ID MOT12_HUMAN Reviewed; 516 AA. AC Q6ZSM3; E9PSF9; Q5M9M9; Q5T7J2; Q6ZV76; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 07-NOV-2018, sequence version 3. DT 27-MAR-2024, entry version 146. DE RecName: Full=Monocarboxylate transporter 12 {ECO:0000305}; DE Short=MCT 12 {ECO:0000305}; DE AltName: Full=Creatine transporter 2 {ECO:0000303|PubMed:23578822}; DE Short=CRT2 {ECO:0000303|PubMed:23578822}; DE AltName: Full=Solute carrier family 16 member 12 {ECO:0000312|HGNC:HGNC:23094}; GN Name=SLC16A12 {ECO:0000312|HGNC:HGNC:23094}; GN Synonyms=MCT12 {ECO:0000303|PubMed:21778275}; 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 [LARGE SCALE MRNA]. RC TISSUE=Hippocampus; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-516. RC TISSUE=Cardiac myocyte, and Skeletal muscle; 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 [4] RP INVOLVEMENT IN CTRCT47, VARIANT CTRCT47 245-GLN--THR-516 DEL, AND TISSUE RP SPECIFICITY. RX PubMed=18304496; DOI=10.1016/j.ajhg.2007.12.013; RA Kloeckener-Gruissem B., Vandekerckhove K., Nuernberg G., Neidhardt J., RA Zeitz C., Nuernberg P., Schipper I., Berger W.; RT "Mutation of solute carrier SLC16A12 associates with a syndrome combining RT juvenile cataract with microcornea and renal glucosuria."; RL Am. J. Hum. Genet. 82:772-779(2008). RN [5] RP CHARACTERIZATION OF VARIANT CTRCT47 245-GLN--THR-516 DEL, INTERACTION WITH RP BSG, AND SUBCELLULAR LOCATION. RX PubMed=21778275; DOI=10.1167/iovs.10-6579; RA Castorino J.J., Gallagher-Colombo S.M., Levin A.V., Fitzgerald P.G., RA Polishook J., Kloeckener-Gruissem B., Ostertag E., Philp N.J.; RT "Juvenile cataract-associated mutation of solute carrier SLC16A12 impairs RT trafficking of the protein to the plasma membrane."; RL Invest. Ophthalmol. Vis. Sci. 52:6774-6784(2011). RN [6] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR RP LOCATION, VARIANT SER-437, CHARACTERIZATION OF VARIANT SER-437, AND TISSUE RP SPECIFICITY. RX PubMed=23578822; DOI=10.1093/hmg/ddt175; RA Abplanalp J., Laczko E., Philp N.J., Neidhardt J., Zuercher J., Braun P., RA Schorderet D.F., Munier F.L., Verrey F., Berger W., Camargo S.M., RA Kloeckener-Gruissem B.; RT "The cataract and glucosuria associated monocarboxylate transporter MCT12 RT is a new creatine transporter."; RL Hum. Mol. Genet. 22:3218-3226(2013). RN [7] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=26376857; DOI=10.1681/asn.2015040411; RA Dhayat N., Simonin A., Anderegg M., Pathare G., Luescher B.P., Deisl C., RA Albano G., Mordasini D., Hediger M.A., Surbek D.V., Vogt B., Sass J.O., RA Kloeckener-Gruissem B., Fuster D.G.; RT "Mutation in the monocarboxylate transporter 12 gene affects RT guanidinoacetate excretion but does not cause glucosuria."; RL J. Am. Soc. Nephrol. 27:1426-1436(2016). RN [8] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND ACTIVITY REGULATION. RX PubMed=31784090; DOI=10.1016/j.bbrc.2019.11.137; RA Futagi Y., Narumi K., Furugen A., Kobayashi M., Iseki K.; RT "Molecular characterization of the orphan transporter SLC16A9, an RT extracellular pH- and Na+-sensitive creatine transporter."; RL Biochem. Biophys. Res. Commun. 522:539-544(2020). RN [9] RP FUNCTION, TRANSPORTER ACTIVITY, MUTAGENESIS OF ARG-67; ASP-95; ASP-329; RP ASP-360 AND ASP-387, AND SUBCELLULAR LOCATION. RX PubMed=32249133; DOI=10.1016/j.dmpk.2020.01.008; RA Takahashi M., Kishimoto H., Shirasaka Y., Inoue K.; RT "Functional characterization of monocarboxylate transporter 12 RT (SLC16A12/MCT12) as a facilitative creatine transporter."; RL Drug Metab. Pharmacokinet. 