ID   DAZP1_HUMAN             Reviewed;         407 AA.
AC   Q96EP5; Q96MJ3; Q9NRR9;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=DAZ-associated protein 1;
DE   AltName: Full=Deleted in azoospermia-associated protein 1;
GN   Name=DAZAP1;
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), RNA-BINDING, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH DAZ AND DAZL.
RC   TISSUE=Testis;
RX   PubMed=10857750; DOI=10.1006/geno.2000.6169;
RA   Tsui S., Dai T., Roettger S., Schempp W., Salido E.C., Yen P.H.;
RT   "Identification of two novel proteins that interact with germ-cell-specific
RT   RNA-binding proteins DAZ and DAZL1.";
RL   Genomics 65:266-273(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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]
RP   PROTEIN SEQUENCE OF 1-27; 136-150 AND 195-209, ACETYLATION AT MET-1, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Ovarian carcinoma;
RA   Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-390 (ISOFORM 2).
RC   TISSUE=Prostate;
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   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
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   [9]
RP   ACETYLATION AT LYS-150, AND SUBCELLULAR LOCATION.
RX   PubMed=22001406; DOI=10.1016/j.gene.2011.09.022;
RA   Sasaki K., Suzuki A., Kagatsume S., Ono M., Matsuzawa K., Taguchi Y.,
RA   Kurihara Y.;
RT   "Acetylation of Prrp K150 regulates the subcellular localization.";
RL   Gene 491:13-19(2012).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-253, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [13]
RP   STRUCTURE BY NMR OF 1-198.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the N-terminal and of the second RNA binding domain
RT   in DAZ-associated protein 1.";
RL   Submitted (SEP-2006) to the PDB data bank.
RN   [14]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-381.
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: RNA-binding protein, which may be required during
CC       spermatogenesis.
CC   -!- SUBUNIT: Interacts with DAZ and DAZL. {ECO:0000269|PubMed:10857750}.
CC   -!- INTERACTION:
CC       Q96EP5; Q9NQZ3: DAZ1; NbExp=3; IntAct=EBI-2133162, EBI-997955;
CC       Q96EP5; P09012: SNRPA; NbExp=3; IntAct=EBI-2133162, EBI-607085;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22001406}. Nucleus
CC       {ECO:0000269|PubMed:22001406}. Note=Predominantly cytoplasmic (By
CC       similarity). Nuclear at some stages of spermatozoides development. In
CC       midpachytene spermatocytes, it is localized in both the cytoplasm and
CC       the nuclei and is clearly excluded from the sex vesicles. In round
CC       spermatids, it localizes mainly in the nuclei, whereas in elongated
CC       spermatids, it localizes to the cytoplasm (By similarity).
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96EP5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96EP5-2; Sequence=VSP_009441;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in testis. Expressed to a lower
CC       level in thymus. Weakly or not expressed in heart, liver, brain,
CC       placenta, lung, skeletal muscle, kidney and pancreas.
CC       {ECO:0000269|PubMed:10857750}.
CC   -!- PTM: Acetylation at Lys-150 is predominantly observed in the nuclear
CC       fraction, and may regulate nucleocytoplasmic transport.
CC       {ECO:0000269|PubMed:22001406, ECO:0000269|Ref.3}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB71295.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF181719; AAF78364.1; -; mRNA.
DR   EMBL; BC012062; AAH12062.1; -; mRNA.
DR   EMBL; AK056850; BAB71295.1; ALT_INIT; mRNA.
DR   CCDS; CCDS12065.1; -. [Q96EP5-1]
DR   CCDS; CCDS12066.1; -. [Q96EP5-2]
DR   RefSeq; NP_061832.2; NM_018959.3. [Q96EP5-1]
DR   RefSeq; NP_733829.1; NM_170711.2. [Q96EP5-2]
DR   PDB; 2DGS; NMR; -; A=110-195.
DR   PDB; 2DH8; NMR; -; A=1-92.
DR   PDBsum; 2DGS; -.
DR   PDBsum; 2DH8; -.
DR   AlphaFoldDB; Q96EP5; -.
DR   SMR; Q96EP5; -.
DR   BioGRID; 117730; 155.
DR   IntAct; Q96EP5; 33.
DR   MINT; Q96EP5; -.
DR   STRING; 9606.ENSP00000233078; -.
DR   GlyGen; Q96EP5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96EP5; -.
DR   MetOSite; Q96EP5; -.
DR   PhosphoSitePlus; Q96EP5; -.
DR   SwissPalm; Q96EP5; -.
DR   BioMuta; DAZAP1; -.
DR   DMDM; 44887869; -.
DR   REPRODUCTION-2DPAGE; IPI00165230; -.
DR   EPD; Q96EP5; -.
DR   jPOST; Q96EP5; -.
DR   MassIVE; Q96EP5; -.
DR   MaxQB; Q96EP5; -.
DR   PaxDb; 9606-ENSP00000233078; -.
DR   PeptideAtlas; Q96EP5; -.
DR   ProteomicsDB; 76437; -. [Q96EP5-1]
DR   ProteomicsDB; 76438; -. [Q96EP5-2]
DR   Pumba; Q96EP5; -.
DR   Antibodypedia; 1414; 225 antibodies from 26 providers.
DR   DNASU; 26528; -.
DR   Ensembl; ENST00000233078.9; ENSP00000233078.4; ENSG00000071626.17. [Q96EP5-1]
DR   Ensembl; ENST00000336761.10; ENSP00000337132.5; ENSG00000071626.17. [Q96EP5-2]
DR   GeneID; 26528; -.
DR   KEGG; hsa:26528; -.
DR   MANE-Select; ENST00000233078.9; ENSP00000233078.4; NM_018959.4; NP_061832.2.
