NAA25_HUMAN
ID NAA25_HUMAN Reviewed; 972 AA.
AC Q14CX7; A0JLU7; Q6MZH1; Q7Z4N6; Q9H911;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=N-alpha-acetyltransferase 25, NatB auxiliary subunit;
DE AltName: Full=Mitochondrial distribution and morphology protein 20;
DE AltName: Full=N-terminal acetyltransferase B complex subunit MDM20;
DE Short=NatB complex subunit MDM20;
DE AltName: Full=N-terminal acetyltransferase B complex subunit NAA25;
DE AltName: Full=p120;
GN Name=NAA25; Synonyms=C12orf30, MDM20, NAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hotokezaka H., Wiedmann M.;
RT "P120 which associates with nascent polypeptide chain.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-972.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP FUNCTION, INTERACTION WITH NAT5, AND SUBCELLULAR LOCATION.
RX PubMed=18570629; DOI=10.1042/bj20080658;
RA Starheim K.K., Arnesen T., Gromyko D., Ryningen A., Varhaug J.E.,
RA Lillehaug J.R.;
RT "Identification of the human N(alpha)-acetyltransferase complex B (hNatB):
RT a complex important for cell-cycle progression.";
RL Biochem. J. 415:325-331(2008).
RN [6]
RP NOMENCLATURE.
RX PubMed=19660095; DOI=10.1186/1753-6561-3-s6-s2;
RA Polevoda B., Arnesen T., Sherman F.;
RT "A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature,
RT subunits and substrates.";
RL BMC Proc. 3:S2-S2(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-789.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Non-catalytic subunit of the NatB complex which catalyzes
CC acetylation of the N-terminal methionine residues of peptides beginning
CC with Met-Asp-Glu. May play a role in normal cell-cycle progression.
CC {ECO:0000269|PubMed:18570629}.
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex
CC which is composed of NAA20 and NAA25.
CC -!- INTERACTION:
CC Q14CX7; P61599: NAA20; NbExp=2; IntAct=EBI-1048503, EBI-1055023;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18570629}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14CX7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14CX7-2; Sequence=VSP_026629, VSP_026630;
CC -!- SIMILARITY: Belongs to the MDM20/NAA25 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14432.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAE46062.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB054990; BAC80174.1; -; mRNA.
DR EMBL; BX641140; CAE46062.1; ALT_INIT; mRNA.
DR EMBL; BC034357; AAH34357.1; -; mRNA.
DR EMBL; BC113585; AAI13586.1; -; mRNA.
DR EMBL; BC113587; AAI13588.1; -; mRNA.
DR EMBL; AK023151; BAB14432.1; ALT_INIT; mRNA.
DR CCDS; CCDS9159.1; -. [Q14CX7-1]
DR RefSeq; NP_079229.2; NM_024953.3. [Q14CX7-1]
DR PDB; 6VP9; EM; 3.46 A; B=1-972.
DR PDB; 7STX; EM; 3.14 A; B=45-972.
DR PDBsum; 6VP9; -.
DR PDBsum; 7STX; -.
DR AlphaFoldDB; Q14CX7; -.
DR SMR; Q14CX7; -.
DR BioGRID; 123072; 56.
DR ComplexPortal; CPX-6270; NatB N-alpha-acetyltransferase complex.
DR DIP; DIP-50826N; -.
DR IntAct; Q14CX7; 10.
DR STRING; 9606.ENSP00000261745; -.
DR GlyGen; Q14CX7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14CX7; -.
DR MetOSite; Q14CX7; -.
DR PhosphoSitePlus; Q14CX7; -.
DR SwissPalm; Q14CX7; -.
DR BioMuta; NAA25; -.
DR DMDM; 121948761; -.
DR EPD; Q14CX7; -.
DR jPOST; Q14CX7; -.
DR MassIVE; Q14CX7; -.
DR MaxQB; Q14CX7; -.
DR PaxDb; Q14CX7; -.
DR PeptideAtlas; Q14CX7; -.
DR PRIDE; Q14CX7; -.
DR ProteomicsDB; 60335; -. [Q14CX7-1]
DR ProteomicsDB; 60336; -. [Q14CX7-2]
DR Antibodypedia; 50891; 118 antibodies from 20 providers.
DR DNASU; 80018; -.
DR Ensembl; ENST00000261745.9; ENSP00000261745.4; ENSG00000111300.10. [Q14CX7-1]
DR GeneID; 80018; -.
DR KEGG; hsa:80018; -.
DR MANE-Select; ENST00000261745.9; ENSP00000261745.4; NM_024953.4; NP_079229.2.
DR UCSC; uc001ttm.4; human. [Q14CX7-1]
DR CTD; 80018; -.
DR DisGeNET; 80018; -.
DR GeneCards; NAA25; -.
DR HGNC; HGNC:25783; NAA25.
DR HPA; ENSG00000111300; Low tissue specificity.
DR MIM; 612755; gene.
DR neXtProt; NX_Q14CX7; -.
DR OpenTargets; ENSG00000111300; -.
DR PharmGKB; PA165513030; -.
DR VEuPathDB; HostDB:ENSG00000111300; -.
DR eggNOG; KOG2053; Eukaryota.
DR GeneTree; ENSGT00950000183174; -.
DR HOGENOM; CLU_008075_0_0_1; -.
DR InParanoid; Q14CX7; -.
DR OMA; ICRRMWA; -.
DR OrthoDB; 1022953at2759; -.
DR PhylomeDB; Q14CX7; -.
DR TreeFam; TF315103; -.
DR BioCyc; MetaCyc:ENSG00000111300-MON; -.
