TET5A_HUMAN
ID TET5A_HUMAN Reviewed; 442 AA.
AC Q96IP4; A8K7U4; Q5TF86; Q8NFZ9; Q9BW32; Q9NXV5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Terminal nucleotidyltransferase 5A {ECO:0000305};
DE EC=2.7.7.19 {ECO:0000269|PubMed:33882302};
DE AltName: Full=HBV X-transactivated gene 11 protein {ECO:0000303|Ref.2};
DE AltName: Full=HBV XAg-transactivated protein 11 {ECO:0000303|Ref.2};
GN Name=TENT5A {ECO:0000312|HGNC:HGNC:18345};
GN Synonyms=C6orf37 {ECO:0000312|HGNC:HGNC:18345},
GN FAM46A {ECO:0000312|HGNC:HGNC:18345}, XTP11 {ECO:0000303|Ref.2};
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), VARIANT 39-GLY--GLY-43 DEL, AND
RP TISSUE SPECIFICITY.
RX PubMed=12054608; DOI=10.1016/s0006-291x(02)00228-0;
RA Lagali P.S., Kakuk L.E., Griesinger I.B., Wong P.W., Ayyagari R.;
RT "Identification and characterization of C6orf37, a novel candidate human
RT retinal disease gene on chromosome 6q14.";
RL Biochem. Biophys. Res. Commun. 293:356-365(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLY-ASP-PHE-GLY-GLY-24
RP INS AND ALA-313.
RC TISSUE=Synovium;
RA Liu Y., Li J., Cheng J., Ji D., Gong M., Zhang L., Chen J.;
RT "Homo sapiens HBV XAg-transactivated protein 11 (XTP11) mRNA.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP GLY-ASP-PHE-GLY-GLY-24 INS AND ALA-313.
RC TISSUE=Colon, and Teratocarcinoma;
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLY-ASP-PHE-GLY-GLY-24 INS.
RC TISSUE=Eye, and Skin;
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 CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF ASP-139 AND ASP-141.
RX PubMed=33882302; DOI=10.1016/j.celrep.2021.109015;
RA Gewartowska O., Aranaz-Novaliches G., Krawczyk P.S., Mroczek S.,
RA Kusio-Kobialka M., Tarkowski B., Spoutil F., Benada O., Kofronova O.,
RA Szwedziak P., Cysewski D., Gruchota J., Szpila M., Chlebowski A.,
RA Sedlacek R., Prochazka J., Dziembowski A.;
RT "Cytoplasmic polyadenylation by TENT5A is required for proper bone
RT formation.";
RL Cell Rep. 35:109015-109015(2021).
RN [8]
RP INVOLVEMENT IN OI18, VARIANTS OI18 ARG-127 AND GLY-231, AND TISSUE
RP SPECIFICITY.
RX PubMed=29358272; DOI=10.1136/jmedgenet-2017-104999;
RA Doyard M., Bacrot S., Huber C., Di Rocco M., Goldenberg A., Aglan M.S.,
RA Brunelle P., Temtamy S., Michot C., Otaify G.A., Haudry C., Castanet M.,
RA Leroux J., Bonnefont J.P., Munnich A., Baujat G., Lapunzina P., Monnot S.,
RA Ruiz-Perez V.L., Cormier-Daire V.;
RT "FAM46A mutations are responsible for autosomal recessive osteogenesis
RT imperfecta.";
RL J. Med. Genet. 55:278-284(2018).
RN [9]
RP VARIANTS GLY-ASP-PHE-GLY-GLY-24 INS AND 39-GLY--GLY-43 DEL.
RX PubMed=16545789; DOI=10.1016/j.cca.2005.12.043;
RA Cui J., Wang W., Lai M.D., Xu E.P., Lv B.J., Lin J., Ruan W.J., Ma Y.,
RA Yao C.;
RT "Identification of a novel VNTR polymorphism in C6orf37 and its association
RT with colorectal cancer risk in Chinese population.";
RL Clin. Chim. Acta 368:155-159(2006).
CC -!- FUNCTION: Cytoplasmic non-canonical poly(A) RNA polymerase that
CC catalyzes the transfer of one adenosine molecule from an ATP to an mRNA
CC poly(A) tail bearing a 3'-OH terminal group and participates in the
CC cytoplasmic polyadenylation (PubMed:33882302). Polyadenylates mRNA
CC encoding extracellular matrix constituents and other genes crucial for
CC bone mineralization and during osteoblast mineralization, mainly
CC focuses on ER-targeted mRNAs (By similarity).
