S39A6_HUMAN
ID S39A6_HUMAN Reviewed; 755 AA.
AC Q13433; B4DR49; B4E224; Q8IXR3; Q96HP5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Zinc transporter ZIP6;
DE AltName: Full=Estrogen-regulated protein LIV-1;
DE AltName: Full=Solute carrier family 39 member 6;
DE AltName: Full=Zrt- and Irt-like protein 6;
DE Short=ZIP-6;
DE Flags: Precursor;
GN Name=SLC39A6; Synonyms=LIV1, ZIP6;
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 VARIANT ASP-119.
RA Green C., Morgan H.E.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-119.
RC TISSUE=Teratocarcinoma, and Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASP-119.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 382-755 (ISOFORM 1).
RC TISSUE=Eye, and Lymph;
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 [6]
RP PROTEIN SEQUENCE OF 29-43.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP INDUCTION.
RX PubMed=2903103; DOI=10.1016/0303-7207(88)90105-0;
RA Manning D.L., Daly R.J., Lord P.G., Kelly K.F., Green C.D.;
RT "Effects of oestrogen on the expression of a 4.4 kb mRNA in the ZR-75-1
RT human breast cancer cell line.";
RL Mol. Cell. Endocrinol. 59:205-212(1988).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=12839489; DOI=10.1042/bj20030478;
RA Taylor K.M., Morgan H.E., Johnson A., Hadley L.J., Nicholson R.I.;
RT "Structure-function analysis of LIV-1, the breast cancer-associated protein
RT that belongs to a new subfamily of zinc transporters.";
RL Biochem. J. 375:51-59(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67 AND ASN-241.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471 AND SER-478, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May act as a zinc-influx transporter.
CC {ECO:0000269|PubMed:12839489}.
CC -!- INTERACTION:
CC Q13433-2; Q92843: BCL2L2; NbExp=3; IntAct=EBI-12956703, EBI-707714;
CC Q13433-2; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-12956703, EBI-10192441;
CC Q13433-2; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12956703, EBI-18159983;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12839489};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12839489}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13433-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13433-2; Sequence=VSP_014309, VSP_014310, VSP_014311;
CC -!- TISSUE SPECIFICITY: Highly expressed in the breast, prostate, placenta,
CC kidney, pituitary and corpus callosum. Weakly expressed in heart and
CC intestine. Also highly expressed in cells derived from an
CC adenocarcinoma of the cervix and lung carcinoma.
CC {ECO:0000269|PubMed:12839489}.
CC -!- INDUCTION: Up-regulated by estrogen in breast cancer cells lines.
CC {ECO:0000269|PubMed:2903103}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12839489,
CC ECO:0000269|PubMed:19349973}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG61161.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SLC39A6ID44189ch18q12.html";
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DR EMBL; U41060; AAA96258.2; -; mRNA.
DR EMBL; AK299102; BAG61161.1; ALT_INIT; mRNA.
DR EMBL; AK304079; BAG64986.1; -; mRNA.
DR EMBL; AC091060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471088; EAX01372.1; -; Genomic_DNA.
DR EMBL; BC008317; AAH08317.2; -; mRNA.
DR EMBL; BC039498; AAH39498.1; -; mRNA.
DR CCDS; CCDS42428.1; -. [Q13433-1]
DR CCDS; CCDS45854.1; -. [Q13433-2]
DR PIR; G02273; G02273.
DR RefSeq; NP_001092876.1; NM_001099406.1. [Q13433-2]
DR RefSeq; NP_036451.3; NM_012319.3. [Q13433-1]
DR RefSeq; XP_011524202.1; XM_011525900.1. [Q13433-1]
DR RefSeq; XP_011524203.1; XM_011525901.1. [Q13433-1]
DR AlphaFoldDB; Q13433; -.
DR BioGRID; 117332; 150.
DR IntAct; Q13433; 16.
DR MINT; Q13433; -.
DR STRING; 9606.ENSP00000269187; -.
DR ChEMBL; CHEMBL4523581; -.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR MEROPS; X40.001; -.
DR TCDB; 2.A.5.4.13; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family.
DR GlyConnect; 1908; 8 N-Linked glycans (3 sites).
DR GlyGen; Q13433; 9 sites, 8 N-linked glycans (3 sites), 2 O-linked glycans (2 sites).
DR iPTMnet; Q13433; -.
DR PhosphoSitePlus; Q13433; -.
DR SwissPalm; Q13433; -.
DR BioMuta; SLC39A6; -.
DR DMDM; 292495066; -.
DR EPD; Q13433; -.
DR jPOST; Q13433; -.
DR MassIVE; Q13433; -.
DR MaxQB; Q13433; -.
DR PaxDb; Q13433; -.
DR PeptideAtlas; Q13433; -.
DR PRIDE; Q13433; -.
