ID   MCLN2_MOUSE             Reviewed;         566 AA.
AC   Q8K595; Q3UCG4; Q8K2T6; Q9CQD3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=Mucolipin-2;
DE   AltName: Full=Transient receptor potential channel mucolipin 2;
DE            Short=TRPML2;
GN   Name=Mcoln2;
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 [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=12403827; DOI=10.1073/pnas.222425399;
RA   Di Palma F., Belyantseva I.A., Kim H.J., Vogt T.F., Kachar B.,
RA   Noben-Trauth K.;
RT   "Mutations in Mcoln3 associated with deafness and pigmentation defects in
RT   varitint-waddler (Va) mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14994-14999(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RA   Kennedy J.C., Falardeau J.L., Acierno J.S. Jr., Slaugenhaupt S.A.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary tumor;
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   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17050035; DOI=10.1016/j.ejcb.2006.08.004;
RA   Song Y., Dayalu R., Matthews S.A., Scharenberg A.M.;
RT   "TRPML cation channels regulate the specialized lysosomal compartment of
RT   vertebrate B-lymphocytes.";
RL   Eur. J. Cell Biol. 85:1253-1264(2006).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19763610; DOI=10.1007/s00424-009-0716-5;
RA   Samie M.A., Grimm C., Evans J.A., Curcio-Morelli C., Heller S.,
RA   Slaugenhaupt S.A., Cuajungco M.P.;
RT   "The tissue-specific expression of TRPML2 (MCOLN-2) gene is influenced by
RT   the presence of TRPML1.";
RL   Pflugers Arch. 459:79-91(2009).
RN   [7]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=22753890; DOI=10.1074/jbc.m112.368876;
RA   Grimm C., Joers S., Guo Z., Obukhov A.G., Heller S.;
RT   "Constitutive activity of TRPML2 and TRPML3 channels versus activation by
RT   low extracellular sodium and small molecules.";
RL   J. Biol. Chem. 287:22701-22708(2012).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=26432893; DOI=10.4049/jimmunol.1500163;
RA   Sun L., Hua Y., Vergarajauregui S., Diab H.I., Puertollano R.;
RT   "Novel role of TRPML2 in the regulation of the innate immune response.";
RL   J. Immunol. 195:4922-4932(2015).
CC   -!- FUNCTION: Nonselective cation channel probably playing a role in the
CC       regulation of membrane trafficking events. Acts as a Ca(2+)-permeable
CC       cation channel with inwardly rectifying activity (PubMed:19763610). May
CC       activate ARF6 and be involved in the trafficking of GPI-anchored cargo
CC       proteins to the cell surface via the ARF6-regulated recycling pathway
CC       (By similarity). May play a role in immune processes. In adaptive
CC       immunity, TRPML2 and TRPML1 may play redundant roles in the function of
CC       the specialized lysosomes of B cells (PubMed:17050035). In the innate
CC       immune response, may play a role in the regulation of chemokine
CC       secretion and macrophage migration (PubMed:26432893). Through a
CC       possible and probably tissue-specific heteromerization with MCOLN1 may
CC       be at least in part involved in many lysosome-dependent cellular
CC       events. {ECO:0000250|UniProtKB:Q8IZK6, ECO:0000269|PubMed:17050035,
CC       ECO:0000269|PubMed:19763610, ECO:0000269|PubMed:22753890,
CC       ECO:0000269|PubMed:26432893, ECO:0000305}.
CC   -!- ACTIVITY REGULATION: Channel activity is reduced by low
CC       extracellular/lumenal pH level. {ECO:0000269|PubMed:22753890,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Forms homooligomeric complexes; probably tetrameric. Can
CC       heterooligomerize with MCOLN1; heteromeric assemblies have different
CC       channel properties as compared to the respective homooligomers and may
CC       be tissue-specific. Interacts with TMEM176A.
CC       {ECO:0000250|UniProtKB:Q8IZK6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IZK6};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Lysosome
CC       membrane {ECO:0000305|PubMed:17050035}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:F6RG56}. Recycling endosome membrane
CC       {ECO:0000269|PubMed:26432893}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:F6RG56}. Note=Localizes to recycling endosomes
CC       in activated macrophages and microglia. {ECO:0000269|PubMed:26432893}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=TRPML2lv;
CC         IsoId=Q8K595-1; Sequence=Displayed;
CC       Name=2; Synonyms=TRPML2sv;
CC         IsoId=Q8K595-2; Sequence=VSP_010822;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed at very low levels.
