ID   S39A6_MOUSE             Reviewed;         765 AA.
AC   Q8C145; Q7TPP9; Q7TQE0; Q8R518;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Zinc transporter ZIP6 {ECO:0000305};
DE   AltName: Full=Endoplasmic reticulum membrane-linked protein;
DE            Short=Ermelin {ECO:0000303|PubMed:11891044};
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 {ECO:0000312|MGI:MGI:2147279}; Synonyms=Zip6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 21-765, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=11891044; DOI=10.1016/s0378-1119(01)00885-x;
RA   Suzuki A., Endo T.;
RT   "Ermelin, an endoplasmic reticulum transmembrane protein, contains the
RT   novel HELP domain conserved in eukaryotes.";
RL   Gene 284:31-40(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-68 AND ASN-275.
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=25143461; DOI=10.1093/molehr/gau066;
RA   Kong B.Y., Duncan F.E., Que E.L., Kim A.M., O'Halloran T.V., Woodruff T.K.;
RT   "Maternally-derived zinc transporters ZIP6 and ZIP10 drive the mammalian
RT   oocyte-to-egg transition.";
RL   Mol. Hum. Reprod. 20:1077-1089(2014).
RN   [8]
RP   FUNCTION, INDUCTION, IDENTIFICATION IN A COMPLEX WITH SLC39A10 AND NCAM1,
RP   AND IDENTIFICATION IN A COMPLEX WITH SLC39A10 AND GSK3B.
RX   PubMed=28098160; DOI=10.1038/srep40313;
RA   Brethour D., Mehrabian M., Williams D., Wang X., Ghodrati F., Ehsani S.,
RA   Rubie E.A., Woodgett J.R., Sevalle J., Xi Z., Rogaeva E., Schmitt-Ulms G.;
RT   "A ZIP6-ZIP10 heteromer controls NCAM1 phosphorylation and integration into
RT   focal adhesion complexes during epithelial-to-mesenchymal transition.";
RL   Sci. Rep. 7:40313-40313(2017).
CC   -!- FUNCTION: Zinc-influx transporter which plays a role in zinc
CC       homeostasis and in the induction of epithelial-to-mesenchymal
CC       transition (EMT) (PubMed:28098160). When associated with SLC39A10, the
CC       heterodimer formed by SLC39A10 and SLC39A6 mediates cellular zinc
CC       uptake to trigger cells to undergo epithelial- to-mesenchymal
CC       transition (EMT) (By similarity). The SLC39A10-SLC39A6 heterodimer also
CC       controls NCAM1 phosphorylation and its integration into focal adhesion
CC       complexes during EMT (PubMed:28098160). Zinc influx inactivates GSK3B,
CC       enabling unphosphorylated SNAI1 in the nucleus to down-regulate
CC       adherence genes such as E-cadherin, causing loss of cell adherence (By
CC       similarity). In addition, the SLC39A10-SLC39A6 heterodimer plays an
CC       essentiel role in initiating mitosis by importing zinc into cells to
CC       initiate a pathway resulting in the onset of mitosis (By similarity).
CC       Participates in the T-cell receptor signaling regulation by mediating
CC       cellular zinc uptake into activated lymphocytes (By similarity).
CC       Regulates the zinc influx necessary for proper meiotic progression to
CC       metaphase II (MII) that allows the oocyte-to-egg transition
CC       (PubMed:25143461). {ECO:0000250|UniProtKB:Q13433,
CC       ECO:0000250|UniProtKB:Q6L8F3, ECO:0000269|PubMed:25143461,
CC       ECO:0000269|PubMed:28098160}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351,
CC         ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q13433};
CC   -!- SUBUNIT: Interacts with SLC39A10; which triggers cells to undergo EMT
CC       and mitosis. Found in a complex with SLC39A6, SLC39A10 and with the
CC       'Ser-727' phosphorylated form of STAT3 throughout mitosis (By
CC       similarity). Found in a complex with SLC39A6, SLC39A10 and with NCAM1;
CC       this complex controls NCAM1 phosphorylation and integration into focal
CC       adhesion complexes during epithelial-to-mesenchymal transition (EMT)
CC       (PubMed:28098160). Found in a complex with SLC39A6, SLC39A10 and with
CC       GSK3B that controls NCAM1 phosphorylation (PubMed:28098160).
