ID   NXN_HUMAN               Reviewed;         435 AA.
AC   Q6DKJ4; B4DXQ0; D3DTH2; Q3SWW6; Q6P3U6; Q7L4C6; Q9H9Q1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Nucleoredoxin;
DE            EC=1.8.1.8;
GN   Name=NXN; Synonyms=NRX;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 124-435 (ISOFORM 1).
RC   TISSUE=Teratocarcinoma, and 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., 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   [2]
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., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., 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 the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), PARTIAL NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 171-435 (ISOFORM 1).
RC   TISSUE=Brain, Liver, Lung, and Uterus;
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   IDENTIFICATION IN A COMPLEX WITH PHOSPHATASE 2A.
RX   PubMed=16764867; DOI=10.1016/j.febslet.2006.04.101;
RA   Lechward K., Sugajska E., de Baere I., Goris J., Hemmings B.A.,
RA   Zolnierowicz S.;
RT   "Interaction of nucleoredoxin with protein phosphatase 2A.";
RL   FEBS Lett. 580:3631-3637(2006).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [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   INVOLVEMENT IN RRS2, AND VARIANTS RRS2 209-ARG--ILE-435 DEL AND GLU-412
RP   DEL.
RX   PubMed=29276006; DOI=10.1016/j.ajhg.2017.10.002;
RG   Baylor-Hopkins Center for Mendelian Genomics;
RA   White J.J., Mazzeu J.F., Coban-Akdemir Z., Bayram Y., Bahrambeigi V.,
RA   Hoischen A., van Bon B.W.M., Gezdirici A., Gulec E.Y., Ramond F.,
RA   Touraine R., Thevenon J., Shinawi M., Beaver E., Heeley J., Hoover-Fong J.,
RA   Durmaz C.D., Karabulut H.G., Marzioglu-Ozdemir E., Cayir A., Duz M.B.,
RA   Seven M., Price S., Ferreira B.M., Vianna-Morgante A.M., Ellard S.,
RA   Parrish A., Stals K., Flores-Daboub J., Jhangiani S.N., Gibbs R.A.,
RA   Brunner H.G., Sutton V.R., Lupski J.R., Carvalho C.M.B.;
RT   "WNT signaling perturbations underlie the genetic heterogeneity of Robinow
RT   syndrome.";
RL   Am. J. Hum. Genet. 102:27-43(2018).
CC   -!- FUNCTION: Functions as a redox-dependent negative regulator of the Wnt
CC       signaling pathway, possibly by preventing ubiquitination of DVL3 by the
CC       BCR(KLHL12) complex. May also function as a transcriptional regulator
CC       act as a regulator of protein phosphatase 2A (PP2A) (By similarity).
CC       {ECO:0000250|UniProtKB:P97346}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC         NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC   -!- SUBUNIT: Associates with the phosphatase 2A holoenzyme. Interacts with
CC       PPP2CA; the interaction is direct. Interacts with DVL1 (via PDZ
CC       domain); the interaction is direct and regulated by oxidative stress
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P97346}. Nucleus {ECO:0000250|UniProtKB:P97346}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6DKJ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6DKJ4-2; Sequence=VSP_033392, VSP_033393, VSP_033394,
CC                                  VSP_033395;
CC       Name=3;
CC         IsoId=Q6DKJ4-3; Sequence=VSP_042792, VSP_042793;
CC   -!- DISEASE: Robinow syndrome, autosomal recessive 2 (RRS2) [MIM:618529]: A
CC       recessive form of Robinow syndrome, a disease characterized by short-
CC       limb dwarfism, costovertebral segmentation defects and abnormalities of
CC       the head, face and external genitalia. The clinical signs are generally
CC       far more severe in recessive cases, particularly skeletal
CC       abnormalities. All patients with the recessive form suffer from
CC       vertebral segmentation abnormalities, resulting in scoliosis and chest
CC       deformities. Rib fusions are considered to be characteristic of the
CC       autosomal recessive form. Patients can also present brachydactyly, with
CC       extensive aplasia/hypoplasia of the phalanges and
CC       metacarpals/metatarsals, and brachy-syn-polydactyly of the hands and
CC       oligodactyly of the feet. {ECO:0000269|PubMed:29276006}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the nucleoredoxin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14171.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB55122.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK022676; BAB14171.1; ALT_INIT; mRNA.
