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 28-JAN-2026, entry version 151. 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). RN [9] RP INTERACTION WITH NAA20. RX PubMed=34230638; DOI=10.1038/s41436-021-01264-0; RA Morrison J., Altuwaijri N.K., Broenstad K., Aksnes H., Alsaif H.S., RA Evans A., Hashem M., Wheeler P.G., Webb B.D., Alkuraya F.S., Arnesen T.; RT "Missense NAA20 variants impairing the NatB protein N-terminal RT acetyltransferase cause autosomal recessive developmental delay, RT intellectual disability, and microcephaly."; RL Genet. Med. 23:2213-2218(2021). 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, Met-Glu, Met-Asn and Met-Gln. May play a role in normal CC cell-cycle progression. {ECO:0000269|PubMed:18570629}. CC -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB) complex CC which is composed of NAA20 and NAA25. {ECO:0000269|PubMed:34230638}. 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}; 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; 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 PDB; 8G0L; EM; 3.39 A; B=1-972. DR PDBsum; 6VP9; -. DR PDBsum; 7STX; -. DR PDBsum; 8G0L; -. DR AlphaFoldDB; Q14CX7; -. DR EMDB; EMD-21307; -. DR EMDB; EMD-25438; -. DR EMDB; EMD-29657; -. DR SMR; Q14CX7; -. DR BioGRID; 123072; 73. DR ComplexPortal; CPX-6270; NatB N-alpha-acetyltransferase complex. DR CORUM; Q14CX7; -. DR DIP; DIP-50826N; -. DR FunCoup; Q14CX7; 3979. DR IntAct; Q14CX7; 37. DR STRING; 9606.ENSP00000261745; -. DR GlyGen; Q14CX7; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; Q14CX7; -. DR MetOSite; Q14CX7; -. DR PhosphoSitePlus; Q14CX7; -. DR SwissPalm; Q14CX7; -. DR BioMuta; NAA25; -. DR DMDM; 121948761; -. DR jPOST; Q14CX7; -. DR MassIVE; Q14CX7; -. DR PaxDb; 9606-ENSP00000261745; -. DR PeptideAtlas; Q14CX7; -. DR ProteomicsDB; 60335; -. [Q14CX7-1] DR ProteomicsDB; 60336; -. [Q14CX7-2] DR Pumba; Q14CX7; -. DR Antibodypedia; 50891; 113 antibodies from 20 providers. DR DNASU; 80018; -. DR Ensembl; ENST00000261745.9; ENSP00000261745.4; ENSG00000111300.11. [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 AGR; HGNC:25783; -. DR ClinPGx; PA165513030; -. 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 OpenTargets; ENSG00000111300; -. DR VEuPathDB; HostDB:ENSG00000111300; -. DR eggNOG; KOG2053; Eukaryota. DR GeneTree; ENSGT00950000183174; -. DR HOGENOM; CLU_008075_0_0_1; -. DR InParanoid; Q14CX7; -. DR OMA; WKRREHQ; -. DR OrthoDB; 1874341at2759; -. DR PAN-GO; Q14CX7; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q14CX7; -. DR BioCyc; MetaCyc:ENSG00000111300-MONOMER; -. DR BRENDA; 2.3.1.254; 2681. DR PathwayCommons; Q14CX7; -. DR SignaLink; Q14CX7; -. DR SIGNOR; Q14CX7; -. DR Agora; ENSG00000111300; -. DR BioGRID-ORCS; 80018; 614 hits in 1171 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 180 other cell types or tissues. DR ExpressionAtlas; Q14CX7; baseline and differential. 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:0010698; F:acetyltransferase activator activity; IBA:GO_Central. DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central. DR FunFam; 1.25.40.1040:FF:000004; N-alpha-acetyltransferase 25, NatB auxiliary subunit; 1. DR Gene3D; 1.25.40.1040; -; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR019183; NAA25_NatB_aux_su. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR PANTHER; PTHR22767:SF3; N-ALPHA-ACETYLTRANSFERASE 25, NATB AUXILIARY SUBUNIT; 1. DR PANTHER; PTHR22767; N-TERMINAL ACETYLTRANSFERASE-RELATED; 1. DR Pfam; PF09797; NatB_MDM20; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50293; TPR_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Proteomics identification; KW Reference proteome; Repeat; 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 HELIX 10..23 FT /evidence="ECO:0007829|PDB:8G0L" FT HELIX 27..40 FT /evidence="ECO:0007829|PDB:8G0L" 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 STRAND 360..362 FT /evidence="ECO:0007829|PDB:8G0L" 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:8G0L" 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 701..703 FT /evidence="ECO:0007829|PDB:8G0L" 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 STRAND 830..832 FT /evidence="ECO:0007829|PDB:8G0L" 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 //