ID   PHB_HUMAN               Reviewed;         272 AA.
AC   P35232; B4DY47; Q4VBQ0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   11-NOV-2015, entry version 155.
DE   RecName: Full=Prohibitin;
GN   Name=PHB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-88 AND
RP   HIS-105.
RC   TISSUE=Mammary gland;
RX   PubMed=1540973;
RA   Sato T., Saito H., Swensen J., Olifant A., Wood C., Danner D.,
RA   Sakamoto T., Takita K., Kasumi F., Miki Y., Skolnick M., Nakamura Y.;
RT   "The human prohibitin gene located on chromosome 17q21 is mutated in
RT   sporadic breast cancer.";
RL   Cancer Res. 52:1643-1646(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8244394; DOI=10.1006/geno.1993.1402;
RA   Sato T., Sakamoto T., Takita K., Saito H., Okui K., Nakamura Y.;
RT   "The human prohibitin (PHB) gene family and its somatic mutations in
RT   human tumors.";
RL   Genomics 17:762-764(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT   the human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and Muscle;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 5-11; 84-93; 106-128; 134-143; 178-186 AND
RP   209-219, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Submitted (MAR-2005) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 75-83; 94-117; 134-143; 158-177; 220-253 AND
RP   256-272, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [9]
RP   FUNCTION, INTERACTION WITH PHB2, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=11302691; DOI=10.1006/excr.2001.5166;
RA   Coates P.J., Nenutil R., McGregor A., Picksley S.M., Crouch D.H.,
RA   Hall P.A., Wright E.G.;
RT   "Mammalian prohibitin proteins respond to mitochondrial stress and
RT   decrease during cellular senescence.";
RL   Exp. Cell Res. 265:262-273(2001).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [11]
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.,
RA   Buerckstuemmer T., 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   [12]
RP   INTERACTION WITH STOML2.
RX   PubMed=21746876; DOI=10.1128/MCB.05393-11;
RA   Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G.,
RA   Li B., Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.;
RT   "Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial
RT   biogenesis and function.";
RL   Mol. Cell. Biol. 31:3845-3856(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91 AND TYR-249, AND
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Prohibitin inhibits DNA synthesis. It has a role in
CC       regulating proliferation. As yet it is unclear if the protein or
CC       the mRNA exhibits this effect. May play a role in regulating
CC       mitochondrial respiration activity and in aging.
CC       {ECO:0000269|PubMed:11302691}.
CC   -!- SUBUNIT: Interacts with PHB2. Interacts with STOML2.
CC       {ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:21746876}.
CC   -!- INTERACTION:
CC       Q496Y0:LONRF3; NbExp=2; IntAct=EBI-354213, EBI-2690768;
CC       Q13309-2:SKP2; NbExp=2; IntAct=EBI-354213, EBI-7791408;
CC       O14980:XPO1; NbExp=2; IntAct=EBI-354213, EBI-355867;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P35232-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35232-2; Sequence=VSP_054922;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed in different tissues.
CC   -!- DEVELOPMENTAL STAGE: Levels of expression in fibroblasts decrease
CC       heterogeneously during cellular aging.
CC       {ECO:0000269|PubMed:11302691}.
CC   -!- INDUCTION: Expression increases approximately 3-fold upon entry
CC       into G1 phase compared with other phases of the cell cycle. Also
CC       induced following inhibition of mitochondrial protein synthesis by
CC       thiamphenicol. {ECO:0000269|PubMed:11302691}.
CC   -!- SIMILARITY: Belongs to the prohibitin family. {ECO:0000305}.
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DR   EMBL; S85655; AAB21614.1; -; mRNA.
DR   EMBL; L14272; AAO18340.1; -; Genomic_DNA.
DR   EMBL; BT007411; AAP36079.1; -; mRNA.
DR   EMBL; AK302258; BAG63609.1; -; mRNA.
DR   EMBL; AC091180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013401; AAH13401.1; -; mRNA.
DR   EMBL; BC095460; AAH95460.1; -; mRNA.
DR   CCDS; CCDS11548.1; -. [P35232-1]
DR   CCDS; CCDS62244.1; -. [P35232-2]
DR   PIR; I52690; I52690.
DR   RefSeq; NP_001268425.1; NM_001281496.1. [P35232-1]
DR   RefSeq; NP_001268426.1; NM_001281497.1. [P35232-2]
DR   RefSeq; NP_001268644.1; NM_001281715.1. [P35232-1]
DR   RefSeq; NP_002625.1; NM_002634.3. [P35232-1]
DR   UniGene; Hs.514303; -.