CC {ECO:0000250|UniProtKB:D3Z5S8, ECO:0000269|PubMed:33882302}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:33882302};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333;
CC Evidence={ECO:0000269|PubMed:33882302};
CC -!- INTERACTION:
CC Q96IP4; P54253: ATXN1; NbExp=5; IntAct=EBI-954084, EBI-930964;
CC Q96IP4; Q9NP31: SH2D2A; NbExp=3; IntAct=EBI-954084, EBI-490630;
CC Q96IP4; P43405: SYK; NbExp=3; IntAct=EBI-954084, EBI-78302;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D3Z5S8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96IP4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96IP4-2; Sequence=VSP_035502;
CC -!- TISSUE SPECIFICITY: Widely expressed, with preferential expression
CC observed in the retina compared to other ocular tissues
CC (PubMed:12054608). Also expressed in osteoblasts (PubMed:29358272).
CC {ECO:0000269|PubMed:12054608, ECO:0000269|PubMed:29358272}.
CC -!- DISEASE: Osteogenesis imperfecta 18 (OI18) [MIM:617952]: An autosomal
CC recessive form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI18 is a severe form characterized by congenital bowing of
CC the lower limb, wormian bones, blue sclerae, vertebral collapses and
CC multiple fractures in the first years of life.
CC {ECO:0000269|PubMed:29358272}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TENT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00683.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF350451; AAM53071.1; -; mRNA.
DR EMBL; AY740520; AAW66943.1; -; mRNA.
DR EMBL; AK000044; BAA90903.1; -; mRNA.
DR EMBL; AK056057; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK292109; BAF84798.1; -; mRNA.
DR EMBL; AL078599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48692.1; -; Genomic_DNA.
DR EMBL; BC000683; AAH00683.1; ALT_INIT; mRNA.
DR EMBL; BC007351; AAH07351.1; -; mRNA.
DR CCDS; CCDS34489.1; -. [Q96IP4-1]
DR PIR; JC7837; JC7837.
DR RefSeq; NP_060103.2; NM_017633.2. [Q96IP4-1]
DR AlphaFoldDB; Q96IP4; -.
DR SMR; Q96IP4; -.
DR BioGRID; 120744; 82.
DR IntAct; Q96IP4; 48.
DR STRING; 9606.ENSP00000318298; -.
DR iPTMnet; Q96IP4; -.
DR PhosphoSitePlus; Q96IP4; -.
DR BioMuta; FAM46A; -.
DR DMDM; 209572613; -.
DR EPD; Q96IP4; -.
DR jPOST; Q96IP4; -.
DR MassIVE; Q96IP4; -.
DR MaxQB; Q96IP4; -.
DR PaxDb; Q96IP4; -.
DR PeptideAtlas; Q96IP4; -.
DR PRIDE; Q96IP4; -.
DR ProteomicsDB; 76841; -. [Q96IP4-1]
DR ProteomicsDB; 76842; -. [Q96IP4-2]
DR Antibodypedia; 46387; 107 antibodies from 20 providers.
DR DNASU; 55603; -.
DR Ensembl; ENST00000320172.11; ENSP00000318298.6; ENSG00000112773.16. [Q96IP4-1]
DR Ensembl; ENST00000369754.7; ENSP00000358769.3; ENSG00000112773.16. [Q96IP4-2]
DR GeneID; 55603; -.
DR KEGG; hsa:55603; -.
DR MANE-Select; ENST00000320172.11; ENSP00000318298.6; NM_017633.3; NP_060103.2.
DR UCSC; uc003pjf.3; human. [Q96IP4-1]
DR CTD; 55603; -.
DR DisGeNET; 55603; -.
DR GeneCards; TENT5A; -.
DR HGNC; HGNC:18345; TENT5A.
DR HPA; ENSG00000112773; Group enriched (bone marrow, salivary gland).
DR MalaCards; TENT5A; -.
DR MIM; 611357; gene.
DR MIM; 617952; phenotype.
DR neXtProt; NX_Q96IP4; -.
DR OpenTargets; ENSG00000112773; -.
DR Orphanet; 216812; Osteogenesis imperfecta type 3.
