S22AG_HUMAN
ID S22AG_HUMAN Reviewed; 577 AA.
AC Q86VW1; O14567; Q5JXM1; Q8IUG8; Q8IZD5; Q96M90; Q96RU0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Solute carrier family 22 member 16;
DE AltName: Full=Carnitine transporter 2;
DE Short=CT2;
DE AltName: Full=Fly-like putative transporter 2;
DE Short=FLIPT2;
DE Short=Flipt 2;
DE AltName: Full=Organic cation transporter OKB1;
DE AltName: Full=Organic cation/carnitine transporter 6;
GN Name=SLC22A16; Synonyms=OCT6;
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), TISSUE SPECIFICITY, AND VARIANT
RP THR-409.
RC TISSUE=Kidney;
RX PubMed=12372408; DOI=10.1016/s0006-291x(02)02343-4;
RA Eraly S.A., Nigam S.K.;
RT "Novel human cDNAs homologous to Drosophila Orct and mammalian carnitine
RT transporters.";
RL Biochem. Biophys. Res. Commun. 297:1159-1166(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT THR-409.
RX PubMed=12384147; DOI=10.1016/s0301-472x(02)00901-3;
RA Gong S., Lu X., Xu Y., Swiderski C.F., Jordan C.T., Moscow J.A.;
RT "Identification of OCT6 as a novel organic cation transporter
RT preferentially expressed in hematopoietic cells and leukemias.";
RL Exp. Hematol. 30:1162-1169(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12089149; DOI=10.1074/jbc.m203883200;
RA Enomoto A., Wempe M.F., Tsuchida H., Shin H.J., Cha S.H., Anzai N.,
RA Goto A., Sakamoto A., Niwa T., Kanai Y., Anders M.W., Endou H.;
RT "Molecular identification of a novel carnitine transporter specific to
RT human testis. Insights into the mechanism of carnitine recognition.";
RL J. Biol. Chem. 277:36262-36271(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT THR-409.
RX PubMed=15963465; DOI=10.1016/j.bbrc.2005.05.174;
RA Okabe M., Unno M., Harigae H., Kaku M., Okitsu Y., Sasaki T., Mizoi T.,
RA Shiiba K., Takanaga H., Terasaki T., Matsuno S., Sasaki I., Ito S., Abe T.;
RT "Characterization of the organic cation transporter SLC22A16: a doxorubicin
RT importer.";
RL Biochem. Biophys. Res. Commun. 333:754-762(2005).
RN [5]
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-577 (ISOFORM 3), AND VARIANT
RP THR-409.
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., 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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=17197897; DOI=10.1097/01.pgp.0000225845.67245.b3;
RA Sato N., Ito K., Onogawa T., Akahira J., Unno M., Abe T., Niikura H.,
RA Yaegashi N.;
RT "Expression of organic cation transporter SLC22A16 in human endometria.";
RL Int. J. Gynecol. Pathol. 26:53-60(2007).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=17581421; DOI=10.1097/01.pgp.0000236951.33914.1b;
RA Ota K., Ito K., Akahira J., Sato N., Onogawa T., Moriya T., Unno M.,
RA Abe T., Niikura H., Takano T., Yaegashi N.;
RT "Expression of organic cation transporter SLC22A16 in human epithelial
RT ovarian cancer: a possible role of the adriamycin importer.";
RL Int. J. Gynecol. Pathol. 26:334-340(2007).
CC -!- FUNCTION: High affinity carnitine transporter; the uptake is partially
CC sodium-ion dependent. Thought to mediate the L-carnitine secretion
CC mechanism from testis epididymal epithelium into the lumen which is
CC involved in the maturation of spermatozoa. Also transports organic
CC cations such as tetraethylammonium (TEA) and doxorubicin. The uptake of
CC TEA is inhibited by various organic cations. The uptake of doxorubicin
CC is sodium-independent. {ECO:0000269|PubMed:12089149,
CC ECO:0000269|PubMed:15963465}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:12089149}.