CC       {ECO:0000250|UniProtKB:Q13433, ECO:0000269|PubMed:28098160}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25143461};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13433}. Cell
CC       projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q13433};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13433}. Membrane
CC       raft {ECO:0000250|UniProtKB:Q13433}; Multi-pass membrane protein
CC       {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q4V887}.
CC       Note=Localizes to lipid rafts in T cells and is recruited into the
CC       immunological synapse in response to TCR stimulation (By similarity).
CC       In the choroid plexus is limited to the apical membrane in epithelial
CC       cells (By similarity). {ECO:0000250|UniProtKB:Q13433,
CC       ECO:0000250|UniProtKB:Q4V887}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain and testis. In the
CC       brain strongly expressed in the CA1 and CA3 regions, Purkinje cells in
CC       cerebellum and dentate gyrus in hippocampus. In testis found in
CC       spermatids or mature sperms in the central areas of seminiferous
CC       tubules. {ECO:0000269|PubMed:11891044}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the oocyte and egg but
CC       decreased and remained low after fertilization (PubMed:25143461).
CC       During preimplantation embryos, localizes to the cortex
CC       (PubMed:25143461). {ECO:0000269|PubMed:25143461}.
CC   -!- INDUCTION: Induced during neuronal differentiation neuroblastoma cells
CC       line but down-regulated during myogenic differentiation of skeletal
CC       muscle cells line (PubMed:11891044). Induced during epithelialto-
CC       mesenchymal transition (EMT) (PubMed:28098160).
CC       {ECO:0000269|PubMed:11891044, ECO:0000269|PubMed:28098160}.
CC   -!- PTM: Cleaved on the N-terminus before locating to the plasma membrane.
CC       {ECO:0000250|UniProtKB:Q13433}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q13433}.
CC   -!- PTM: Phosphorylated by ZAP70 in response to TCR stimulation leading to
CC       its activation. {ECO:0000250|UniProtKB:Q13433}.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH54780.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB86300.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK028976; BAC26223.1; -; mRNA.
DR   EMBL; BC054780; AAH54780.2; ALT_INIT; mRNA.
DR   EMBL; BC055012; AAH55012.1; -; mRNA.
DR   EMBL; AB071697; BAB86300.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS50239.1; -.
DR   RefSeq; NP_631882.2; NM_139143.3.
DR   AlphaFoldDB; Q8C145; -.
DR   BioGRID; 223167; 5.
DR   STRING; 10090.ENSMUSP00000064667; -.
DR   GlyConnect; 2833; 2 N-Linked glycans (2 sites).
DR   GlyCosmos; Q8C145; 5 sites, 2 glycans.
DR   GlyGen; Q8C145; 5 sites, 2 N-linked glycans (2 sites).
DR   iPTMnet; Q8C145; -.
DR   PhosphoSitePlus; Q8C145; -.
DR   SwissPalm; Q8C145; -.
DR   EPD; Q8C145; -.
DR   jPOST; Q8C145; -.
DR   MaxQB; Q8C145; -.
DR   PaxDb; 10090-ENSMUSP00000064667; -.
DR   PeptideAtlas; Q8C145; -.
DR   ProteomicsDB; 256684; -.
DR   Pumba; Q8C145; -.
DR   Antibodypedia; 5245; 332 antibodies from 36 providers.
DR   DNASU; 106957; -.
DR   Ensembl; ENSMUST00000070726.10; ENSMUSP00000064667.4; ENSMUSG00000024270.12.
DR   GeneID; 106957; -.
DR   KEGG; mmu:106957; -.
DR   UCSC; uc008egv.1; mouse.
DR   AGR; MGI:2147279; -.
DR   CTD; 25800; -.
DR   MGI; MGI:2147279; Slc39a6.
DR   VEuPathDB; HostDB:ENSMUSG00000024270; -.
DR   eggNOG; KOG2693; Eukaryota.
DR   GeneTree; ENSGT00940000156387; -.
DR   HOGENOM; CLU_015114_13_2_1; -.
DR   InParanoid; Q8C145; -.