DR   EMBL; AK027451; BAB55122.1; ALT_INIT; mRNA.
DR   EMBL; AK302073; BAG63462.1; -; mRNA.
DR   EMBL; AC015884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC036164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC087392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90640.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90641.1; -; Genomic_DNA.
DR   EMBL; BC009327; AAH09327.2; -; mRNA.
DR   EMBL; BC063828; AAH63828.1; -; mRNA.
DR   EMBL; BC073845; AAH73845.1; -; mRNA.
DR   EMBL; BC104634; AAI04635.1; -; mRNA.
DR   CCDS; CCDS10998.1; -. [Q6DKJ4-1]
DR   CCDS; CCDS56013.1; -. [Q6DKJ4-3]
DR   RefSeq; NP_001192248.1; NM_001205319.1. [Q6DKJ4-3]
DR   RefSeq; NP_071908.2; NM_022463.4. [Q6DKJ4-1]
DR   AlphaFoldDB; Q6DKJ4; -.
DR   SMR; Q6DKJ4; -.
DR   BioGRID; 122144; 36.
DR   IntAct; Q6DKJ4; 10.
DR   MINT; Q6DKJ4; -.
DR   STRING; 9606.ENSP00000337443; -.
DR   iPTMnet; Q6DKJ4; -.
DR   MetOSite; Q6DKJ4; -.
DR   PhosphoSitePlus; Q6DKJ4; -.
DR   BioMuta; NXN; -.
DR   DMDM; 187471109; -.
DR   EPD; Q6DKJ4; -.
DR   jPOST; Q6DKJ4; -.
DR   MassIVE; Q6DKJ4; -.
DR   MaxQB; Q6DKJ4; -.
DR   PaxDb; 9606-ENSP00000337443; -.
DR   PeptideAtlas; Q6DKJ4; -.
DR   ProteomicsDB; 66233; -. [Q6DKJ4-1]
DR   ProteomicsDB; 66234; -. [Q6DKJ4-2]
DR   ProteomicsDB; 66235; -. [Q6DKJ4-3]
DR   Pumba; Q6DKJ4; -.
DR   Antibodypedia; 10317; 168 antibodies from 26 providers.
DR   DNASU; 64359; -.
DR   Ensembl; ENST00000336868.8; ENSP00000337443.3; ENSG00000167693.17. [Q6DKJ4-1]
DR   Ensembl; ENST00000575801.5; ENSP00000461038.1; ENSG00000167693.17. [Q6DKJ4-3]
DR   GeneID; 64359; -.
DR   KEGG; hsa:64359; -.
DR   MANE-Select; ENST00000336868.8; ENSP00000337443.3; NM_022463.5; NP_071908.2.
DR   UCSC; uc002fsa.4; human. [Q6DKJ4-1]
DR   AGR; HGNC:18008; -.
DR   CTD; 64359; -.
DR   DisGeNET; 64359; -.
DR   GeneCards; NXN; -.
DR   HGNC; HGNC:18008; NXN.
DR   HPA; ENSG00000167693; Low tissue specificity.
DR   MalaCards; NXN; -.
DR   MIM; 612895; gene.
DR   MIM; 618529; phenotype.
DR   neXtProt; NX_Q6DKJ4; -.
DR   OpenTargets; ENSG00000167693; -.
DR   Orphanet; 1507; Autosomal recessive Robinow syndrome.
DR   PharmGKB; PA31863; -.
DR   VEuPathDB; HostDB:ENSG00000167693; -.
DR   eggNOG; KOG2501; Eukaryota.
DR   GeneTree; ENSGT00940000161894; -.
DR   HOGENOM; CLU_019626_2_1_1; -.
DR   InParanoid; Q6DKJ4; -.
DR   OMA; NAPCRQF; -.
