SEBP2_HUMAN
ID SEBP2_HUMAN Reviewed; 854 AA.
AC Q96T21; F8W892; Q5HYY1; Q7L1Z0; Q8IYC0; Q9H0A1;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Selenocysteine insertion sequence-binding protein 2;
DE Short=SECIS-binding protein 2;
GN Name=SECISBP2; Synonyms=SBP2;
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), AND TISSUE SPECIFICITY.
RX PubMed=12095701; DOI=10.1016/s0378-1119(02)00629-7;
RA Lescure A., Allmang C., Yamada K., Carbon P., Krol A.;
RT "cDNA cloning, expression pattern and RNA binding analysis of human
RT selenocysteine insertion sequence (SECIS) binding protein 2.";
RL Gene 291:279-285(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP SUBCELLULAR LOCATION (ISOFORM 2), AND ALTERNATIVE SPLICING (ISOFORMS 1; 2
RP AND 3).
RX PubMed=19004874; DOI=10.1093/nar/gkn829;
RA Papp L.V., Wang J., Kennedy D., Boucher D., Zhang Y., Gladyshev V.N.,
RA Singh R.N., Khanna K.K.;
RT "Functional characterization of alternatively spliced human SECISBP2
RT transcript variants.";
RL Nucleic Acids Res. 36:7192-7206(2008).
RN [8]
RP INVOLVEMENT IN THMA, AND VARIANT THMA GLN-540.
RX PubMed=16228000; DOI=10.1038/ng1654;
RA Dumitrescu A.M., Liao X.-H., Abdullah M.S.Y., Lado-Abeal J., Majed F.A.,
RA Moeller L.C., Boran G., Schomburg L., Weiss R.E., Refetoff S.;
RT "Mutations in SECISBP2 result in abnormal thyroid hormone metabolism.";
RL Nat. Genet. 37:1247-1252(2005).
RN [9]
RP INVOLVEMENT IN THMA.
RX PubMed=29882503; DOI=10.1089/thy.2018.0015;
RA Catli G., Fujisawa H., Kirbiyik O., Mimoto M.S., Gencpinar P.,
RA Oezdemir T.R., Duendar B.N., Dumitrescu A.M.;
RT "A Novel Homozygous Selenocysteine Insertion Sequence Binding Protein 2
RT (SECISBP2, SBP2) Gene Mutation in a Turkish Boy.";
RL Thyroid 28:1221-1223(2018).
CC -!- FUNCTION: Binds to the SECIS element in the 3'-UTR of some mRNAs
CC encoding selenoproteins. Binding is stimulated by SELB.
CC -!- SUBUNIT: Interacts with SELB. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96T21; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-954116, EBI-11978259;
CC Q96T21; Q08379: GOLGA2; NbExp=3; IntAct=EBI-954116, EBI-618309;
CC Q96T21; P42858: HTT; NbExp=3; IntAct=EBI-954116, EBI-466029;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion
CC {ECO:0000269|PubMed:19004874}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96T21-1; Sequence=Displayed;
CC Name=2; Synonyms=mtSBP2;
CC IsoId=Q96T21-2; Sequence=VSP_039070, VSP_039071;
CC Name=3; Synonyms=SBP2_delta2;
CC IsoId=Q96T21-3; Sequence=VSP_055755;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in testis.
CC {ECO:0000269|PubMed:12095701}.
CC -!- DISEASE: Thyroid hormone metabolism, abnormal (THMA) [MIM:609698]: A
CC disorder associated with a reduction in type II iodothyronine
CC deiodinase activity. {ECO:0000269|PubMed:16228000,
CC ECO:0000269|PubMed:29882503}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Contains a transit peptide at positions 1-
CC 15. {ECO:0000305}.
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DR EMBL; AF380995; AAK57518.1; -; mRNA.
DR EMBL; AL136881; CAB66815.1; -; mRNA.
DR EMBL; AK290182; BAF82871.1; -; mRNA.