CC       Isoform 2 is expressed at high levels in lymphoid tissues (thymus and
CC       spleen) and kidney, and at moderate levels in heart, lung, liver and
CC       stomach. Expressed in activated macrophages and microglia (at protein
CC       level). {ECO:0000269|PubMed:19763610, ECO:0000269|PubMed:26432893}.
CC   -!- INDUCTION: Up-regulated in microglia cells and macrophages by bacterial
CC       lipopolysaccharide (LPS). Up-regulated by infection with M.smegmatis.
CC       {ECO:0000269|PubMed:26432893}.
CC   -!- DOMAIN: The most N-terminal extracellular/lumenal domain (referred to
CC       as I-II linker or polycystin-mucolipin domain) contributes to a
CC       structure with a four-fold rotational symmetry in a tetrameric
CC       assembly; the structure contains a central highly electronegative pore
CC       with a 14 A diameter. The pore is critical for Ca(2+) and pH
CC       regulation. The protruding structure formed by the I-II linkers may
CC       contain all the interaction sites with lipids and proteins in the
CC       endolysosomal lumen. {ECO:0000250|UniProtKB:Q9GZU1}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. The secretion of specific
CC       cytokines (CCL3, CCL5 and CXCL2) by macrophages exposed to bacterial
CC       lipopolysaccharide (LPS) is decreased. Mutant mice display decreased
CC       migration of macrophages into the intraperitoneal space after injection
CC       with LPS, or after infection with E.coli O78:H11 (strain H10407).
CC       {ECO:0000269|PubMed:26432893}.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC       Polycystin subfamily. MCOLN2 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AY083532; AAM08925.1; -; mRNA.
DR   EMBL; AF503575; AAM28596.1; -; mRNA.
DR   EMBL; AK014467; BAB29372.1; -; mRNA.
DR   EMBL; AK019454; BAB31730.1; -; mRNA.
DR   EMBL; AK150446; BAE29568.1; -; mRNA.
DR   EMBL; AK150547; BAE29649.1; -; mRNA.
DR   EMBL; AK152067; BAE30921.1; -; mRNA.
DR   EMBL; AK152943; BAE31614.1; -; mRNA.
DR   EMBL; AK159172; BAE34872.1; -; mRNA.
DR   EMBL; BC029847; AAH29847.1; -; mRNA.
DR   CCDS; CCDS38663.1; -. [Q8K595-1]
DR   CCDS; CCDS38664.1; -. [Q8K595-2]
DR   RefSeq; NP_001005846.1; NM_001005846.2. [Q8K595-2]
DR   RefSeq; NP_080932.2; NM_026656.4. [Q8K595-1]
DR   PDB; 7DYS; EM; 3.18 A; A/B/C/D=1-518.
DR   PDBsum; 7DYS; -.
DR   AlphaFoldDB; Q8K595; -.
DR   EMDB; EMD-30924; -.
DR   SMR; Q8K595; -.
DR   STRING; 10090.ENSMUSP00000011152; -.
DR   iPTMnet; Q8K595; -.
DR   PhosphoSitePlus; Q8K595; -.
DR   PaxDb; 10090-ENSMUSP00000011152; -.
DR   ProteomicsDB; 292193; -. [Q8K595-1]
DR   ProteomicsDB; 292194; -. [Q8K595-2]
DR   Antibodypedia; 19780; 69 antibodies from 13 providers.
DR   DNASU; 68279; -.
DR   Ensembl; ENSMUST00000011152.14; ENSMUSP00000011152.8; ENSMUSG00000011008.14. [Q8K595-1]
DR   Ensembl; ENSMUST00000098524.5; ENSMUSP00000096125.5; ENSMUSG00000011008.14. [Q8K595-2]
DR   GeneID; 68279; -.
DR   KEGG; mmu:68279; -.
DR   UCSC; uc008rqy.1; mouse. [Q8K595-1]
DR   AGR; MGI:1915529; -.
DR   CTD; 255231; -.
DR   MGI; MGI:1915529; Mcoln2.
DR   VEuPathDB; HostDB:ENSMUSG00000011008; -.
DR   eggNOG; KOG3733; Eukaryota.
DR   GeneTree; ENSGT00950000183036; -.
DR   HOGENOM; CLU_020945_1_1_1; -.
DR   InParanoid; Q8K595; -.
DR   OMA; CDADRWE; -.
DR   OrthoDB; 2877219at2759; -.
DR   PhylomeDB; Q8K595; -.
DR   TreeFam; TF317783; -.
DR   Reactome; R-MMU-3295583; TRP channels.
DR   BioGRID-ORCS; 68279; 3 hits in 62 CRISPR screens.
DR   PRO; PR:Q8K595; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8K595; Protein.
