S35B1_HUMAN
ID S35B1_HUMAN Reviewed; 322 AA.
AC P78383; B4DEC4; J3KQV4; Q96EW7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Solute carrier family 35 member B1;
DE AltName: Full=ATP/ADP exchanger ER {ECO:0000303|PubMed:30154480};
DE Short=AXER {ECO:0000303|PubMed:30154480};
DE AltName: Full=Endoplasmic reticulum ATP/ADP translocase {ECO:0000305|PubMed:30154480};
DE AltName: Full=UDP-galactose transporter-related protein 1 {ECO:0000303|PubMed:9010752};
DE Short=UGTrel1 {ECO:0000303|PubMed:9010752};
GN Name=SLC35B1 {ECO:0000303|PubMed:35041824, ECO:0000312|HGNC:HGNC:20798};
GN Synonyms=UGTREL1;
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).
RX PubMed=9010752; DOI=10.1093/oxfordjournals.jbchem.a021523;
RA Ishida N., Miura N., Yoshioka S., Kawakita M.;
RT "Molecular cloning and characterization of a novel isoform of the human
RT UDP-galactose transporter, and of related complementary DNAs belonging to
RT the nucleotide-sugar transporter gene family.";
RL J. Biochem. 120:1074-1078(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-81.
RC TISSUE=Skin;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-29 (ISOFORM 2),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP FUNCTION (ISOFORMS 1 AND 2), TRANSPORTER ACTIVITY (ISOFORMS 1 AND 2),
RP BIOPHYSICOCHEMICAL PROPERTIES (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION.
RX PubMed=30154480; DOI=10.1038/s41467-018-06003-9;
RA Klein M.C., Zimmermann K., Schorr S., Landini M., Klemens P.A.W.,
RA Altensell J., Jung M., Krause E., Nguyen D., Helms V., Rettig J.,
RA Fecher-Trost C., Cavalie A., Hoth M., Bogeski I., Neuhaus H.E.,
RA Zimmermann R., Lang S., Haferkamp I.;
RT "AXER is an ATP/ADP exchanger in the membrane of the endoplasmic
RT reticulum.";
RL Nat. Commun. 9:3489-3489(2018).
RN [9]
RP FUNCTION (ISOFORM 1), TRANSPORTER ACTIVITY (ISOFORM 1), BIOPHYSICOCHEMICAL
RP PROPERTIES (ISOFORM 1), AND MUTAGENESIS OF LYS-117; LYS-120; ARG-276 AND
RP LYS-277.
RX PubMed=35041824; DOI=10.1016/j.jbc.2021.101537;
RA Schwarzbaum P.J., Schachter J., Bredeston L.M.;
RT "The broad range di- and trinucleotide exchanger SLC35B1 displays
RT asymmetrical affinities for ATP transport across the ER membrane.";
RL J. Biol. Chem. 299:101537-101537(2022).
CC -!- FUNCTION: ATP:ADP antiporter that catalyzes the exchange of ATP and ADP
CC across the endoplasmic reticulum (ER) membrane. Imports ATP from the
CC cytosol to the ER lumen and exports ADP in the opposite direction
CC (PubMed:30154480, PubMed:35041824). Regulates ER energy metabolism and
CC protein biogenesis. Appears to be part of a calcium-dependent ER to
CC cytosol low energy response axis, where calcium efflux from ER to the
CC cytosol triggers ATP import into the ER lumen to maintain sufficient
CC ATP supply. Provides ATP to ER chaperone HSPA5 that drives protein
CC folding and trafficking in the ER (PubMed:30154480, PubMed:35041824).
CC Can transport UTP or UDP in exchange for ATP, but the physiological
CC relevance of this process remains to be established (PubMed:30154480,
CC PubMed:35041824). {ECO:0000269|PubMed:30154480,
CC ECO:0000269|PubMed:35041824}.
CC -!- FUNCTION: [Isoform 1]: ATP:ADP antiporter.
CC {ECO:0000269|PubMed:30154480, ECO:0000269|PubMed:35041824}.
CC -!- FUNCTION: [Isoform 2]: ATP:ADP antiporter.
CC {ECO:0000269|PubMed:30154480}.