CC Note=Detected in the plasma membrane of Sertoli cells and in the
CC luminal membrane of epithelial cells in the epididymis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86VW1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VW1-2; Sequence=VSP_031336, VSP_031337;
CC Name=3;
CC IsoId=Q86VW1-3; Sequence=VSP_031338;
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels in adult tissues and
CC fetal brain, lung, liver and kidney. Expressed in testis and epididymis
CC (at protein level). Expressed at lower levels in bone marrow and fetal
CC liver. Expressed in hematopoietic cells, including CD34(+) leukocytes
CC and leukemia cells. Abundantly expressed in ovarian cancer clear-cell
CC adenocarcinoma. Expressed in endometrium (at protein level); highly
CC expressed during the normal secretory phase, but expression is
CC significantly reduced in the proliferative phase.
CC {ECO:0000269|PubMed:12089149, ECO:0000269|PubMed:12372408,
CC ECO:0000269|PubMed:12384147, ECO:0000269|PubMed:15963465,
CC ECO:0000269|PubMed:17197897, ECO:0000269|PubMed:17581421}.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71419.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY145502; AAN52928.1; -; mRNA.
DR EMBL; AB055798; BAC23062.1; -; mRNA.
DR EMBL; AF268892; AAK58593.1; -; mRNA.
DR EMBL; AC002464; AAB67044.1; -; Genomic_DNA.
DR EMBL; AL050350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48313.1; -; Genomic_DNA.
DR EMBL; BC047565; AAH47565.1; -; mRNA.
DR EMBL; AK057306; BAB71419.1; ALT_INIT; mRNA.
DR CCDS; CCDS5084.1; -. [Q86VW1-1]
DR RefSeq; NP_149116.2; NM_033125.3. [Q86VW1-1]
DR RefSeq; XP_011534507.1; XM_011536205.2. [Q86VW1-3]
DR AlphaFoldDB; Q86VW1; -.
DR SMR; Q86VW1; -.
DR BioGRID; 124519; 40.
DR IntAct; Q86VW1; 28.
DR STRING; 9606.ENSP00000357915; -.
DR BindingDB; Q86VW1; -.
DR ChEMBL; CHEMBL2073722; -.
DR DrugBank; DB00997; Doxorubicin.
DR DrugBank; DB00583; Levocarnitine.
DR TCDB; 2.A.1.19.12; the major facilitator superfamily (mfs).
DR GlyGen; Q86VW1; 8 sites.
DR iPTMnet; Q86VW1; -.
DR PhosphoSitePlus; Q86VW1; -.
DR BioMuta; SLC22A16; -.
DR DMDM; 74750474; -.
DR jPOST; Q86VW1; -.
DR MassIVE; Q86VW1; -.
DR PaxDb; Q86VW1; -.
DR PeptideAtlas; Q86VW1; -.
DR PRIDE; Q86VW1; -.
DR Antibodypedia; 32327; 117 antibodies from 23 providers.
DR DNASU; 85413; -.
DR Ensembl; ENST00000330550.8; ENSP00000328583.4; ENSG00000004809.14. [Q86VW1-2]
DR Ensembl; ENST00000368919.8; ENSP00000357915.3; ENSG00000004809.14. [Q86VW1-1]
DR GeneID; 85413; -.
DR KEGG; hsa:85413; -.
DR MANE-Select; ENST00000368919.8; ENSP00000357915.3; NM_033125.4; NP_149116.2.
DR UCSC; uc003puf.5; human. [Q86VW1-1]
DR CTD; 85413; -.
DR DisGeNET; 85413; -.
DR GeneCards; SLC22A16; -.
DR HGNC; HGNC:20302; SLC22A16.
DR HPA; ENSG00000004809; Group enriched (bone marrow, testis).
DR MIM; 608276; gene.
DR neXtProt; NX_Q86VW1; -.
DR OpenTargets; ENSG00000004809; -.
DR PharmGKB; PA134911502; -.