35:281-287(2020). RN [10] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=32781157; DOI=10.1016/j.bbamem.2020.183434; RA Jomura R., Tanno Y., Akanuma S.I., Kubo Y., Tachikawa M., Hosoya K.I.; RT "Monocarboxylate transporter 12 as a guanidinoacetate efflux transporter in RT renal proximal tubular epithelial cells."; RL Biochim. Biophys. Acta 1862:183434-183434(2020). CC -!- FUNCTION: Functions as a transporter for creatine and as well for its CC precursor guanidinoacetate. Transport of creatine and GAA is CC independent of resting membrane potential and extracellular Na(+), CC Cl(-), or pH. Contributes to the process of creatine biosynthesis and CC distribution. {ECO:0000269|PubMed:23578822, CC ECO:0000269|PubMed:26376857, ECO:0000269|PubMed:31784090, CC ECO:0000269|PubMed:32249133, ECO:0000269|PubMed:32781157}. CC -!- CATALYTIC ACTIVITY: CC Reaction=creatine(in) = creatine(out); Xref=Rhea:RHEA:73043, CC ChEBI:CHEBI:57947; Evidence={ECO:0000269|PubMed:23578822, CC ECO:0000269|PubMed:26376857, ECO:0000269|PubMed:31784090, CC ECO:0000269|PubMed:32249133, ECO:0000269|PubMed:32781157}; CC -!- CATALYTIC ACTIVITY: CC Reaction=guanidinoacetate(in) = guanidinoacetate(out); CC Xref=Rhea:RHEA:73047, ChEBI:CHEBI:57742; CC Evidence={ECO:0000269|PubMed:32781157}; CC -!- ACTIVITY REGULATION: Creatine uptake is inhibited by carbonyl cyanide CC 3-chlorophenylhydrazone (CCCP) and by valinomycin. CC {ECO:0000269|PubMed:23578822}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.57 mM for creatine {ECO:0000269|PubMed:23578822}; CC KM=0.32 mM for creatine {ECO:0000269|PubMed:31784090}; CC -!- SUBUNIT: Interacts with isoform 2 of BSG; this interaction is required CC for its localization to the plasma membrane. CC {ECO:0000269|PubMed:21778275}. CC -!- INTERACTION: CC Q6ZSM3; Q13520: AQP6; NbExp=3; IntAct=EBI-17460560, EBI-13059134; CC Q6ZSM3; P11912: CD79A; NbExp=3; IntAct=EBI-17460560, EBI-7797864; CC Q6ZSM3; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-17460560, EBI-12175685; CC Q6ZSM3; P48165: GJA8; NbExp=3; IntAct=EBI-17460560, EBI-17458373; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21778275, CC ECO:0000269|PubMed:23578822, ECO:0000269|PubMed:31784090, CC ECO:0000269|PubMed:32249133}; Multi-pass membrane protein CC {ECO:0000255}. Basolateral cell membrane CC {ECO:0000250|UniProtKB:Q8BGC3}; Multi-pass membrane protein CC {ECO:0000255}. Note=Interaction with isoform 2 of BSG is required for CC its localization to the plasma membrane. {ECO:0000269|PubMed:26376857}. CC -!- TISSUE SPECIFICITY: Most highly expressed in kidney, followed by CC retina, lung, heart and testis. Very weakly expressed in brain and CC liver. Also detected in lens. {ECO:0000269|PubMed:18304496, CC ECO:0000269|PubMed:23578822}. CC -!