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:30154480, ECO:0000269|PubMed:35041824};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35001;
CC Evidence={ECO:0000305|PubMed:30154480, ECO:0000305|PubMed:35041824};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:30154480};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35001;
CC Evidence={ECO:0000305|PubMed:30154480};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC Kinetic parameters:
CC KM=34.7 uM for ATP {ECO:0000269|PubMed:30154480};
CC KM=37.3 uM for ADP {ECO:0000269|PubMed:30154480};
CC Vmax=871 pmol/h/mg enzyme toward ATP {ECO:0000269|PubMed:30154480};
CC Vmax=962.3 pmol/h/mg enzyme toward ADP {ECO:0000269|PubMed:30154480};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:35041824};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]:
CC Kinetic parameters:
CC KM=28.7 uM for ATP {ECO:0000269|PubMed:30154480};
CC KM=22.5 uM for ADP {ECO:0000269|PubMed:30154480};
CC Vmax=676.8 pmol/h/mg enzyme toward ATP {ECO:0000269|PubMed:30154480};
CC Vmax=710.5 pmol/h/mg enzyme toward ADP {ECO:0000269|PubMed:30154480};
CC -!- INTERACTION:
CC P78383; Q13520: AQP6; NbExp=3; IntAct=EBI-12147661, EBI-13059134;
CC P78383; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12147661, EBI-11343438;
CC P78383; Q12983: BNIP3; NbExp=3; IntAct=EBI-12147661, EBI-749464;
CC P78383; Q8WV48: CCDC107; NbExp=3; IntAct=EBI-12147661, EBI-947033;
CC P78383; P04233-2: CD74; NbExp=3; IntAct=EBI-12147661, EBI-12222807;
CC P78383; P11912: CD79A; NbExp=3; IntAct=EBI-12147661, EBI-7797864;
CC P78383; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12147661, EBI-6942903;
CC P78383; Q14318: FKBP8; NbExp=3; IntAct=EBI-12147661, EBI-724839;
CC P78383; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-12147661, EBI-12175685;
CC P78383; Q13467: FZD5; NbExp=3; IntAct=EBI-12147661, EBI-3913027;
CC P78383; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12147661, EBI-13345167;
CC P78383; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12147661, EBI-11956541;
CC P78383; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-12147661, EBI-716063;
CC P78383; P54829: PTPN5; NbExp=3; IntAct=EBI-12147661, EBI-1220572;
CC P78383; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-12147661, EBI-1059156;
CC P78383; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-12147661, EBI-744988;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30154480}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P78383-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78383-2; Sequence=VSP_054234;
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B
CC subfamily. {ECO:0000305}.
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DR EMBL; D87989; BAA13525.1; -; mRNA.
DR EMBL; AK293563; BAG57035.1; -; mRNA.
DR EMBL; AC015795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94666.1; -; Genomic_DNA.
DR EMBL; BC011888; AAH11888.1; -; mRNA.
DR CCDS; CCDS11552.2; -. [P78383-1]
DR PIR; JC5024; JC5024.
DR RefSeq; NP_005818.2; NM_005827.2. [P78383-1]
DR AlphaFoldDB; P78383; -.
DR SMR; P78383; -.
DR BioGRID; 115531; 23.
DR IntAct; P78383; 21.
DR MINT; P78383; -.
DR STRING; 9606.ENSP00000240333; -.
DR TCDB; 2.A.7.11.1; the drug/metabolite transporter (dmt) superfamily.
DR iPTMnet; P78383; -.
DR BioMuta; SLC35B1; -.
DR DMDM; 74735602; -.
DR EPD; P78383; -.
DR jPOST; P78383; -.
DR MassIVE; P78383; -.
DR MaxQB; P78383; -.
DR PaxDb; P78383; -.
DR PeptideAtlas; P78383; -.
DR PRIDE; P78383; -.
DR ProteomicsDB; 57608; -. [P78383-1]
DR Antibodypedia; 17968; 70 antibodies from 19 providers.
DR DNASU; 10237; -.
DR Ensembl; ENST00000240333.12; ENSP00000240333.8; ENSG00000121073.15. [P78383-1]
DR Ensembl; ENST00000649906.1; ENSP00000497423.1; ENSG00000121073.15. [P78383-2]
DR GeneID; 10237; -.