DR   UCSC; uc002lsm.5; human. [Q96EP5-1]
DR   AGR; HGNC:2683; -.
DR   CTD; 26528; -.
DR   DisGeNET; 26528; -.
DR   GeneCards; DAZAP1; -.
DR   HGNC; HGNC:2683; DAZAP1.
DR   HPA; ENSG00000071626; Low tissue specificity.
DR   MIM; 607430; gene.
DR   neXtProt; NX_Q96EP5; -.
DR   OpenTargets; ENSG00000071626; -.
DR   PharmGKB; PA27153; -.
DR   VEuPathDB; HostDB:ENSG00000071626; -.
DR   eggNOG; KOG4205; Eukaryota.
DR   GeneTree; ENSGT00940000156757; -.
DR   InParanoid; Q96EP5; -.
DR   OMA; FVMFRKA; -.
DR   OrthoDB; 3127428at2759; -.
DR   PhylomeDB; Q96EP5; -.
DR   TreeFam; TF314808; -.
DR   PathwayCommons; Q96EP5; -.
DR   SignaLink; Q96EP5; -.
DR   SIGNOR; Q96EP5; -.
DR   BioGRID-ORCS; 26528; 111 hits in 1161 CRISPR screens.
DR   ChiTaRS; DAZAP1; human.
DR   EvolutionaryTrace; Q96EP5; -.
DR   GeneWiki; DAZ_associated_protein_1; -.
DR   GenomeRNAi; 26528; -.
DR   Pharos; Q96EP5; Tbio.
DR   PRO; PR:Q96EP5; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q96EP5; Protein.
DR   Bgee; ENSG00000071626; Expressed in left testis and 193 other cell types or tissues.
DR   ExpressionAtlas; Q96EP5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IMP:UniProtKB.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR   GO; GO:0034046; F:poly(G) binding; IMP:UniProtKB.
DR   GO; GO:0008266; F:poly(U) RNA binding; IMP:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0035613; F:RNA stem-loop binding; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
DR   GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
DR   CDD; cd12574; RRM1_DAZAP1; 1.
DR   CDD; cd12327; RRM2_DAZAP1; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR034134; DAZAP1_RRM1.
DR   InterPro; IPR034131; DAZAP1_RRM2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR48032:SF16; DAZ-ASSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR48032; RNA-BINDING PROTEIN MUSASHI HOMOLOG RBP6; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 2.
DR   Genevisible; Q96EP5; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Methylation; Nucleus; Reference proteome; Repeat; RNA-binding;
KW   Spermatogenesis.
FT   CHAIN           1..407
FT                   /note="DAZ-associated protein 1"
FT                   /id="PRO_0000081565"
FT   DOMAIN          10..97
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          113..190
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          74..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..283
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..333
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   MOD_RES         150
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:22001406"
FT   MOD_RES         253
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   VAR_SEQ         350..407
FT                   /note="AGYGQDLSGFGQGFSDPSQQPPSYGGPSVPGSGGPPAGGSGFGRGQNHNVQG
FT                   FHPYRR -> GLGSYSPAPPGCGPHFVYSLMVRLSSDVA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_009441"
FT   VARIANT         381
FT                   /note="S -> T (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035480"
FT   CONFLICT        109
FT                   /note="N -> Y (in Ref. 1; AAF78364)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..12
FT                   /evidence="ECO:0007829|PDB:2DH8"
FT   HELIX           23..31
FT                   /evidence="ECO:0007829|PDB:2DH8"
FT   STRAND          36..43
FT                   /evidence="ECO:0007829|PDB:2DH8"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:2DH8"
FT   STRAND          50..60
FT                   /evidence="ECO:0007829|PDB:2DH8"
FT   HELIX           63..70
FT                   /evidence="ECO:0007829|PDB:2DH8"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:2DH8"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:2DH8"
FT   STRAND          114..119
FT                   /evidence="ECO:0007829|PDB:2DGS"
FT   HELIX           126..133
FT                   /evidence="ECO:0007829|PDB:2DGS"
FT   STRAND          134..137
FT                   /evidence="ECO:0007829|PDB:2DGS"
FT   STRAND          139..144
FT                   /evidence="ECO:0007829|PDB:2DGS"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:2DGS"
FT   STRAND          155..163
FT                   /evidence="ECO:0007829|PDB:2DGS"
FT   HELIX           164..173
FT                   /evidence="ECO:0007829|PDB:2DGS"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:2DGS"
FT   STRAND          184..187
FT                   /evidence="ECO:0007829|PDB:2DGS"
SQ   SEQUENCE   407 AA;  43383 MW;  CFEB42903F4D5AFB CRC64;
     MNNSGADEIG KLFVGGLDWS TTQETLRSYF SQYGEVVDCV IMKDKTTNQS RGFGFVKFKD
     PNCVGTVLAS RPHTLDGRNI DPKPCTPRGM QPERTRPKEG WQKGPRSDNS KSNKIFVGGI
     PHNCGETELR EYFKKFGVVT EVVMIYDAEK QRPRGFGFIT FEDEQSVDQA VNMHFHDIMG
     KKVEVKRAEP RDSKSQAPGQ PGASQWGSRV VPNAANGWAG QPPPTWQQGY GPQGMWVPAG
     QAIGGYGPPP AGRGAPPPPP PFTSYIVSTP PGGFPPPQGF PQGYGAPPQF SFGYGPPPPP
     PDQFAPPGVP PPPATPGAAP LAFPPPPSQA APDMSKPPTA QPDFPYGQYA GYGQDLSGFG
     QGFSDPSQQP PSYGGPSVPG SGGPPAGGSG FGRGQNHNVQ GFHPYRR
//