- DISEASE: Cataract 47 (CTRCT47) [MIM:612018]: A form of cataract, an CC opacification of the crystalline lens of the eye that frequently CC results in visual impairment or blindness. Opacities vary in CC morphology, are often confined to a portion of the lens, and may be CC static or progressive. In general, the more posteriorly located and CC dense an opacity, the greater the impact on visual function. CTRCT47 is CC characterized by the association of cataract with microcornea and renal CC glucosuria. Microcornea is defined by a corneal diameter inferior to 10 CC mm in both meridians in an otherwise normal eye. Renal glucosuria is CC defined by elevated glucose level in the urine without hyperglycemia CC and without evidence of morphological renal anomalies. CC {ECO:0000269|PubMed:18304496, ECO:0000269|PubMed:21778275}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-31 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC85987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC86925.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK124901; BAC85987.1; ALT_INIT; mRNA. DR EMBL; AK127303; BAC86925.1; ALT_FRAME; mRNA. DR EMBL; AL353146; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC086873; AAH86873.1; -; mRNA. DR CCDS; CCDS7404.2; -. DR RefSeq; NP_998771.3; NM_213606.3. DR RefSeq; XP_016871726.1; XM_017016237.1. DR RefSeq; XP_016871727.1; XM_017016238.1. DR RefSeq; XP_016871728.1; XM_017016239.1. DR AlphaFoldDB; Q6ZSM3; -. DR SMR; Q6ZSM3; -. DR BioGRID; 132399; 4. DR IntAct; Q6ZSM3; 4. DR STRING; 9606.ENSP00000360855; -. DR TCDB; 2.A.1.13.14; the major facilitator superfamily (mfs). DR iPTMnet; Q6ZSM3; -. DR PhosphoSitePlus; Q6ZSM3; -. DR BioMuta; SLC16A12; -. DR DMDM; 147704293; -. DR MassIVE; Q6ZSM3; -. DR PaxDb; 9606-ENSP00000360855; -. DR PeptideAtlas; Q6ZSM3; -. DR Antibodypedia; 16234; 157 antibodies from 24 providers. DR DNASU; 387700; -. DR Ensembl; ENST00000371790.5; ENSP00000360855.4; ENSG00000152779.14. DR GeneID; 387700; -. DR KEGG; hsa:387700; -. DR MANE-Select; ENST00000371790.5; ENSP00000360855.4; NM_213606.4; NP_998771.3. DR AGR; HGNC:23094; -. DR CTD; 387700; -. DR DisGeNET; 387700; -. DR GeneCards; SLC16A12; -. DR HGNC; HGNC:23094; SLC16A12. DR HPA; ENSG00000152779; Tissue enhanced (choroid plexus, epididymis, kidney). DR MalaCards; SLC16A12; -. DR MIM; 611910; gene. DR MIM; 612018; phenotype. DR neXtProt; NX_Q6ZSM3; -. DR OpenTargets; ENSG00000152779; -. DR Orphanet; 247794; Juvenile cataract-microcornea-renal glucosuria syndrome. DR PharmGKB; PA134969386; -. DR VEuPathDB; HostDB:ENSG00000152779; -. DR eggNOG; KOG2504; Eukaryota. DR GeneTree; ENSGT00940000156169; -. DR HOGENOM; CLU_001265_59_1_1; -. DR InParanoid; Q6ZSM3; -. DR OMA; WVLASHQ; -. DR OrthoDB; 2904526at2759; -. DR PhylomeDB; Q6ZSM3; -. DR TreeFam; TF313792; -. DR PathwayCommons; Q6ZSM3; -. DR SignaLink; Q6ZSM3; -. DR BioGRID-ORCS; 387700; 8 hits in 1138 CRISPR screens. DR ChiTaRS; SLC16A12; human. DR GenomeRNAi; 387700; -. DR Pharos; Q6ZSM3; Tbio. DR PRO; PR:Q6ZSM3; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q6ZSM3; Protein. DR Bgee; ENSG00000152779; Expressed in body of pancreas and 93 other cell types or tissues. DR ExpressionAtlas; Q6ZSM3; baseline and differential. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005308; F:creatine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015292; F:uniporter activity; IDA:UniProtKB. DR GO; GO:0015881; P:creatine transmembrane transport; IDA:UniProtKB. DR GO; GO:0046449; P:creatinine metabolic process; IEA:Ensembl. DR GO; GO:0015718; P:monocarboxylic acid transport; IBA:GO_Central. