BAP1_MOUSE
ID BAP1_MOUSE Reviewed; 728 AA.
AC Q99PU7; Q3TCR6; Q6ZQE6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase BAP1;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q92560};
DE AltName: Full=BRCA1-associated protein 1;
DE AltName: Full=Ubiquitin C-terminal hydrolase X4;
DE Short=UCH-X4;
GN Name=Bap1; Synonyms=Kiaa0272;
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].
RA Mizuta R.;
RT "Ubiquitin C-terminal hydrolase.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetal brain;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=9528852; DOI=10.1038/sj.onc.1201861;
RA Jensen D.E., Proctor M., Marquis S.T., Gardner H.P., Ha S.I., Chodosh L.A.,
RA Ishov A.M., Tommerup N., Vissing H., Sekido Y., Minna J., Borodovsky A.,
RA Schultz D.C., Wilkinson K.D., Maul G.G., Barlev N., Berger S.,
RA Prendergast G.C., Rauscher F.J. III;
RT "BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING finger and
RT enhances BRCA1-mediated cell growth suppression.";
RL Oncogene 16:1097-1112(1998).
RN [6]
RP MUTAGENESIS OF CYS-91 AND 716-ARG--ARG-721.
RX PubMed=18757409; DOI=10.1158/0008-5472.can-08-0365;
RA Ventii K.H., Devi N.S., Friedrich K.L., Chernova T.A., Tighiouart M.,
RA Van Meir E.G., Wilkinson K.D.;
RT "BRCA1-associated protein-1 is a tumor suppressor that requires
RT deubiquitinating activity and nuclear localization.";
RL Cancer Res. 68:6953-6962(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369 AND SER-395, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Pancreas, 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: Deubiquitinating enzyme that plays a key role in chromatin by
CC mediating deubiquitination of histone H2A and HCFC1. Catalytic
CC component of the PR-DUB complex, a complex that specifically mediates
CC deubiquitination of histone H2A monoubiquitinated at 'Lys-119'
CC (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B.
CC Acts as a regulator of cell growth by mediating deubiquitination of
CC HCFC1 N-terminal and C-terminal chains, with some specificity toward
CC 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked
CC polyubiquitin chains. Deubiquitination of HCFC1 does not lead to
CC increase stability of HCFC1. Interferes with the BRCA1 and BARD1
CC heterodimer activity by inhibiting their ability to mediate
CC ubiquitination and autoubiquitination. It however does not mediate
CC deubiquitination of BRCA1 and BARD1. Able to mediate
CC autodeubiquitination via intramolecular interactions to couteract
CC monoubiquitination at the nuclear localization signal (NLS), thereby
CC protecting it from cytoplasmic sequestration. Acts as a tumor
CC suppressor. {ECO:0000250|UniProtKB:Q92560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q92560};
CC -!- SUBUNIT: Component of the PR-DUB complex, at least composed of BAP1 and
CC ASXL1. Interacts with BRCA1 (via the RING finger). Interacts (via HBM-
CC like motif) with HCFC1. Interacts (when phosphorylated at Thr-492) with
CC FOXK1. Interacts (when phosphorylated at Thr-492) with FOXK2; leading
CC to recruit the PR-DUB complex and repress FOXK2 target genes.
CC {ECO:0000250|UniProtKB:Q92560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92560}. Nucleus
CC {ECO:0000250|UniProtKB:Q92560}. Note=Mainly nuclear. Binds to
CC chromatin. Localizes to the cytoplasm when monoubiquitinated by the
CC E2/E3 hybrid ubiquitin-protein ligase UBE2O.
CC {ECO:0000250|UniProtKB:Q92560}.
CC -!- TISSUE SPECIFICITY: Highly expressed in mammary glands, testis and
CC ovary. Up-regulated in mammary glands during puberty, pregnancy, and as
CC a result of parity. {ECO:0000269|PubMed:9528852}.
CC -!- PTM: Ubiquitinated: monoubiquitinated at multiple site of its nuclear
CC localization signal (NLS) BY UBE2O, leading to cytoplasmic retention.
CC Able to mediate autodeubiquitination via intramolecular interactions to
CC couteract cytoplasmic retention. {ECO:0000250|UniProtKB:Q92560}.
CC -!- MISCELLANEOUS: Has the ability to ability to suppress tumorigenicity
CC when expressed in NCI-H226 cells. {ECO:0000305|PubMed:18757409}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97918.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB047820; BAB32976.1; -; mRNA.
DR EMBL; AK129108; BAC97918.1; ALT_INIT; mRNA.
DR EMBL; AK170576; BAE41889.1; -; mRNA.
DR EMBL; BC050901; AAH50901.1; -; mRNA.
DR CCDS; CCDS26910.1; -.
DR RefSeq; NP_081364.1; NM_027088.2.
DR AlphaFoldDB; Q99PU7; -.
DR SMR; Q99PU7; -.
DR BioGRID; 222625; 28.
DR ComplexPortal; CPX-423; PR-DUB complex.
DR IntAct; Q99PU7; 19.
DR STRING; 10090.ENSMUSP00000022458; -.