DR   PDB; 1LU7; Model; -; A=1-272.
DR   PDBsum; 1LU7; -.
DR   ProteinModelPortal; P35232; -.
DR   BioGrid; 111264; 83.
DR   DIP; DIP-24248N; -.
DR   IntAct; P35232; 63.
DR   MINT; MINT-1158239; -.
DR   STRING; 9606.ENSP00000300408; -.
DR   PhosphoSite; P35232; -.
DR   DMDM; 464371; -.
DR   DOSAC-COBS-2DPAGE; P35232; -.
DR   OGP; P35232; -.
DR   REPRODUCTION-2DPAGE; IPI00017334; -.
DR   REPRODUCTION-2DPAGE; P35232; -.
DR   SWISS-2DPAGE; P35232; -.
DR   UCD-2DPAGE; P35232; -.
DR   MaxQB; P35232; -.
DR   PaxDb; P35232; -.
DR   PeptideAtlas; P35232; -.
DR   PRIDE; P35232; -.
DR   DNASU; 5245; -.
DR   Ensembl; ENST00000300408; ENSP00000300408; ENSG00000167085. [P35232-1]
DR   Ensembl; ENST00000511832; ENSP00000425035; ENSG00000167085. [P35232-2]
DR   Ensembl; ENST00000614445; ENSP00000479488; ENSG00000167085. [P35232-1]
DR   Ensembl; ENST00000617874; ENSP00000484113; ENSG00000167085. [P35232-1]
DR   GeneID; 5245; -.
DR   KEGG; hsa:5245; -.
DR   UCSC; uc002iox.1; human. [P35232-1]
DR   CTD; 5245; -.
DR   GeneCards; PHB; -.
DR   HGNC; HGNC:8912; PHB.
DR   HPA; HPA003280; -.
DR   MIM; 176705; gene.
DR   neXtProt; NX_P35232; -.
DR   PharmGKB; PA33251; -.
DR   eggNOG; KOG3083; Eukaryota.
DR   eggNOG; COG0330; LUCA.
DR   GeneTree; ENSGT00550000074770; -.
DR   HOGENOM; HOG000205692; -.
DR   HOVERGEN; HBG004457; -.
DR   InParanoid; P35232; -.
DR   KO; K17080; -.
DR   OMA; YLNIGLD; -.
DR   OrthoDB; EOG7V4B04; -.
DR   PhylomeDB; P35232; -.
DR   TreeFam; TF300095; -.
DR   Reactome; R-HSA-5673000; RAF activation.
DR   GeneWiki; Prohibitin; -.
DR   GenomeRNAi; 5245; -.
DR   NextBio; 20266; -.
DR   PRO; PR:P35232; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; P35232; -.
DR   CleanEx; HS_PHB; -.
DR   ExpressionAtlas; P35232; baseline and differential.
DR   Genevisible; P35232; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:HGNC.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0001850; F:complement component C3a binding; IDA:UniProtKB.
DR   GO; GO:0001851; F:complement component C3b binding; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0031871; F:proteinase activated receptor binding; IPI:UniProtKB.
DR   GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
DR   GO; GO:0071354; P:cellular response to interleukin-6; IDA:BHF-UCL.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR   GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR   GO; GO:2000323; P:negative regulation of glucocorticoid receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
DR   GO; GO:0045917; P:positive regulation of complement activation; IDA:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR   GO; GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0050847; P:progesterone receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR000163; Prohibitin.
DR   PANTHER; PTHR23222; PTHR23222; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00679; PROHIBITIN.
DR   SMART; SM00244; PHB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW   Complete proteome; Direct protein sequencing; DNA synthesis; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Polymorphism; Proto-oncogene; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:25944712}.
FT   CHAIN         2    272       Prohibitin.
FT                                /FTId=PRO_0000213878.
FT   COILED      177    211       {ECO:0000255}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:25944712}.
FT   MOD_RES      91     91       Phosphothreonine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   MOD_RES     128    128       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P67778}.
FT   MOD_RES     186    186       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P67778}.
FT   MOD_RES     202    202       N6-acetyllysine; alternate.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     202    202       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P67778}.
FT   MOD_RES     249    249       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:24275569}.
FT   VAR_SEQ     140    256       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_054922.
FT   VARIANT      88     88       V -> A (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:1540973}.
FT                                /FTId=VAR_006479.
FT   VARIANT     105    105       R -> H (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:1540973}.
FT                                /FTId=VAR_006480.
SQ   SEQUENCE   272 AA;  29804 MW;  915494273E342C76 CRC64;
     MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW
     VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP
     SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT
     EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK
     LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ
//