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR CDD; cd17424; MFS_MCT12; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR11360; MONOCARBOXYLATE TRANSPORTER; 1. DR PANTHER; PTHR11360:SF315; MONOCARBOXYLATE TRANSPORTER 12; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. PE 1: Evidence at protein level; KW Cataract; Cell membrane; Disease variant; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..516 FT /note="Monocarboxylate transporter 12" FT /id="PRO_0000286675" FT TOPO_DOM 1..50 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 51..73 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 88..108 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 116..136 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 145..165 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 178..198 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 207..227 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 283..303 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 319..339 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 350..370 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 377..397 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 410..430 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 440..460 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 461..516 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT VARIANT 245..516 FT /note="Missing (in CTRCT47; loss of localization to the FT plasma membrane; retained in the endoplasmic reticulum FT where it undergoes degradation by the proteasome; has no FT dominant effect on wild-type protein expression and FT localization)" FT /evidence="ECO:0000269|PubMed:18304496" FT /id="VAR_080957" FT VARIANT 437 FT /note="G -> S (found in a patient with age-related FT cataract; uncertain significance; decreases creatine FT transport; dbSNP:rs759863805)" FT /evidence="ECO:0000269|PubMed:23578822" FT /id="VAR_071890" FT MUTAGEN 67 FT /note="R->A: Abolishes creatine efflux activity. Does not FT affect plasma membrane localization." FT /evidence="ECO:0000269|PubMed:32249133" FT MUTAGEN 95 FT /note="D->A: Decreases in the creatine efflux activity. FT Does not affect plasma membrane localization." FT /evidence="ECO:0000269|PubMed:32249133" FT MUTAGEN 329 FT /note="D->A: Decreases creatine efflux activity. Loss of FT localization to the plasma membrane." FT /evidence="ECO:0000269|PubMed:32249133" FT MUTAGEN 360 FT /note="D->A: Does not affect creatine efflux activity. Does FT not affect plasma membrane localization." FT /evidence="ECO:0000269|PubMed:32249133" FT MUTAGEN 387 FT /note="D->A: Does not affect creatine efflux activity." FT /evidence="ECO:0000269|PubMed:32249133" FT CONFLICT 334 FT /note="I -> T (in Ref. 1; BAC86925)" FT /evidence="ECO:0000305" FT CONFLICT 363 FT /note="C -> S (in Ref. 1; BAC85987)" FT /evidence="ECO:0000305" SQ SEQUENCE 516 AA; 56498 MW; 467BF0C95C98052A CRC64; MPSGSHWTAN SSKIITWLLE QPGKEEKRKT MAKVNRARST SPPDGGWGWM IVAGCFLVTI CTRAVTRCIS IFFVEFQTYF TQDYAQTAWI HSIVDCVTML CAPLGSVVSN HLSCQVGIML GGLLASTGLI LSSFATSLKH LYLTLGVLTG LGFALCYSPA IAMVGKYFSR RKALAYGIAM SGSGIGTFIL APVVQLLIEQ FSWRGALLIL GGFVLNLCVC GALMRPITLK EDHTTPEQNH VCRTQKEDIK RVSPYSSLTK EWAQTCLCCC LQQEYSFLLM SDFVVLAVSV LFMAYGCSPL FVYLVPYALS VGVSHQQAAF LMSILGVIDI IGNITFGWLT DRRCLKNYQY VCYLFAVGMD GLCYLCLPML QSLPLLVPFS CTFGYFDGAY VTLIPVVTTE IVGTTSLSSA LGVVYFLHAV PYLVSPPIAG RLVDTTGSYT AAFLLCGFSM IFSSVLLGFA RLIKRMRKTQ LQFIAKESDP KLQLWTNGSV AYSVARELDQ KHGEPVATAV PGYSLT //