DR ProteomicsDB; 59428; -. [Q13433-1]
DR ProteomicsDB; 59429; -. [Q13433-2]
DR ABCD; Q13433; 1 sequenced antibody.
DR Antibodypedia; 5245; 292 antibodies from 35 providers.
DR DNASU; 25800; -.
DR Ensembl; ENST00000269187.10; ENSP00000269187.4; ENSG00000141424.13. [Q13433-1]
DR Ensembl; ENST00000440549.6; ENSP00000401139.1; ENSG00000141424.13. [Q13433-2]
DR Ensembl; ENST00000590986.5; ENSP00000465915.1; ENSG00000141424.13. [Q13433-1]
DR GeneID; 25800; -.
DR KEGG; hsa:25800; -.
DR MANE-Select; ENST00000269187.10; ENSP00000269187.4; NM_012319.4; NP_036451.4.
DR UCSC; uc002kzj.3; human. [Q13433-1]
DR CTD; 25800; -.
DR DisGeNET; 25800; -.
DR GeneCards; SLC39A6; -.
DR HGNC; HGNC:18607; SLC39A6.
DR HPA; ENSG00000141424; Low tissue specificity.
DR MIM; 608731; gene.
DR neXtProt; NX_Q13433; -.
DR OpenTargets; ENSG00000141424; -.
DR PharmGKB; PA134905551; -.
DR VEuPathDB; HostDB:ENSG00000141424; -.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000156387; -.
DR HOGENOM; CLU_015114_13_2_1; -.
DR InParanoid; Q13433; -.
DR OMA; YEGDLMS; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q13433; -.
DR TreeFam; TF318470; -.
DR PathwayCommons; Q13433; -.
DR Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family.
DR SignaLink; Q13433; -.
DR BioGRID-ORCS; 25800; 15 hits in 1083 CRISPR screens.
DR ChiTaRS; SLC39A6; human.
DR GeneWiki; SLC39A6; -.
DR GenomeRNAi; 25800; -.
DR Pharos; Q13433; Tbio.
DR PRO; PR:Q13433; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q13433; protein.
DR Bgee; ENSG00000141424; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; Q13433; baseline and differential.
DR Genevisible; Q13433; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0031258; C:lamellipodium membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IMP:UniProtKB.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil;
KW Direct protein sequencing; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 29..755
FT /note="Zinc transporter ZIP6"
FT /id="PRO_0000041650"
FT TOPO_DOM 29..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 658..678
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 679..686
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..755
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 95..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 464..480
FT /evidence="ECO:0000255"
FT COMPBIAS 95..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014309"
FT VAR_SEQ 707..708
FT /note="PE -> SF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014310"
FT VAR_SEQ 709..755
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014311"
FT VARIANT 119
FT /note="E -> D (in dbSNP:rs1789528)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.4"
FT /id="VAR_059964"
FT CONFLICT 127..132
FT /note="Missing (in Ref. 1; AAA96258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 755 AA; 85047 MW; 8BC1D02CA116DD25 CRC64;
MARKLSVILI LTFALSVTNP LHELKAAAFP QTTEKISPNW ESGINVDLAI STRQYHLQQL
FYRYGENNSL SVEGFRKLLQ NIGIDKIKRI HIHHDHDHHS DHEHHSDHER HSDHEHHSEH
EHHSDHDHHS HHNHAASGKN KRKALCPDHD SDSSGKDPRN SQGKGAHRPE HASGRRNVKD
SVSASEVTST VYNTVSEGTH FLETIETPRP GKLFPKDVSS STPPSVTSKS RVSRLAGRKT
NESVSEPRKG FMYSRNTNEN PQECFNASKL LTSHGMGIQV PLNATEFNYL CPAIINQIDA
RSCLIHTSEK KAEIPPKTYS LQIAWVGGFI AISIISFLSL LGVILVPLMN RVFFKFLLSF
LVALAVGTLS GDAFLHLLPH SHASHHHSHS HEEPAMEMKR GPLFSHLSSQ NIEESAYFDS
TWKGLTALGG LYFMFLVEHV LTLIKQFKDK KKKNQKKPEN DDDVEIKKQL SKYESQLSTN
EEKVDTDDRT EGYLRADSQE PSHFDSQQPA VLEEEEVMIA HAHPQEVYNE YVPRGCKNKC
HSHFHDTLGQ SDDLIHHHHD YHHILHHHHH QNHHPHSHSQ RYSREELKDA GVATLAWMVI
MGDGLHNFSD GLAIGAAFTE GLSSGLSTSV AVFCHELPHE LGDFAVLLKA GMTVKQAVLY
NALSAMLAYL GMATGIFIGH YAENVSMWIF ALTAGLFMYV ALVDMVPEML HNDASDHGCS
RWGYFFLQNA GMLLGFGIML LISIFEHKIV FRINF