DR   OMA; LLMSHGM; -.
DR   OrthoDB; 5488029at2759; -.
DR   PhylomeDB; Q8C145; -.
DR   TreeFam; TF318470; -.
DR   Reactome; R-MMU-442380; Zinc influx into cells by the SLC39 gene family.
DR   BioGRID-ORCS; 106957; 6 hits in 79 CRISPR screens.
DR   ChiTaRS; Slc39a6; mouse.
DR   PRO; PR:Q8C145; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q8C145; Protein.
DR   Bgee; ENSMUSG00000024270; Expressed in hair follicle and 249 other cell types or tissues.
DR   ExpressionAtlas; Q8C145; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0140410; F:monoatomic cation:bicarbonate symporter activity; IBA:GO_Central.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
DR   GO; GO:0006882; P:intracellular zinc ion homeostasis; ISO:MGI.
DR   GO; GO:0046649; P:lymphocyte activation; ISS:UniProtKB.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0071578; P:zinc ion import across plasma membrane; ISS:UniProtKB.
DR   GO; GO:0071577; P:zinc ion transmembrane transport; ISS:UniProtKB.
DR   InterPro; IPR003689; ZIP.
DR   PANTHER; PTHR12191; SOLUTE CARRIER FAMILY 39; 1.
DR   PANTHER; PTHR12191:SF22; ZINC TRANSPORTER ZIP6; 1.
DR   Pfam; PF02535; Zip; 1.
DR   Genevisible; Q8C145; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Coiled coil; Glycoprotein; Ion transport;
KW   Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Transport; Zinc; Zinc transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..765
FT                   /note="Zinc transporter ZIP6"
FT                   /id="PRO_0000041651"
FT   TOPO_DOM        21..335
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q13433"
FT   TRANSMEM        336..356
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..433
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..454
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        455..667
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        668..688
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        689..696
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        697..717
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        718..734
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        735..755
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        756..765
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q13433"
FT   REGION          96..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          475..495
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        96..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13433"
FT   MOD_RES         488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13433"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        694
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        102..107
FT                   /note="Missing (in Ref. 3; BAB86300)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="A -> V (in Ref. 2; AAH55012)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   765 AA;  86380 MW;  C8938B9C3371377B CRC64;
     MATDLSVIMI LTFALWVTSP LHELQSTAAF SQTTEKINSN WEPGVNVDLA VTMQRHHLQQ
     LFYRYGENDS LSVEGFRKLL QNIGIDKIKR VHIHHDHEHH ADHEHHSDHE HHSDHEHHSD
     HEHHSDHEHH SDHEHHSHRS HTVAGKNNRK AFCPDLDSDN SGKNPRTSLG KGSRPAEHMN
     GRRNIKESAS SSEVTSAVYN AVSEGTRFVE TIETPKPGRR TKDVNPSTPP SITEKSRVGR
     LSRLARKKSN ESVSEPRKSF MYSRNTNDNI QECFNTTKLL TSHGMSIQAL LNATEFNYLC
     PAIINQIDAR ACLIHTASEK KAEIPPKTYS LQIAWLGGFI AISIISFLSL LGVILVPLMN
     RVFFKFLLSF LVALAVGTLS GDALLHLLPH SHASHQHSHS HEEPAMEMKR GPLFSHLSAQ
     NIEESSYFDS TWKGLTALGG LYFMFLVEHV LTLIKQFKDK KKKNQKKPEN DEDVESKKQL
     SKYDSQLSSN EEKVDPGERP ESYLRADSQE PSPFDSQQPT MLEEEEVMIA HAHPQEVYNE
     YVPRGCKNKC HSHFHDTLGQ SDDLIHHHHD YHHILHHHHH QNHHPHSHSQ RYSREELKDA
     GIATLAWMVI MGDGLHNFSD GLAIGAAFTE GLSSGLSTSV AVFCHELPHE LGDFAVLLKA
     GMTVKQAVLY NALSAMLAYL GMATGIFIGH YAENVSMWIF ALTAGLFMYV ALVDMVPEML
     HNDASDHGCS RWGYFFLQNA GILLGFGIML LISIFEHKIV FRINF
//