DR KEGG; hsa:10237; -.
DR MANE-Select; ENST00000240333.12; ENSP00000240333.8; NM_005827.4; NP_005818.3.
DR UCSC; uc002iph.3; human. [P78383-1]
DR CTD; 10237; -.
DR GeneCards; SLC35B1; -.
DR HGNC; HGNC:20798; SLC35B1.
DR HPA; ENSG00000121073; Low tissue specificity.
DR MIM; 610790; gene.
DR neXtProt; NX_P78383; -.
DR OpenTargets; ENSG00000121073; -.
DR PharmGKB; PA134864001; -.
DR VEuPathDB; HostDB:ENSG00000121073; -.
DR eggNOG; KOG1580; Eukaryota.
DR GeneTree; ENSGT00940000157900; -.
DR HOGENOM; CLU_036019_1_0_1; -.
DR InParanoid; P78383; -.
DR OrthoDB; 1220063at2759; -.
DR PhylomeDB; P78383; -.
DR TreeFam; TF105967; -.
DR PathwayCommons; P78383; -.
DR SignaLink; P78383; -.
DR BioGRID-ORCS; 10237; 610 hits in 983 CRISPR screens.
DR ChiTaRS; SLC35B1; human.
DR GenomeRNAi; 10237; -.
DR Pharos; P78383; Tdark.
DR PRO; PR:P78383; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P78383; protein.
DR Bgee; ENSG00000121073; Expressed in islet of Langerhans and 200 other tissues.
DR ExpressionAtlas; P78383; baseline and differential.
DR Genevisible; P78383; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005459; F:UDP-galactose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005460; F:UDP-glucose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0072334; P:UDP-galactose transmembrane transport; IBA:GO_Central.
DR InterPro; IPR013657; UAA.
DR PANTHER; PTHR10778; PTHR10778; 1.
DR Pfam; PF08449; UAA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..322
FT /note="Solute carrier family 35 member B1"
FT /id="PRO_0000213366"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 318..322
FT /note="Di-lysine motif"
FT VAR_SEQ 1
FT /note="M -> MRPLPPVGDVRLELSPPPPLLPVPVVSGSPVGSSGRLM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054234"
FT VARIANT 81
FT /note="R -> H (in dbSNP:rs1135034)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_023778"
FT MUTAGEN 117
FT /note="K->A: Loss of ATP:ADP antiporter activity."
FT /evidence="ECO:0000269|PubMed:35041824"
FT MUTAGEN 120
FT /note="K->A: Loss of ATP:ADP antiporter activity."
FT /evidence="ECO:0000269|PubMed:35041824"
FT MUTAGEN 276
FT /note="R->A: Loss of ATP:ADP antiporter activity."
FT /evidence="ECO:0000269|PubMed:35041824"
FT MUTAGEN 277
FT /note="K->A: Loss of ATP:ADP antiporter activity."
FT /evidence="ECO:0000269|PubMed:35041824"
FT CONFLICT 160
FT /note="K -> N (in Ref. 2; BAG57035)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="W -> R (in Ref. 2; BAG57035)"
FT /evidence="ECO:0000305"
FT MOD_RES P78383-2:15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES P78383-2:29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CONFLICT P78383-2:33
FT /note="S -> P (in Ref. 2; BAG57035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35760 MW; 7B5124A4DEC23598 CRC64;
MASSSSLVPD RLRLPLCFLG VFVCYFYYGI LQEKITRGKY GEGAKQETFT FALTLVFIQC
VINAVFAKIL IQFFDTARVD RTRSWLYAAC SISYLGAMVS SNSALQFVNY PTQVLGKSCK
PIPVMLLGVT LLKKKYPLAK YLCVLLIVAG VALFMYKPKK VVGIEEHTVG YGELLLLLSL
TLDGLTGVSQ DHMRAHYQTG SNHMMLNINL WSTLLLGMGI LFTGELWEFL SFAERYPAII
YNILLFGLTS ALGQSFIFMT VVYFGPLTCS IITTTRKFFT ILASVILFAN PISPMQWVGT
VLVFLGLGLD AKFGKGAKKT SH
