S15A1_MOUSE
ID S15A1_MOUSE Reviewed; 709 AA.
AC Q9JIP7; E9QMX3;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Solute carrier family 15 member 1 {ECO:0000305};
DE AltName: Full=Intestinal H(+)/peptide cotransporter {ECO:0000303|PubMed:11004485};
DE AltName: Full=Oligopeptide transporter, small intestine isoform {ECO:0000303|PubMed:11004485};
DE AltName: Full=Peptide transporter 1 {ECO:0000303|PubMed:11004485};
DE AltName: Full=Proton-coupled dipeptide cotransporter;
GN Name=Slc15a1 {ECO:0000312|MGI:MGI:1861376};
GN Synonyms=Pept1 {ECO:0000303|PubMed:11004485};
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].
RC STRAIN=129/SvJ;
RX PubMed=11004485; DOI=10.1016/s0167-4781(00)00101-9;
RA Fei Y.-J., Sugawara M., Liu J.-C., Li H.W., Ganapathy V., Ganapathy M.E.,
RA Leibach F.H.;
RT "cDNA structure, genomic organization, and promoter analysis of the mouse
RT intestinal peptide transporter PEPT1.";
RL Biochim. Biophys. Acta 1492:145-154(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-439 AND ASN-515.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [5] {ECO:0007744|PDB:5A9D}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 391-579, FUNCTION, TRANSPORTER
RP ACTIVITY, DOMAIN, INTERACTION WITH TRYPSIN, AND MUTAGENESIS OF
RP 453-HIS--GLU-456; 472-ARG--LYS-475; ASP-476; GLU-509; ASN-515; ASP-550 AND
RP GLU-573.
RX PubMed=26320580; DOI=10.1016/j.str.2015.07.016;
RA Beale J.H., Parker J.L., Samsudin F., Barrett A.L., Senan A., Bird L.E.,
RA Scott D., Owens R.J., Sansom M.S.P., Tucker S.J., Meredith D., Fowler P.W.,
RA Newstead S.;
RT "Crystal structures of the extracellular domain from PepT1 and PepT2
RT provide novel insights into mammalian peptide transport.";
RL Structure 23:1889-1899(2015).
CC -!- FUNCTION: Proton-coupled amino-acid transporter that transports
CC oligopeptides of 2 to 4 amino acids with a preference for dipeptides
CC (PubMed:11004485, PubMed:26320580). Primarily responsible for the
CC absorption of dietary di- and tripeptides from the small intestinal
CC lumen (By similarity). {ECO:0000250|UniProtKB:P36836,
CC ECO:0000269|PubMed:11004485, ECO:0000269|PubMed:26320580}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dipeptide(out) + H(+)(out) = a dipeptide(in) + H(+)(in);
CC Xref=Rhea:RHEA:64392, ChEBI:CHEBI:15378, ChEBI:CHEBI:90799;
CC Evidence={ECO:0000269|PubMed:26320580};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000269|PubMed:26320580};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-amino acid tripeptide(out) + H(+)(out) = an L-amino acid
CC tripeptide(in) + H(+)(in); Xref=Rhea:RHEA:64400, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155837; Evidence={ECO:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64401;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-sarcosine(out) + H(+)(out) = glycyl-sarcosine(in) +
CC H(+)(in); Xref=Rhea:RHEA:64396, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155838; Evidence={ECO:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64397;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-alanyl-L-proline(out) = H(+)(in) + L-alanyl-L-
CC proline(in); Xref=Rhea:RHEA:64420, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155848; Evidence={ECO:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64421;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-leucyl-L-proline(out) = H(+)(in) + L-leucyl-L-
CC proline(in); Xref=Rhea:RHEA:64424, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155847; Evidence={ECO:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64425;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-L-proline(out) + H(+)(out) = glycyl-L-proline(in) +
CC H(+)(in); Xref=Rhea:RHEA:64428, ChEBI:CHEBI:15378, ChEBI:CHEBI:73779;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64429;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-alanyl-L-prolylglycine(out) = H(+)(in) + L-
CC alanyl-L-prolylglycine(in); Xref=Rhea:RHEA:64432, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155849; Evidence={ECO:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64433;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycylglycyl-L-isoleucine(out) + H(+)(out) = glycylglycyl-L-
CC isoleucine(in) + H(+)(in); Xref=Rhea:RHEA:64436, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155850; Evidence={ECO:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64437;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycylglycyl-L-proline(out) + H(+)(out) = glycylglycyl-L-
CC proline(in) + H(+)(in); Xref=Rhea:RHEA:64440, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:155851; Evidence={ECO:0000250|UniProtKB:P46059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64441;
CC Evidence={ECO:0000250|UniProtKB:P46059};
CC -!- SUBUNIT: Interacts (via extracellular domain region) with trypsin.
CC {ECO:0000269|PubMed:26320580}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11004485}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The extracellular domain (ECD) region specifically binds
CC trypsin. {ECO:0000269|PubMed:26320580}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
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DR EMBL; AF205540; AAF81666.1; -; mRNA.
DR EMBL; AC126253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37017.1; -.
DR RefSeq; NP_444309.2; NM_053079.2.
DR PDB; 5A9D; X-ray; 2.10 A; A/B=391-579.
DR PDBsum; 5A9D; -.
DR AlphaFoldDB; Q9JIP7; -.
DR SMR; Q9JIP7; -.
DR IntAct; Q9JIP7; 1.
DR STRING; 10090.ENSMUSP00000085728; -.
DR BindingDB; Q9JIP7; -.
DR ChEMBL; CHEMBL2073714; -.
DR GlyGen; Q9JIP7; 5 sites.
DR iPTMnet; Q9JIP7; -.