DR VEuPathDB; HostDB:ENSG00000004809; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000160723; -.
DR InParanoid; Q86VW1; -.
DR OMA; TEVYQSI; -.
DR PhylomeDB; Q86VW1; -.
DR TreeFam; TF315847; -.
DR PathwayCommons; Q86VW1; -.
DR Reactome; R-HSA-549127; Organic cation transport.
DR SignaLink; Q86VW1; -.
DR BioGRID-ORCS; 85413; 11 hits in 1065 CRISPR screens.
DR GenomeRNAi; 85413; -.
DR Pharos; Q86VW1; Tbio.
DR PRO; PR:Q86VW1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q86VW1; protein.
DR Bgee; ENSG00000004809; Expressed in trabecular bone tissue and 110 other tissues.
DR ExpressionAtlas; Q86VW1; baseline and differential.
DR Genevisible; Q86VW1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015101; F:organic cation transmembrane transporter activity; IDA:MGI.
DR GO; GO:0046717; P:acid secretion; IDA:UniProtKB.
DR GO; GO:0015879; P:carnitine transport; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0015695; P:organic cation transport; IDA:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Developmental protein;
KW Differentiation; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW Spermatogenesis; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..577
FT /note="Solute carrier family 22 member 16"
FT /id="PRO_0000318991"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 543..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..17
FT /note="MGSRHFEGIYDHVGHFG -> MRTLHAVSHPYSNSM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12089149"
FT /id="VSP_031336"
FT VAR_SEQ 58..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12089149"
FT /id="VSP_031337"
FT VAR_SEQ 509..577
FT /note="FVGTMALLSGVLTLKLPETLGKRLATTWEEAAKLESENESKSSKLLLTTNNS
FT GLEKTEAITPRDSGLGE -> LGQHLQE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031338"
FT VARIANT 49
FT /note="H -> R (in dbSNP:rs714368)"
FT /id="VAR_038930"
FT VARIANT 252
FT /note="V -> A (in dbSNP:rs723685)"
FT /id="VAR_038931"
FT VARIANT 409
FT /note="M -> T (in dbSNP:rs12210538)"
FT /evidence="ECO:0000269|PubMed:12372408,
FT ECO:0000269|PubMed:12384147, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15963465"
FT /id="VAR_038932"
FT VARIANT 431
FT /note="V -> I (in dbSNP:rs35948062)"
FT /id="VAR_038933"
FT CONFLICT 257
FT /note="V -> G (in Ref. 1; AAN52928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 64614 MW; EA4ABBED0AE99632 CRC64;
MGSRHFEGIY DHVGHFGRFQ RVLYFICAFQ NISCGIHYLA SVFMGVTPHH VCRPPGNVSQ
VVFHNHSNWS LEDTGALLSS GQKDYVTVQL QNGEIWELSR CSRNKRENTS SLGYEYTGSK
KEFPCVDGYI YDQNTWKSTA VTQWNLVCDR KWLAMLIQPL FMFGVLLGSV TFGYFSDRLG
RRVVLWATSS SMFLFGIAAA FAVDYYTFMA ARFFLAMVAS GYLVVGFVYV MEFIGMKSRT
WASVHLHSFF AVGTLLVALT GYLVRTWWLY QMILSTVTVP FILCCWVLPE TPFWLLSEGR
YEEAQKIVDI MAKWNRASSC KLSELLSLDL QGPVSNSPTE VQKHNLSYLF YNWSITKRTL
TVWLIWFTGS LGFYSFSLNS VNLGGNEYLN LFLLGVVEIP AYTFVCIAMD KVGRRTVLAY
SLFCSALACG VVMVIPQKHY ILGVVTAMVG KFAIGAAFGL IYLYTAELYP TIVRSLAVGS
GSMVCRLASI LAPFSVDLSS IWIFIPQLFV GTMALLSGVL TLKLPETLGK RLATTWEEAA
KLESENESKS SKLLLTTNNS GLEKTEAITP RDSGLGE