DR MEROPS; C12.004; -.
DR iPTMnet; Q99PU7; -.
DR PhosphoSitePlus; Q99PU7; -.
DR EPD; Q99PU7; -.
DR jPOST; Q99PU7; -.
DR MaxQB; Q99PU7; -.
DR PaxDb; Q99PU7; -.
DR PeptideAtlas; Q99PU7; -.
DR PRIDE; Q99PU7; -.
DR ProteomicsDB; 277110; -.
DR Antibodypedia; 3812; 454 antibodies from 37 providers.
DR DNASU; 104416; -.
DR Ensembl; ENSMUST00000022458; ENSMUSP00000022458; ENSMUSG00000021901.
DR GeneID; 104416; -.
DR KEGG; mmu:104416; -.
DR UCSC; uc007sxh.1; mouse.
DR CTD; 8314; -.
DR MGI; MGI:1206586; Bap1.
DR VEuPathDB; HostDB:ENSMUSG00000021901; -.
DR eggNOG; KOG2778; Eukaryota.
DR GeneTree; ENSGT00940000156388; -.
DR HOGENOM; CLU_018316_5_0_1; -.
DR InParanoid; Q99PU7; -.
DR OMA; VLKMNRQ; -.
DR OrthoDB; 1363547at2759; -.
DR PhylomeDB; Q99PU7; -.
DR TreeFam; TF313976; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR BioGRID-ORCS; 104416; 28 hits in 78 CRISPR screens.
DR ChiTaRS; Bap1; mouse.
DR PRO; PR:Q99PU7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q99PU7; protein.
DR Bgee; ENSMUSG00000021901; Expressed in rostral migratory stream and 256 other tissues.
DR ExpressionAtlas; Q99PU7; baseline and differential.
DR Genevisible; Q99PU7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035517; C:PR-DUB complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035726; P:common myeloid progenitor cell proliferation; IMP:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0043249; P:erythrocyte maturation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0030851; P:granulocyte differentiation; IMP:MGI.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0070661; P:leukocyte proliferation; IMP:MGI.
DR GO; GO:0061519; P:macrophage homeostasis; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0033028; P:myeloid cell apoptotic process; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR GO; GO:0030223; P:neutrophil differentiation; IMP:MGI.
DR GO; GO:0043363; P:nucleate erythrocyte differentiation; IMP:MGI.
DR GO; GO:0036344; P:platelet morphogenesis; IMP:MGI.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0010035; P:response to inorganic substance; IMP:MGI.
DR GO; GO:0002574; P:thrombocyte differentiation; IMP:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.532.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Cytoplasm; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..728
FT /note="Ubiquitin carboxyl-terminal hydrolase BAP1"
FT /id="PRO_0000211070"
FT REGION 273..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..720
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000250"
FT REGION 702..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 629..660
FT /evidence="ECO:0000255"
FT MOTIF 363..366
FT /note="HBM-like motif"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT MOTIF 716..721
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..728
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:18757409"
FT ACT_SITE 169
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT SITE 184
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 492
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92560"
FT MUTAGEN 91
FT /note="C->A: Abolishes ability to suppress tumorigenicity
FT when expressed in NCI-H226 cells."
FT /evidence="ECO:0000269|PubMed:18757409"
FT MUTAGEN 716..721
FT /note="RRKRSR->AAAAAA: Abolishes ability to suppress
FT tumorigenicity when expressed in NCI-H226 cells."
FT /evidence="ECO:0000269|PubMed:18757409"
FT CONFLICT 725
FT /note="A -> V (in Ref. 2; BAC97918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 80492 MW; 2BDEAFB09CD276DB CRC64;
MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF KWIEERRSRR
KVSTLVDDTS VIDDDIVNNM FFAHQLIPNS CATHALLSVL LNCSNVDLGP TLSRMKDFTK
GFSPESKGYA IGNAPELAKA HNSHARPEPR HLPEKQNGLS AVRTMEAFHF VSYVPITGRL
FELDGLKVYP IDHGPWGEDE EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK
YETRLHVLKV NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKPASS KSPLGLEAGR
TPVASECTQT DGAEEVAGSC PQTTTHSPPS KCKLVVKPPG SSLNGVPPNP APIVQRLPAF
LDNHNYAKSP MQEEEDLAAG VGRSRVPVRA PQQYSEDEDD YEDEDEDVQN TNPAIRYKRK
GTGKPGSLSN SSDGQLSVLQ PNTINVLTEK LQESQKDLSV PLSIKTSSGA GSPAVAVPTH
SQPSPTPSNE STDTASEIGS AFNSPLRSPI RSANPTRPSS PVTSHISKVL FGEDDSLLRV
DCIRYNRAVR DLGPVISTGL LHLAEDGVLS PLALTEGGKG SSPSTRSSQG SQGSSGLEEK
EVVEVTESRD KPGLNRSSEP LSGEKYSPKE LLALLKCVEA EIANYEACLK EEVEKRKKFK
IDDQRRTHNY DEFICTFISM LAQEGMLANL VEQNISVRRR QGVSIGRLHK QRKPDRRKRS
RPYKAKRQ
