; -.
DR iPTMnet; O88379; -.
DR PhosphoSitePlus; O88379; -.
DR SwissPalm; O88379; -.
DR EPD; O88379; -.
DR jPOST; O88379; -.
DR MaxQB; O88379; -.
DR PaxDb; O88379; -.
DR PeptideAtlas; O88379; -.
DR PRIDE; O88379; -.
DR ProteomicsDB; 273730; -.
DR Antibodypedia; 113; 137 antibodies from 25 providers.
DR Ensembl; ENSMUST00000038926; ENSMUSP00000039757; ENSMUSG00000035021.
DR MGI; MGI:1309478; Baz1a.
DR VEuPathDB; HostDB:ENSMUSG00000035021; -.
DR eggNOG; KOG1245; Eukaryota.
DR GeneTree; ENSGT00940000158135; -.
DR InParanoid; O88379; -.
DR PhylomeDB; O88379; -.
DR TreeFam; TF316326; -.
DR ChiTaRS; Baz1a; mouse.
DR PRO; PR:O88379; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O88379; protein.
DR Bgee; ENSMUSG00000035021; Expressed in spermatocyte and 175 other tissues.
DR ExpressionAtlas; O88379; baseline and differential.
DR Genevisible; O88379; MM.
DR GO; GO:0016590; C:ACF complex; ISO:MGI.
DR GO; GO:0008623; C:CHRAC; ISO:MGI.
DR GO; GO:0000228; C:nuclear chromosome; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0006261; P:DNA-templated DNA replication; ISO:MGI.
DR GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0031445; P:regulation of heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd05504; Bromo_Acf1_like; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR037325; Acf1_Bromo.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR013136; WSTF_Acf1_Cbp146.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS51136; WAC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Bromodomain; Coiled coil; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1555
FT /note="Bromodomain adjacent to zinc finger domain protein
FT 1A"
FT /id="PRO_0000211168"
FT DOMAIN 22..128
FT /note="WAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00475"
FT DOMAIN 422..488
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 1445..1515
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 1149..1199
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..133
FT /note="Required for interaction with NCOR1"
FT /evidence="ECO:0000250"
FT REGION 1..128
FT /note="Required for association with the CHRAC1/POLE3
FT complex"
FT /evidence="ECO:0000250"
FT REGION 1..128
FT /note="Required for interaction with the CHRAC1-POLE3
FT heterodimer. Required for interaction with the CHRAC1-POLE3
FT heterodimer"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT REGION 652..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..935
FT /note="Interaction with SMARCA5"
FT /evidence="ECO:0000250"
FT REGION 668..935
FT /note="Required for interaction with SMARCA5 and formation
FT of the CHRAC ISWI chromatin remodeling complex"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT REGION 843..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 635..701
FT /evidence="ECO:0000255"
FT COILED 773..798
FT /evidence="ECO:0000255"
FT COMPBIAS 652..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 963
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT MOD_RES 1320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT MOD_RES 1401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT MOD_RES 1412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT MOD_RES 1546
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT CROSSLNK 954
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NRL2"
FT CONFLICT 18..20
FT /note="LRP -> EFR (in Ref. 3; AAC32043)"
FT /evidence="ECO:0000305"
FT CONFLICT 148..149
FT /note="FA -> LL (in Ref. 2; BAE22607)"
FT /evidence="ECO:0000305"
FT CONFLICT 342..361
FT /note="KEDKEKKREELKKMVEEERL -> AGILTPDQLVMVATGAQLEF (in
FT Ref. 3; AAC32043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1555 AA; 178459 MW; F7BE6227A420A842 CRC64;
MPLLHRKPFV RQKPPGDLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP
GLTYQEALES ERKARQNLQS FPEPLIIPVL YLTNLTRRSR LHEICDDIFA YVKDRYFVEE
TVEVIRNNGT RLQCRILEVL PPLHQNGFAN GHLSSADGET IVISDSDDSE TQSSSFHHGK
KKDAIDPLLF RYRVQPTKKE MYESAVVKAT QISRRKHLFS RDKLKLFLKQ HCEAQDGVIK
IKASSFSAYN IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRISFGQEDS IASKQTAARY
RNKAIKERDK LLKQEEMRAL AFEKAKLKRE RADALEARKR EKEDKEKKRE ELKKMVEEER
LKKKEEKERL KIEREKEREK LREEKRKYME YLKQWSKPRE DMECDDLKEL PEPTPVKTRL
PPEVFGDALM VLEFLNAFGE LFDLQDEFPE GVTLAEVLEE ALVGNDSEGP LCELLFFFLT
AIFQAMAEEE EEVAKEQITD ADTKDLTEAL DEDADPTKSA LSAVAALAAA WPQLHQGCSL
KSLDLDSCTL SEILRLHILA SGADVTSANA KYRYQKRGGF DATDDACMEL RLSNPSLVKK
LSSTSVYDLT PGEKMKILHA LCGKLLTLVS TRDFIEDYVD VLRQAKQEFR ELKAEQHRKE
REATAARIRR RKEEKLKEQE QKMKEKQEKL KEDEQRNSAA VPGYGEEERE DFDTSTENKN
IEQKDLDPDV VTEDEDDPGS HKRSRRGKVG QTAVKQCIKQ EEMNYCIKQE PLSADAEEAL
RQEQQQKEKE LLDKIQSAIA CTNIFPLGRD RLYRRYWIFP SIPGLFIEED YSGLTEDMLL
PRPSSFHNNA QPRDPQVSIK TEESFLSEST SSLDQGPFDD SVLLPKPVHK PNRWCFYSSC
AQLDQLIDAL NSRGHRESAL KETLLQEKSR ICAQLAHFSE EKFHFSDKPQ ADSKPVSSRG
RSSGACDISQ MSAERQLELR LRDFLLDIED RIYQGTLGAI KVTDRQVWRS ALENGRYELL
SEESKENGVI KTVNEDVEEM EMEQARVIVR DRLLGIKTET PSTISTSAST PQSVSNVVHY
LALALFQIEQ GIERRFLKAP LDGNDSGRSY KTVLDRWRES LLSSASLSQV FLHLSTLDRS
VMWSKSILNA RCKICRKKGD AENMVLCDGC DRGHHTYCVR PKLKAVPDGD WFCPECRPKQ
RSRRLSSRQR PSLESDEEME EGMEDDDDEV DDDDEEGQSE EEEYEVEQDE EDSDDDEALS
PPKRGRPQVR LPIKTKGRFG PSFPSRSQRQ DPGRYPSRSQ QSTPKNTAKS ASKNLRKTRS
APPTETRSLR VGSRSTRHSP SALQDVFVEL LSPHSKRRGR KGADHTPEHS PSFTNFRVST
SRSSRQLIPL NTAESLSLQH SESKRRGRKR QSTESSPVPL NRRSSGRQGG VHELSAFEQL
VVELVRHDDS WPFLKLVSKI QVPDYYDIIK KPIALNIIRE KVNKCEYKLA SEFIDDIELM
FSNCFEYNPR NTSEAKAGTR LQAFFHIQAQ KLGLHVSPST VDQVSTPLAA KKSRI