DR EMBL; BX000356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62763.1; -; Genomic_DNA.
DR EMBL; CH471089; EAW62764.1; -; Genomic_DNA.
DR EMBL; BC023142; AAH23142.2; -; mRNA.
DR EMBL; BC036109; AAH36109.1; -; mRNA.
DR CCDS; CCDS65076.1; -. [Q96T21-2]
DR CCDS; CCDS65077.1; -. [Q96T21-3]
DR CCDS; CCDS6683.1; -. [Q96T21-1]
DR RefSeq; NP_001269617.1; NM_001282688.1.
DR RefSeq; NP_001269618.1; NM_001282689.1. [Q96T21-2]
DR RefSeq; NP_076982.3; NM_024077.4. [Q96T21-1]
DR RefSeq; XP_006717345.1; XM_006717282.2. [Q96T21-2]
DR RefSeq; XP_011517302.1; XM_011519000.2. [Q96T21-3]
DR AlphaFoldDB; Q96T21; -.
DR BioGRID; 122507; 77.
DR IntAct; Q96T21; 14.
DR MINT; Q96T21; -.
DR STRING; 9606.ENSP00000364965; -.
DR GlyGen; Q96T21; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96T21; -.
DR PhosphoSitePlus; Q96T21; -.
DR BioMuta; SECISBP2; -.
DR DMDM; 52788293; -.
DR EPD; Q96T21; -.
DR jPOST; Q96T21; -.
DR MassIVE; Q96T21; -.
DR MaxQB; Q96T21; -.
DR PaxDb; Q96T21; -.
DR PeptideAtlas; Q96T21; -.
DR PRIDE; Q96T21; -.
DR ProteomicsDB; 30103; -.
DR ProteomicsDB; 78173; -. [Q96T21-1]
DR ProteomicsDB; 78174; -. [Q96T21-2]
DR Antibodypedia; 27996; 204 antibodies from 32 providers.
DR DNASU; 79048; -.
DR Ensembl; ENST00000339901.8; ENSP00000364959.3; ENSG00000187742.15. [Q96T21-2]
DR Ensembl; ENST00000375807.8; ENSP00000364965.3; ENSG00000187742.15. [Q96T21-1]
DR Ensembl; ENST00000534113.6; ENSP00000436650.2; ENSG00000187742.15. [Q96T21-3]
DR GeneID; 79048; -.
DR KEGG; hsa:79048; -.
DR MANE-Select; ENST00000375807.8; ENSP00000364965.3; NM_024077.5; NP_076982.3.
DR UCSC; uc004aqj.3; human. [Q96T21-1]
DR CTD; 79048; -.
DR DisGeNET; 79048; -.
DR GeneCards; SECISBP2; -.
DR HGNC; HGNC:30972; SECISBP2.
DR HPA; ENSG00000187742; Low tissue specificity.
DR MalaCards; SECISBP2; -.
DR MIM; 607693; gene.
DR MIM; 609698; phenotype.
DR neXtProt; NX_Q96T21; -.
DR OpenTargets; ENSG00000187742; -.
DR Orphanet; 171706; Short stature-delayed bone age due to thyroid hormone metabolism deficiency.
DR PharmGKB; PA134863749; -.
DR VEuPathDB; HostDB:ENSG00000187742; -.
DR eggNOG; ENOG502QUP4; Eukaryota.
DR GeneTree; ENSGT00490000043356; -.
DR HOGENOM; CLU_016771_0_0_1; -.
DR InParanoid; Q96T21; -.
DR OMA; CVFPSCA; -.
DR OrthoDB; 236436at2759; -.
DR PhylomeDB; Q96T21; -.
DR TreeFam; TF328821; -.
DR PathwayCommons; Q96T21; -.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR SignaLink; Q96T21; -.
DR BioGRID-ORCS; 79048; 29 hits in 1083 CRISPR screens.
DR ChiTaRS; SECISBP2; human.
DR GeneWiki; SECISBP2; -.
DR GenomeRNAi; 79048; -.