DR PharmGKB; PA38531; -.
DR VEuPathDB; HostDB:ENSG00000112773; -.
DR eggNOG; KOG3852; Eukaryota.
DR GeneTree; ENSGT00940000157191; -.
DR HOGENOM; CLU_008115_2_1_1; -.
DR InParanoid; Q96IP4; -.
DR OrthoDB; 612201at2759; -.
DR PhylomeDB; Q96IP4; -.
DR TreeFam; TF315239; -.
DR BRENDA; 2.7.7.19; 2681.
DR PathwayCommons; Q96IP4; -.
DR SignaLink; Q96IP4; -.
DR BioGRID-ORCS; 55603; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; FAM46A; human.
DR GeneWiki; FAM46A; -.
DR GenomeRNAi; 55603; -.
DR Pharos; Q96IP4; Tbio.
DR PRO; PR:Q96IP4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96IP4; protein.
DR Bgee; ENSG00000112773; Expressed in parotid gland and 192 other tissues.
DR ExpressionAtlas; Q96IP4; baseline and differential.
DR Genevisible; Q96IP4; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IBA:GO_Central.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0030278; P:regulation of ossification; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR InterPro; IPR012937; TET5.
DR PANTHER; PTHR12974; PTHR12974; 1.
DR Pfam; PF07984; NTP_transf_7; 1.
DR SMART; SM01153; DUF1693; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; Nucleotidyltransferase;
KW Osteogenesis imperfecta; Reference proteome; Repeat; Transferase.
FT CHAIN 1..442
FT /note="Terminal nucleotidyltransferase 5A"
FT /id="PRO_0000259929"
FT REPEAT 24..28
FT /note="1"
FT REPEAT 29..33
FT /note="2"
FT REPEAT 34..38
FT /note="3"
FT REPEAT 39..43
FT /note="4"
FT VAR_SEQ 1
FT /note="M -> MHQRYFWTDQGQVALGGHYM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035502"
FT VARIANT 24
FT /note="G -> GGDFGG"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_046649"
FT VARIANT 39..43
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:12054608,
FT ECO:0000269|PubMed:16545789"
FT /id="VAR_028978"
FT VARIANT 127
FT /note="H -> R (in OI18; unknown pathological significance;
FT dbSNP:rs1187611948)"
FT /evidence="ECO:0000269|PubMed:29358272"
FT /id="VAR_080798"
FT VARIANT 231
FT /note="D -> G (in OI18; unknown pathological significance;
FT dbSNP:rs1554200371)"
FT /evidence="ECO:0000269|PubMed:29358272"
FT /id="VAR_080799"
FT VARIANT 313
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_028979"
FT MUTAGEN 139
FT /note="D->N: Does not elongate poly(A) tail; when
FT associated with N-141."
FT /evidence="ECO:0000269|PubMed:33882302"
FT MUTAGEN 141
FT /note="D->N: Does not elongate poly(A) tail; when
FT associated with N-139."
FT /evidence="ECO:0000269|PubMed:33882302"
FT CONFLICT 47
FT /note="S -> T (in Ref. 1; AAM53071)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="C -> S (in Ref. 1; AAM53071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49666 MW; C72092C590C1E369 CRC64;
MAEGEGYFAM SEDELACSPY IPLGGDFGGG DFGGGDFGGG DFGGGGSFGG HCLDYCESPT
AHCNVLNWEQ VQRLDGILSE TIPIHGRGNF PTLELQPSLI VKVVRRRLAE KRIGVRDVRL
NGSAASHVLH QDSGLGYKDL DLIFCADLRG EGEFQTVKDV VLDCLLDFLP EGVNKEKITP
LTLKEAYVQK MVKVCNDSDR WSLISLSNNS GKNVELKFVD SLRRQFEFSV DSFQIKLDSL
LLFYECSENP MTETFHPTII GESVYGDFQE AFDHLCNKII ATRNPEEIRG GGLLKYCNLL
VRGFRPASDE IKTLQRYMCS RFFIDFSDIG EQQRKLESYL QNHFVGLEDR KYEYLMTLHG
VVNESTVCLM GHERRQTLNL ITMLAIRVLA DQNVIPNVAN VTCYYQPAPY VADANFSNYY
IAQVQPVFTC QQQTYSTWLP CN
