NOE3_HUMAN
ID NOE3_HUMAN Reviewed; 478 AA.
AC Q96PB7; Q5T3V6; Q6IMI7; Q6IMI8; Q6IMI9; Q6IMJ1; Q8TBG1; Q96PB2; Q96PB3;
AC Q96PB4; Q96PB5; Q96PB6;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Noelin-3;
DE AltName: Full=Olfactomedin-3;
DE AltName: Full=Optimedin;
DE Flags: Precursor;
GN Name=OLFM3; Synonyms=NOE3; ORFNames=UNQ1924/PRO4399;
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] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
RA Rhodes C.H., Call K.M., Little R., Braunschweiger K., Park J.P.;
RT "NOE3: a novel olfactomedin/noelin/pancortin homolog identified near an
RT ependymoma-associated translocation breakpoint.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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] (ISOFORM 3).
RC TISSUE=Hippocampus;
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 TISSUE SPECIFICITY.
RX PubMed=12019210; DOI=10.1093/hmg/11.11.1291;
RA Torrado M., Trivedi R., Zinovieva R., Karavanova I., Tomarev S.I.;
RT "Optimedin: a novel olfactomedin-related protein that interacts with
RT myocilin.";
RL Hum. Mol. Genet. 11:1291-1301(2002).
RN [8]
RP ALTERNATIVE SPLICING.
RX PubMed=15123989;
RA Mukhopadhyay A., Talukdar S., Bhattacharjee A., Ray K.;
RT "Bioinformatic approaches for identification and characterization of
RT olfactomedin related genes with a potential role in pathogenesis of ocular
RT disorders.";
RL Mol. Vis. 10:304-314(2004).
RN [9]
RP INTERACTION WITH OLFM2.
RX PubMed=21228389; DOI=10.1167/iovs.10-6356;
RA Sultana A., Nakaya N., Senatorov V.V., Tomarev S.I.;
RT "Olfactomedin 2: expression in the eye and interaction with other
RT olfactomedin domain-containing proteins.";
RL Invest. Ophthalmol. Vis. Sci. 52:2584-2592(2011).
CC -!- SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents, including OLFM3. Alone or in
CC combination, these auxiliary subunits control the gating and
CC pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing. Homodimer. Interacts with MYOC (By
CC similarity). Interacts with OLFM2 (PubMed:21228389). {ECO:0000250,
CC ECO:0000269|PubMed:21228389}.
CC -!- INTERACTION:
CC Q96PB7; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-10292253, EBI-10173507;
CC Q96PB7; O76003: GLRX3; NbExp=3; IntAct=EBI-10292253, EBI-374781;
CC Q96PB7; Q9UNE7: STUB1; NbExp=4; IntAct=EBI-10292253, EBI-357085;
CC Q96PB7-3; P63172: DYNLT1; NbExp=3; IntAct=EBI-12005356, EBI-1176455;
CC Q96PB7-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12005356, EBI-16439278;
CC Q96PB7-3; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-12005356, EBI-357085;
CC Q96PB7-3; P15884-3: TCF4; NbExp=3; IntAct=EBI-12005356, EBI-13636688;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q96PB7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96PB7-2; Sequence=VSP_003771, VSP_003772;
CC Name=3;
CC IsoId=Q96PB7-3; Sequence=VSP_003769;
CC Name=4;
CC IsoId=Q96PB7-4; Sequence=VSP_003769, VSP_003771, VSP_003772;
CC Name=5;
CC IsoId=Q96PB7-5; Sequence=VSP_003770;
CC Name=6;
CC IsoId=Q96PB7-6; Sequence=VSP_003770, VSP_003771, VSP_003772;
CC -!- TISSUE SPECIFICITY: In the eye, expressed in trabecular meshwork and
CC neural retina; in non-ocular tissues, expressed in brain and lung.
CC {ECO:0000269|PubMed:12019210}.
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DR EMBL; AF397392; AAK97473.1; -; mRNA.
DR EMBL; AF397393; AAK97474.1; -; mRNA.
DR EMBL; AF397394; AAK97475.1; -; mRNA.
DR EMBL; AF397395; AAK97476.1; -; mRNA.
DR EMBL; AF397396; AAK97477.1; -; mRNA.
DR EMBL; AF397397; AAK97478.1; -; mRNA.
DR EMBL; AY358722; AAQ89084.1; -; mRNA.
DR EMBL; AK095724; BAG53115.1; -; mRNA.
DR EMBL; AL356280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW72922.1; -; Genomic_DNA.
DR EMBL; BC022531; AAH22531.1; -; mRNA.
DR EMBL; BK001429; DAA01551.1; -; Genomic_DNA.
DR EMBL; BK001429; DAA01553.1; -; Genomic_DNA.
DR EMBL; BK001429; DAA01554.1; -; Genomic_DNA.
DR EMBL; BK001429; DAA01555.1; -; Genomic_DNA.
DR EMBL; BK001429; DAA01556.1; -; Genomic_DNA.
DR CCDS; CCDS30781.1; -. [Q96PB7-3]
DR CCDS; CCDS72832.1; -. [Q96PB7-1]
DR RefSeq; NP_001275750.1; NM_001288821.1. [Q96PB7-1]
DR RefSeq; NP_001275752.1; NM_001288823.1. [Q96PB7-5]
DR RefSeq; NP_477518.2; NM_058170.3. [Q96PB7-3]
DR RefSeq; XP_016855729.1; XM_017000240.1. [Q96PB7-5]
DR AlphaFoldDB; Q96PB7; -.
