SFXN1_HUMAN
ID SFXN1_HUMAN Reviewed; 322 AA.
AC Q9H9B4; B3KPW3; D3DQN2; Q9HA53;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Sideroflexin-1 {ECO:0000250|UniProtKB:Q99JR1};
GN Name=SFXN1 {ECO:0000312|HGNC:HGNC:16085};
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].
RA Li N., Chen T., Wan T., Zhang W., Cao X.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland, Prostate, and Teratocarcinoma;
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 MRNA].
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and PNS;
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 [7]
RP PROTEIN SEQUENCE OF 2-12; 16-48; 56-70; 73-86; 137-170; 203-214; 224-233
RP AND 291-314, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=30442778; DOI=10.1126/science.aat9528;
RA Kory N., Wyant G.A., Prakash G., Uit de Bos J., Bottanelli F., Pacold M.E.,
RA Chan S.H., Lewis C.A., Wang T., Keys H.R., Guo Y.E., Sabatini D.M.;
RT "SFXN1 is a mitochondrial serine transporter required for one-carbon
RT metabolism.";
RL Science 362:0-0(2018).
CC -!- FUNCTION: Amino acid transporter importing serine, an essential
CC substrate of the mitochondrial branch of the one-carbon pathway, into
CC mitochondria. Mitochondrial serine is then converted to glycine and
CC formate, which exits to the cytosol where it is used to generate the
CC charged folates that serve as one-carbon donors (PubMed:30442778). May
CC also transport other amino acids including alanine and cysteine
CC (PubMed:30442778). {ECO:0000269|PubMed:30442778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine(in) = L-serine(out); Xref=Rhea:RHEA:35031,
CC ChEBI:CHEBI:33384; Evidence={ECO:0000269|PubMed:30442778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine(in) = L-alanine(out); Xref=Rhea:RHEA:70719,
CC ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:30442778};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine(in) = L-cysteine(out); Xref=Rhea:RHEA:29655,
CC ChEBI:CHEBI:35235; Evidence={ECO:0000305|PubMed:30442778};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=170 uM for L-serine {ECO:0000269|PubMed:30442778};
CC KM=371 uM for L-alanine {ECO:0000269|PubMed:30442778};
CC -!- INTERACTION:
CC Q9H9B4; Q13520: AQP6; NbExp=3; IntAct=EBI-355861, EBI-13059134;
CC Q9H9B4; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-355861, EBI-7062247;
CC Q9H9B4; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-355861, EBI-18053395;
CC Q9H9B4; Q15546: MMD; NbExp=3; IntAct=EBI-355861, EBI-17873222;
CC Q9H9B4; O15173: PGRMC2; NbExp=3; IntAct=EBI-355861, EBI-1050125;
CC Q9H9B4; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-355861, EBI-7545592;
CC Q9H9B4; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-355861, EBI-17247926;
CC Q9H9B4; Q14973: SLC10A1; NbExp=3; IntAct=EBI-355861, EBI-3923031;
CC Q9H9B4; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-355861, EBI-18159983;
CC Q9H9B4; O60669: SLC16A7; NbExp=3; IntAct=EBI-355861, EBI-3921243;
CC Q9H9B4; P27105: STOM; NbExp=3; IntAct=EBI-355861, EBI-1211440;
CC Q9H9B4; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-355861, EBI-12947623;
CC Q9H9B4; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-355861, EBI-8638294;
CC Q9H9B4; Q9Y320: TMX2; NbExp=3; IntAct=EBI-355861, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:30442778}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in tissues with high one-carbon
CC metabolism activity, such as blood, liver and kidney.
CC {ECO:0000269|PubMed:30442778}.
CC -!- SIMILARITY: Belongs to the sideroflexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20517.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14003.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAB14318.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF327346; AAL56007.1; -; mRNA.
DR EMBL; AK022287; BAB14003.1; ALT_SEQ; mRNA.
DR EMBL; AK022938; BAB14318.1; ALT_INIT; mRNA.
DR EMBL; AK056915; BAG51825.1; -; mRNA.
DR EMBL; BX648188; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC091393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61370.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61372.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61374.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61375.1; -; Genomic_DNA.
DR EMBL; BC020517; AAH20517.1; ALT_INIT; mRNA.
DR EMBL; BC063241; AAH63241.1; -; mRNA.
DR CCDS; CCDS4394.1; -.
DR RefSeq; NP_001309906.1; NM_001322977.1.
DR RefSeq; NP_073591.2; NM_022754.6.
DR AlphaFoldDB; Q9H9B4; -.
DR BioGRID; 125107; 405.
DR IntAct; Q9H9B4; 182.
DR MINT; Q9H9B4; -.
DR STRING; 9606.ENSP00000316905; -.
DR TCDB; 2.A.54.1.1; the sideroflexin (sfxn) family (formerly the mitochondrial tricarboxylate carrier (mtc) family.