DR Pharos; Q96T21; Tbio.
DR PRO; PR:Q96T21; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96T21; protein.
DR Bgee; ENSG00000187742; Expressed in secondary oocyte and 194 other tissues.
DR ExpressionAtlas; Q96T21; baseline and differential.
DR Genevisible; Q96T21; HS.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0035368; F:selenocysteine insertion sequence binding; IBA:GO_Central.
DR GO; GO:0021884; P:forebrain neuron development; IEA:Ensembl.
DR GO; GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:Ensembl.
DR GO; GO:0001514; P:selenocysteine incorporation; IBA:GO_Central.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR DisProt; DP00420; -.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR040051; SECISBP2.
DR PANTHER; PTHR13284; PTHR13284; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Mitochondrion; Nucleus;
KW Protein biosynthesis; Reference proteome; RNA-binding; Transit peptide.
FT CHAIN 1..854
FT /note="Selenocysteine insertion sequence-binding protein 2"
FT /id="PRO_0000097655"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..694
FT /note="RNA-binding"
FT /evidence="ECO:0000255"
FT REGION 787..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 380..387
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 332..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..804
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_039070"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055755"
FT VAR_SEQ 74..101
FT /note="STFPPQYLSSEITLHPYAYSPYTLDSTQ -> MVRVLRSMCLPQLCSHILSV
FT CSGTTSDR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_039071"
FT VARIANT 428
FT /note="Q -> E (in dbSNP:rs45452691)"
FT /id="VAR_061704"
FT VARIANT 540
FT /note="R -> Q (in THMA; dbSNP:rs119461976)"
FT /evidence="ECO:0000269|PubMed:16228000"
FT /id="VAR_025282"
FT CONFLICT 553
FT /note="S -> G (in Ref. 6; AAH36109)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="P -> L (in Ref. 1; AAK57518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 854 AA; 95462 MW; A911370853BE4E6E CRC64;
MASEGPREPE SEGIKLSADV KPFVPRFAGL NVAWLESSEA CVFPSSAATY YPFVQEPPVT
EQKIYTEDMA FGASTFPPQY LSSEITLHPY AYSPYTLDST QNVYSVPGSQ YLYNQPSCYR
GFQTVKHRNE NTCPLPQEMK ALFKKKTYDE KKTYDQQKFD SERADGTISS EIKSARGSHH
LSIYAENSLK SDGYHKRTDR KSRIIAKNVS TSKPEFEFTT LDFPELQGAE NNMSEIQKQP
KWGPVHSVST DISLLREVVK PAAVLSKGEI VVKNNPNESV TANAATNSPS CTRELSWTPM
GYVVRQTLST ELSAAPKNVT SMINLKTIAS SADPKNVSIP SSEALSSDPS YNKEKHIIHP
TQKSKASQGS DLEQNEASRK NKKKKEKSTS KYEVLTVQEP PRIEDAEEFP NLAVASERRD
RIETPKFQSK QQPQDNFKNN VKKSQLPVQL DLGGMLTALE KKQHSQHAKQ SSKPVVVSVG
AVPVLSKECA SGERGRRMSQ MKTPHNPLDS SAPLMKKGKQ REIPKAKKPT SLKKIILKER
QERKQRLQEN AVSPAFTSDD TQDGESGGDD QFPEQAELSG PEGMDELIST PSVEDKSEEP
PGTELQRDTE ASHLAPNHTT FPKIHSRRFR DYCSQMLSKE VDACVTDLLK ELVRFQDRMY
QKDPVKAKTK RRLVLGLREV LKHLKLKKLK CVIISPNCEK IQSKGGLDDT LHTIIDYACE
QNIPFVFALN RKALGRSLNK AVPVSVVGIF SYDGAQDQFH KMVELTVAAR QAYKTMLENV
QQELVGEPRP QAPPSLPTQG PSCPAEDGPP ALKEKEEPHY IEIWKKHLEA YSGCTLELEE
SLEASTSQMM NLNL