DR SMR; Q96PB7; -.
DR BioGRID; 125601; 22.
DR IntAct; Q96PB7; 12.
DR STRING; 9606.ENSP00000345192; -.
DR GlyGen; Q96PB7; 5 sites.
DR iPTMnet; Q96PB7; -.
DR PhosphoSitePlus; Q96PB7; -.
DR BioMuta; OLFM3; -.
DR DMDM; 20139068; -.
DR jPOST; Q96PB7; -.
DR MassIVE; Q96PB7; -.
DR PaxDb; Q96PB7; -.
DR PeptideAtlas; Q96PB7; -.
DR PRIDE; Q96PB7; -.
DR ProteomicsDB; 77652; -. [Q96PB7-1]
DR ProteomicsDB; 77653; -. [Q96PB7-2]
DR ProteomicsDB; 77654; -. [Q96PB7-3]
DR ProteomicsDB; 77655; -. [Q96PB7-4]
DR ProteomicsDB; 77656; -. [Q96PB7-5]
DR ProteomicsDB; 77657; -. [Q96PB7-6]
DR Antibodypedia; 33701; 152 antibodies from 21 providers.
DR DNASU; 118427; -.
DR Ensembl; ENST00000338858.9; ENSP00000345192.5; ENSG00000118733.17. [Q96PB7-1]
DR Ensembl; ENST00000370103.9; ENSP00000359121.5; ENSG00000118733.17. [Q96PB7-3]
DR Ensembl; ENST00000536598.1; ENSP00000443471.1; ENSG00000118733.17. [Q96PB7-6]
DR GeneID; 118427; -.
DR KEGG; hsa:118427; -.
DR MANE-Select; ENST00000370103.9; ENSP00000359121.5; NM_058170.4; NP_477518.2. [Q96PB7-3]
DR UCSC; uc001duf.4; human. [Q96PB7-1]
DR CTD; 118427; -.
DR DisGeNET; 118427; -.
DR GeneCards; OLFM3; -.
DR HGNC; HGNC:17990; OLFM3.
DR HPA; ENSG00000118733; Group enriched (brain, retina).
DR MIM; 607567; gene.
DR neXtProt; NX_Q96PB7; -.
DR OpenTargets; ENSG00000118733; -.
DR PharmGKB; PA31917; -.
DR VEuPathDB; HostDB:ENSG00000118733; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000156998; -.
DR HOGENOM; CLU_035236_0_0_1; -.
DR InParanoid; Q96PB7; -.
DR OMA; XELKEKM; -.
DR PhylomeDB; Q96PB7; -.
DR TreeFam; TF315964; -.
DR PathwayCommons; Q96PB7; -.
DR SignaLink; Q96PB7; -.
DR BioGRID-ORCS; 118427; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; OLFM3; human.
DR GeneWiki; OLFM3; -.
DR GenomeRNAi; 118427; -.
DR Pharos; Q96PB7; Tbio.
DR PRO; PR:Q96PB7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96PB7; protein.
DR Bgee; ENSG00000118733; Expressed in endothelial cell and 87 other tissues.
DR ExpressionAtlas; Q96PB7; baseline and differential.
DR Genevisible; Q96PB7; HS.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0042462; P:eye photoreceptor cell development; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR031216; Noelin-3.
DR InterPro; IPR022082; Noelin_dom.
DR InterPro; IPR003112; Olfac-like_dom.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR PANTHER; PTHR23192:SF36; PTHR23192:SF36; 1.
DR Pfam; PF12308; Noelin-1; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Synapse.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..478
FT /note="Noelin-3"
FT /id="PRO_0000020080"
FT DOMAIN 218..470
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT COILED 77..217
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 219..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_003770"
FT VAR_SEQ 1..43
FT /note="MSPPLLKLGAVLSTMAMISNWMSQTLPSLVGLNTTRLSTPDTL -> MQATS
FT NLLNLLLLSLFAGLDPSK (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_003769"
FT VAR_SEQ 218..235
FT /note="TCGKLMKITGPVTVKTSG -> IDLKKRKEEEKRQQKGEA (in isoform
FT 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_003771"
FT VAR_SEQ 236..478
FT /note="Missing (in isoform 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_003772"
FT CONFLICT 88
FT /note="Q -> K (in Ref. 6; AAH22531)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="Y -> C (in Ref. 6; AAH22531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 54930 MW; 02EAAF58741489E5 CRC64;
MSPPLLKLGA VLSTMAMISN WMSQTLPSLV GLNTTRLSTP DTLTQISPKE GWQVYSSAQD
PDGRCICTVV APEQNLCSRD AKSRQLRQLL EKVQNMSQSI EVLNLRTQRD FQYVLKMETQ
MKGLKAKFRQ IEDDRKTLMT KHFQELKEKM DELLPLIPVL EQYKTDAKLI TQFKEEIRNL
SAVLTGIQEE IGAYDYEELH QRVLSLETRL RDCMKKLTCG KLMKITGPVT VKTSGTRFGA
WMTDPLASEK NNRVWYMDSY TNNKIVREYK SIADFVSGAE SRTYNLPFKW AGTNHVVYNG
SLYFNKYQSN IIIKYSFDMG RVLAQRSLEY AGFHNVYPYT WGGFSDIDLM ADEIGLWAVY
ATNQNAGNIV ISQLNQDTLE VMKSWSTGYP KRSAGESFMI CGTLYVTNSH LTGAKVYYSY
STKTSTYEYT DIPFHNQYFH ISMLDYNARD RALYAWNNGH QVLFNVTLFH IIKTEDDT