DR PhosphoSitePlus; Q9JIP7; -.
DR MaxQB; Q9JIP7; -.
DR PaxDb; Q9JIP7; -.
DR PRIDE; Q9JIP7; -.
DR ProteomicsDB; 253351; -.
DR Antibodypedia; 10820; 230 antibodies from 31 providers.
DR DNASU; 56643; -.
DR Ensembl; ENSMUST00000088386; ENSMUSP00000085728; ENSMUSG00000025557.
DR GeneID; 56643; -.
DR KEGG; mmu:56643; -.
DR UCSC; uc007vad.1; mouse.
DR CTD; 6564; -.
DR MGI; MGI:1861376; Slc15a1.
DR VEuPathDB; HostDB:ENSMUSG00000025557; -.
DR eggNOG; KOG1237; Eukaryota.
DR GeneTree; ENSGT00940000155995; -.
DR HOGENOM; CLU_004790_3_0_1; -.
DR InParanoid; Q9JIP7; -.
DR OMA; YNASEYQ; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q9JIP7; -.
DR TreeFam; TF330897; -.
DR BRENDA; 7.4.2.5; 3474.
DR Reactome; R-MMU-427975; Proton/oligopeptide cotransporters.
DR BioGRID-ORCS; 56643; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9JIP7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JIP7; protein.
DR Bgee; ENSMUSG00000025557; Expressed in epithelium of small intestine and 48 other tissues.
DR Genevisible; Q9JIP7; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016248; F:channel inhibitor activity; ISO:MGI.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015333; F:peptide:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; IDA:MGI.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0051956; P:negative regulation of amino acid transport; ISO:MGI.
DR GO; GO:0006857; P:oligopeptide transport; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004768; Oligopep_transport.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00926; 2A1704; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..709
FT /note="Solute carrier family 15 member 1"
FT /id="PRO_0000064305"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..585
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..646
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 383..585
FT /note="Extracellular domain (ECD)"
FT /evidence="ECO:0000303|PubMed:26320580"
FT REGION 690..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 453..456
FT /note="HDFE->AAFA,ERFR: Does not affect trypsin-binding."
FT /evidence="ECO:0000269|PubMed:26320580"
FT MUTAGEN 472..475
FT /note="RVVK->AVVA,EVVE: Does not affect trypsin-binding."
FT /evidence="ECO:0000269|PubMed:26320580"
FT MUTAGEN 476
FT /note="D->A: Does not affect trypsin-binding."
FT /evidence="ECO:0000269|PubMed:26320580"
FT MUTAGEN 509
FT /note="E->R: Does not affect trypsin-binding."
FT /evidence="ECO:0000269|PubMed:26320580"
FT MUTAGEN 515
FT /note="N->A: Does not affect trypsin-binding."
FT /evidence="ECO:0000269|PubMed:26320580"
FT MUTAGEN 550
FT /note="D->A: Reduced trypsin-binding; when associated with
FT A-573."
FT /evidence="ECO:0000269|PubMed:26320580"
FT MUTAGEN 573
FT /note="E->A: Reduced trypsin-binding; when associated with
FT A-550."
FT /evidence="ECO:0000269|PubMed:26320580"
FT CONFLICT 287
FT /note="Y -> F (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="A -> G (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="I -> N (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 333..339
FT /note="IVIMVPI -> NVNNGPN (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..347
FT /note="PL -> RS (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="T -> N (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="N -> E (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="L -> P (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="I -> N (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 510..511
FT /note="NV -> KF (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT CONFLICT 520..522
FT /note="QFF -> KFL (in Ref. 1; AAF81666)"
FT /evidence="ECO:0000305"
FT STRAND 393..401
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:5A9D"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:5A9D"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 470..480
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 506..511
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 554..561
FT /evidence="ECO:0007829|PDB:5A9D"
FT STRAND 565..574
FT /evidence="ECO:0007829|PDB:5A9D"
SQ SEQUENCE 709 AA; 78560 MW; 7DF0D0F9068CD046 CRC64;
MGMSKSRGCF GYPLSIFFIV VNEFCERFSY YGMRALLVLY FRNFLGWDDN LSTAIYHTFV
ALCYLTPILG ALIADSWLGK FKTIVSLSIV YTIGQAVISV SSINDLTDHD HNGSPDSLPV
HVALSMVGLA LIALGTGGIK PCVSAFGGDQ FEEGQEKQRN RFFSIFYLAI NGGSLLSTII
TPILRVQQCG IHSQQACYPL AFGVPAALMA VALIVFVLGS GMYKKFQPQG NIMGKVAKCI
GFAIKNRFRH RSKAYPKREH WLDWAKEKYD ERLISQIKMV TKVMFLYIPL PMFWALFDQQ
GSRWTLQATT MNGKIGAIEI QPDQMQTVNA ILIVIMVPIV DAVVYPLIAK CGFNFTSLKK
MTVGMFLASM AFVVAAIVQV EIDKTLPVFP GGNQVQIKVL NIGNNNMTVH FPGNSVTLAQ
MSQTDTFMTF DIDKLTSINI SSSGSPGVTT VAHDFEQGHR HTLLVWNPSQ YRVVKDGLNQ
KPEKGENGIR FVNTLNEMVT IKMSGKVYEN VTSHNASGYQ FFPSGEKQYT INTTAVAPTC
LTDFKSSNLD FGSAYTYVIR RASDGCLEVK EFEDIPPNTV NMALQIPQYF LLTCGEVVFS
VTGLEFSYSQ APSNMKSVLQ AGWLLTVAVG NIIVLIVAGA GHFPKQWAEY ILFASLLLVV
CVIFAIMARF YTYINPAEIE AQFDEDEKKK GIGKENPYSS LEPVSQTNM