DR iPTMnet; Q9H9B4; -.
DR MetOSite; Q9H9B4; -.
DR PhosphoSitePlus; Q9H9B4; -.
DR SwissPalm; Q9H9B4; -.
DR BioMuta; SFXN1; -.
DR EPD; Q9H9B4; -.
DR jPOST; Q9H9B4; -.
DR MassIVE; Q9H9B4; -.
DR MaxQB; Q9H9B4; -.
DR PaxDb; Q9H9B4; -.
DR PeptideAtlas; Q9H9B4; -.
DR PRIDE; Q9H9B4; -.
DR ProteomicsDB; 81311; -.
DR TopDownProteomics; Q9H9B4; -.
DR Antibodypedia; 17087; 172 antibodies from 26 providers.
DR DNASU; 94081; -.
DR Ensembl; ENST00000321442.10; ENSP00000316905.5; ENSG00000164466.13.
DR GeneID; 94081; -.
DR KEGG; hsa:94081; -.
DR MANE-Select; ENST00000321442.10; ENSP00000316905.5; NM_022754.7; NP_073591.2.
DR UCSC; uc003mda.3; human.
DR CTD; 94081; -.
DR DisGeNET; 94081; -.
DR GeneCards; SFXN1; -.
DR HGNC; HGNC:16085; SFXN1.
DR HPA; ENSG00000164466; Tissue enhanced (liver).
DR MIM; 615569; gene.
DR neXtProt; NX_Q9H9B4; -.
DR OpenTargets; ENSG00000164466; -.
DR PharmGKB; PA38090; -.
DR VEuPathDB; HostDB:ENSG00000164466; -.
DR eggNOG; KOG3767; Eukaryota.
DR GeneTree; ENSGT01030000234641; -.
DR HOGENOM; CLU_039425_1_0_1; -.
DR InParanoid; Q9H9B4; -.
DR OMA; GRVRHCA; -.
DR OrthoDB; 881974at2759; -.
DR PhylomeDB; Q9H9B4; -.
DR TreeFam; TF313205; -.
DR PathwayCommons; Q9H9B4; -.
DR SignaLink; Q9H9B4; -.
DR SIGNOR; Q9H9B4; -.
DR BioGRID-ORCS; 94081; 28 hits in 1086 CRISPR screens.
DR ChiTaRS; SFXN1; human.
DR GeneWiki; SFXN1; -.
DR GenomeRNAi; 94081; -.
DR Pharos; Q9H9B4; Tbio.
DR PRO; PR:Q9H9B4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H9B4; protein.
DR Bgee; ENSG00000164466; Expressed in adrenal tissue and 202 other tissues.
DR ExpressionAtlas; Q9H9B4; baseline and differential.
DR Genevisible; Q9H9B4; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022889; F:serine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0006826; P:iron ion transport; IEA:Ensembl.
DR GO; GO:0015808; P:L-alanine transport; IDA:UniProtKB.
DR GO; GO:0015825; P:L-serine transport; IDA:UniProtKB.
DR GO; GO:1990542; P:mitochondrial transmembrane transport; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IDA:UniProtKB.
DR GO; GO:0140300; P:serine import into mitochondrion; IDA:UniProtKB.
DR InterPro; IPR004686; Mtc.
DR PANTHER; PTHR11153; PTHR11153; 1.
DR Pfam; PF03820; SFXNs; 1.
DR TIGRFAMs; TIGR00798; mtc; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid transport; Direct protein sequencing; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; One-carbon metabolism;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..322
FT /note="Sideroflexin-1"
FT /id="PRO_0000177032"
FT TOPO_DOM 2..102
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:30442778"
FT TRANSMEM 103..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..146
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..174
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..228
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..266
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..322
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:30442778"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT VARIANT 26
FT /note="N -> S (in dbSNP:rs17065105)"
FT /id="VAR_051966"
FT VARIANT 266
FT /note="P -> S (in dbSNP:rs34907038)"
FT /id="VAR_051967"
FT CONFLICT 73
FT /note="Y -> K (in Ref. 2; BAB14318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35619 MW; 47E03172F27990DB CRC64;
MSGELPPNIN IKEPRWDQST FIGRANHFFT VTDPRNILLT NEQLESARKI VHDYRQGIVP
PGLTENELWR AKYIYDSAFH PDTGEKMILI GRMSAQVPMN MTITGCMMTF YRTTPAVLFW
QWINQSFNAV VNYTNRSGDA PLTVNELGTA YVSATTGAVA TALGLNALTK HVSPLIGRFV
PFAAVAAANC INIPLMRQRE LKVGIPVTDE NGNRLGESAN AAKQAITQVV VSRILMAAPG
MAIPPFIMNT LEKKAFLKRF PWMSAPIQVG LVGFCLVFAT PLCCALFPQK SSMSVTSLEA
ELQAKIQESH PELRRVYFNK GL