DR BRENDA; 2.3.1.254; 2681.
DR PathwayCommons; Q14CX7; -.
DR SignaLink; Q14CX7; -.
DR SIGNOR; Q14CX7; -.
DR BioGRID-ORCS; 80018; 580 hits in 1092 CRISPR screens.
DR ChiTaRS; NAA25; human.
DR GenomeRNAi; 80018; -.
DR Pharos; Q14CX7; Tbio.
DR PRO; PR:Q14CX7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q14CX7; protein.
DR Bgee; ENSG00000111300; Expressed in tibialis anterior and 179 other tissues.
DR ExpressionAtlas; Q14CX7; baseline and differential.
DR Genevisible; Q14CX7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0031416; C:NatB complex; IPI:ComplexPortal.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IDA:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR019183; N-acetylTrfase_B_cplx_non-cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22767:SF3; PTHR22767:SF3; 1.
DR Pfam; PF09797; NatB_MDM20; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..972
FT /note="N-alpha-acetyltransferase 25, NatB auxiliary
FT subunit"
FT /id="PRO_0000294337"
FT REPEAT 11..44
FT /note="TPR 1"
FT REPEAT 45..78
FT /note="TPR 2"
FT REPEAT 79..112
FT /note="TPR 3"
FT REPEAT 114..146
FT /note="TPR 4"
FT VAR_SEQ 847..859
FT /note="TISVILWVSSYCE -> VSFCSLPKRHCCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026629"
FT VAR_SEQ 860..972
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_026630"
FT VARIANT 426
FT /note="L -> F (in dbSNP:rs16941860)"
FT /id="VAR_054099"
FT VARIANT 789
FT /note="S -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035872"
FT VARIANT 876
FT /note="K -> R (in dbSNP:rs12231744)"
FT /id="VAR_033156"
FT VARIANT 915
FT /note="L -> I (in dbSNP:rs12298022)"
FT /id="VAR_054100"
FT CONFLICT 202
FT /note="I -> T (in Ref. 4; BAB14432)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="Y -> S (in Ref. 4; BAB14432)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="S -> T (in Ref. 4; BAB14432)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="S -> G (in Ref. 2; CAE46062)"
FT /evidence="ECO:0000305"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:6VP9"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:6VP9"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6VP9"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:6VP9"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:6VP9"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:6VP9"
FT TURN 35..39
FT /evidence="ECO:0007829|PDB:6VP9"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 168..173
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 263..278
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 380..383
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 384..388
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:6VP9"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 409..423
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 470..475
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 476..482
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 488..501
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 506..519
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 523..529
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 536..543
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 544..550
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 551..554
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 556..582
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 583..588
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 593..604
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 607..623
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 624..629
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 631..635
FT /evidence="ECO:0007829|PDB:7STX"
FT TURN 636..638
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 667..670
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 673..697
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 724..727
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 729..745
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 761..766
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 770..789
FT /evidence="ECO:0007829|PDB:7STX"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 795..819
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 827..829
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 836..867
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 884..904
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 908..911
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 934..963
FT /evidence="ECO:0007829|PDB:7STX"
FT HELIX 964..968
FT /evidence="ECO:0007829|PDB:7STX"
SQ SEQUENCE 972 AA; 112292 MW; 232B8FD14447DDD6 CRC64;
MATRGHVQDP NDRRLRPIYD YLDNGNNKMA IQQADKLLKK HKDLHCAKVL KAIGLQRTGK
QEEAFTLAQE VAALEPTDDN SLQALTILYR EMHRPELVTK LYEAAVKKVP NSEEYHSHLF
MAYARVGEYK KMQQAGMALY KIVPKNPYYF WSVMSLIMQS ISAQDENLSK TMFLPLAERM
VEKMVKEDKI EAEAEVELYY MILERLGKYQ EALDVIRGKL GEKLTSEIQS RENKCMAMYK
KLSRWPECNA LSRRLLLKNS DDWQFYLTYF DSVFRLIEEA WSPPAEGEHS LEGEVHYSAE
KAVKFIEDRI TEESKSSRHL RGPHLAKLEL IRRLRSQGCN DEYKLGDPEE LMFQYFKKFG
DKPCCFTDLK VFVDLLPATQ CTKFINQLLG VVPLSTPTED KLALPADIRA LQQHLCVVQL
TRLLGLYHTM DKNQKLSVVR ELMLRYQHGL EFGKTCLKTE LQFSDYYCLL AVHALIDVWR
ETGDETTVWQ ALTLLEEGLT HSPSNAQFKL LLVRIYCMLG AFEPVVDLYS SLDAKHIQHD
TIGYLLTRYA ESLGQYAAAS QSCNFALRFF HSNQKDTSEY IIQAYKYGAF EKIPEFIAFR
NRLNNSLHFA QVRTERMLLD LLLEANISTS LAESIKSMNL RPEEDDIPWE DLRDNRDLNV
FFSWDPKDRD VSEEHKKLSL EEETLWLRIR SLTLRLISGL PSLNHPVEPK NSEKTAENGV
SSRIDILRLL LQQLEATLET GKRFIEKDIQ YPFLGPVPTR MGGFFNSGCS QCQISSFYLV
NDIYELDTSG LEDTMEIQER IENSFKSLLD QLKDVFSKCK GDLLEVKDGN LKTHPTLLEN
LVFFVETISV ILWVSSYCES VLRPYKLNLQ KKKKKKKETS IIMPPVFTSF QDYVTGLQTL
ISNVVDHIKG LETHLIALKL EELILEDTSL SPEERKFSKT VQGKVQSSYL HSLLEMGELL
KKRLETTKKL KI