DR   OrthoDB; 1201562at2759; -.
DR   PhylomeDB; Q6DKJ4; -.
DR   TreeFam; TF331873; -.
DR   PathwayCommons; Q6DKJ4; -.
DR   SignaLink; Q6DKJ4; -.
DR   BioGRID-ORCS; 64359; 10 hits in 1151 CRISPR screens.
DR   ChiTaRS; NXN; human.
DR   GenomeRNAi; 64359; -.
DR   Pharos; Q6DKJ4; Tbio.
DR   PRO; PR:Q6DKJ4; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q6DKJ4; Protein.
DR   Bgee; ENSG00000167693; Expressed in cervix squamous epithelium and 197 other cell types or tissues.
DR   ExpressionAtlas; Q6DKJ4; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0072359; P:circulatory system development; ISS:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
DR   CDD; cd03071; PDI_b'_NRX; 1.
DR   CDD; cd03009; TryX_like_TryX_NRX; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR   InterPro; IPR041861; NRX_PDI_b.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR   PANTHER; PTHR46472; NUCLEOREDOXIN; 1.
DR   PANTHER; PTHR46472:SF1; NUCLEOREDOXIN; 1.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   Pfam; PF13905; Thioredoxin_8; 2.
DR   SUPFAM; SSF52833; Thioredoxin-like; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   Genevisible; Q6DKJ4; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW   Differentiation; Disease variant; Dwarfism; NAD; Nucleus; Oxidoreductase;
KW   Reference proteome; Wnt signaling pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..435
FT                   /note="Nucleoredoxin"
FT                   /id="PRO_0000332933"
FT   DOMAIN          167..321
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   VAR_SEQ         1..113
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033392"
FT   VAR_SEQ         1..108
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042792"
FT   VAR_SEQ         109..120
FT                   /note="WLALPYKEKHRK -> MADVSLHRNPAT (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042793"
FT   VAR_SEQ         114..120
FT                   /note="YKEKHRK -> MQELRNS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033393"
FT   VAR_SEQ         275..290
FT                   /note="IPTLIMLDPQGEVITR -> RRSRPRLRVAPGNLLT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033394"
FT   VAR_SEQ         291..435
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033395"
FT   VARIANT         209..435
FT                   /note="Missing (in RRS2)"
FT                   /evidence="ECO:0000269|PubMed:29276006"
FT                   /id="VAR_083246"
FT   VARIANT         412
FT                   /note="Missing (in RRS2; uncertain significance;
FT                   dbSNP:rs1555607285)"
FT                   /evidence="ECO:0000269|PubMed:29276006"
FT                   /id="VAR_083247"
FT   CONFLICT        124
FT                   /note="W -> K (in Ref. 1; BAB55122)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="W -> K (in Ref. 1; BAB14171)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        372
FT                   /note="V -> I (in Ref. 4; AAH73845)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   435 AA;  48392 MW;  B67927F001BE4E5B CRC64;
     MSGFLEELLG EKLVTGGGEE VDVHSLGARG ISLLGLYFGC SLSAPCAQLS ASLAAFYGRL
     RGDAAAGPGP GAGAGAAAEP EPRRRLEIVF VSSDQDQRQW QDFVRDMPWL ALPYKEKHRK
     LKLWNKYRIS NIPSLIFLDA TTGKVVCRNG LLVIRDDPEG LEFPWGPKPF REVIAGPLLR
     NNGQSLESSS LEGSHVGVYF SAHWCPPCRS LTRVLVESYR KIKEAGQNFE IIFVSADRSE
     ESFKQYFSEM PWLAVPYTDE ARRSRLNRLY GIQGIPTLIM LDPQGEVITR QGRVEVLNDE
     DCREFPWHPK PVLELSDSNA AQLNEGPCLV LFVDSEDDGE SEAAKQLIQP IAEKIIAKYK
     AKEEEAPLLF FVAGEDDMTD SLRDYTNLPE AAPLLTILDM SARAKYVMDV EEITPAIVEA
     FVNDFLAEKL KPEPI
//