DR   Bgee; ENSMUSG00000011008; Expressed in ileal epithelium and 78 other cell types or tissues.
DR   ExpressionAtlas; Q8K595; baseline and differential.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0072345; F:NAADP-sensitive calcium-release channel activity; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:1905517; P:macrophage migration; IMP:MGI.
DR   GO; GO:1990266; P:neutrophil migration; IMP:MGI.
DR   GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; IMP:MGI.
DR   GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IMP:MGI.
DR   GO; GO:0032722; P:positive regulation of chemokine production; IMP:MGI.
DR   GO; GO:0071642; P:positive regulation of macrophage inflammatory protein 1 alpha production; IMP:MGI.
DR   GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:2000341; P:regulation of chemokine (C-X-C motif) ligand 2 production; IMP:MGI.
DR   Gene3D; 1.10.287.70; -; 1.
DR   InterPro; IPR049134; MCLN_ECD.
DR   InterPro; IPR039031; Mucolipin.
DR   InterPro; IPR013122; PKD1_2_channel.
DR   PANTHER; PTHR12127; MUCOLIPIN; 1.
DR   PANTHER; PTHR12127:SF4; MUCOLIPIN-2; 1.
DR   Pfam; PF21381; MCLN_ECD; 1.
DR   Pfam; PF08016; PKD_channel; 1.
DR   Genevisible; Q8K595; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Alternative splicing; Calcium;
KW   Calcium channel; Calcium transport; Cell membrane; Disulfide bond;
KW   Endosome; Immunity; Innate immunity; Ion channel; Ion transport; Lysosome;
KW   Membrane; Protein transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..566
FT                   /note="Mucolipin-2"
FT                   /id="PRO_0000215366"
FT   TOPO_DOM        1..65
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TOPO_DOM        87..288
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TOPO_DOM        310..346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TOPO_DOM        368..376
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TOPO_DOM        398..419
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TOPO_DOM        441..448
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   INTRAMEM        449..469
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TOPO_DOM        470..480
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TRANSMEM        481..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   TOPO_DOM        503..566
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   REGION          107..123
FT                   /note="Extracellular/lumenal pore loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZU1"
FT   MOTIF           461..464
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:F6RG56"
FT   DISULFID        164..190
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZU1"
FT   DISULFID        243..274
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZU1"
FT   VAR_SEQ         1..28
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12403827,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010822"
FT   CONFLICT        558
FT                   /note="S -> N (in Ref. 4; AAH29847)"
FT                   /evidence="ECO:0000305"
FT   HELIX           67..105
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          123..125
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           126..139
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           141..144
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          147..151
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          160..168
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          186..193
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           195..198
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           209..211
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   TURN            215..217
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          218..229
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   TURN            233..237
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          246..253
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          261..266
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           292..318
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           346..365
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           377..396
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           397..399
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           401..439
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           449..460
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   STRAND          462..464
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           465..470
FT                   /evidence="ECO:0007829|PDB:7DYS"
FT   HELIX           478..516
FT                   /evidence="ECO:0007829|PDB:7DYS"
SQ   SEQUENCE   566 AA;  65450 MW;  314CEC662B3BDC07 CRC64;
     MPGDEETLDL PAWNRVPDLT WGPHHRSAMA SLDSEVREEC LREDLKFYFM SPCEKYRARR
     QIPWKLGLQI LKIVMVTTQL VRFGLSNQLV VAFKEDNTVA FKHLFLKGFS GVDEDDYSCS
     IYTQENTYES IFFAIKQYRH LKNISLATLG YGESEDNRTG LKVCKQHYKT GAMFSSNETL
     NIDSDIETDC IHLDLQVLTT EPEDWAQTSF FRLDFYRLVQ VDISFALKGI DLQAVHSREI
     PDCYLFQNTI TFDNTAHSGK IKIYLNSEAN IEECKNMNIS GSTQRSTHYL LVFDVFVIMI
     CLASLILCTR SIVLALRLRK RFLNFFLEKY KQRVCGADQW EFVNGWYVLV TISDLMTIIG
     SILKMEIKAK KLTNYDVCSI LLGTSTLFVW VGVIRYLGYF QTYNVLILTM QASLPKVLRF
     CACAGMIYLG YTFCGWIVLG PYHEKFENLN IVAECLFSLV NGDDMFATFA QIQQKSILVW
     LFSRLYLYSF ISLFIYMVLS LFIALITDSY HTIKKYQQHG FPETDLQKFL KESGSKDGYQ
     KQPSALLSCL CCLRRRRSND HLILID
//