GLYM_MOUSE
ID GLYM_MOUSE Reviewed; 504 AA.
AC Q9CZN7; Q3TFD0; Q99K87;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Serine hydroxymethyltransferase, mitochondrial {ECO:0000305};
DE Short=SHMT {ECO:0000305};
DE EC=2.1.2.1 {ECO:0000250|UniProtKB:P34897};
DE AltName: Full=Glycine hydroxymethyltransferase {ECO:0000305};
DE AltName: Full=Serine methylase {ECO:0000305};
DE Flags: Precursor;
GN Name=Shmt2 {ECO:0000312|MGI:MGI:1277989};
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 {ECO:0000312|EMBL:BAB28184.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Spinal ganglion, and Thymus;
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-474, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP FUNCTION.
RX PubMed=29452640; DOI=10.1016/j.molcel.2018.01.024;
RA Minton D.R., Nam M., McLaughlin D.J., Shin J., Bayraktar E.C.,
RA Alvarez S.W., Sviderskiy V.O., Papagiannakopoulos T., Sabatini D.M.,
RA Birsoy K., Possemato R.;
RT "Serine catabolism by SHMT2 is required for proper mitochondrial
RT translation initiation and maintenance of formylmethionyl-tRNAs.";
RL Mol. Cell 69:610-621(2018).
RN [7]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=29323231; DOI=10.1038/s41598-017-18828-3;
RA Tani H., Ohnishi S., Shitara H., Mito T., Yamaguchi M., Yonekawa H.,
RA Hashizume O., Ishikawa K., Nakada K., Hayashi J.I.;
RT "Mice deficient in the Shmt2 gene have mitochondrial respiration defects
RT and are embryonic lethal.";
RL Sci. Rep. 8:425-425(2018).
CC -!- FUNCTION: Catalyzes the cleavage of serine to glycine accompanied with
CC the production of 5,10-methylenetetrahydrofolate, an essential
CC intermediate for purine biosynthesis (By similarity). Serine provides
CC the major source of folate one-carbon in cells by catalyzing the
CC transfer of one carbon from serine to tetrahydrofolate (By similarity).
CC Contributes to the de novo mitochondrial thymidylate biosynthesis
CC pathway via its role in glycine and tetrahydrofolate metabolism:
CC thymidylate biosynthesis is required to prevent uracil accumulation in
CC mtDNA (By similarity). Also required for mitochondrial translation by
CC producing 5,10-methylenetetrahydrofolate; 5,10-
CC methylenetetrahydrofolate providing methyl donors to produce the
CC taurinomethyluridine base at the wobble position of some mitochondrial
CC tRNAs (PubMed:29452640). Associates with mitochondrial DNA (By
CC similarity). In addition to its role in mitochondria, also plays a role
CC in the deubiquitination of target proteins as component of the BRISC
CC complex: required for IFNAR1 deubiquitination by the BRISC complex (By
CC similarity). {ECO:0000250|UniProtKB:P34897,
CC ECO:0000269|PubMed:29452640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC Evidence={ECO:0000250|UniProtKB:P34897};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15483;
CC Evidence={ECO:0000250|UniProtKB:P34897};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P34897};
CC -!- ACTIVITY REGULATION: Hydroxymethyltransferase is inhibited by
CC succinylation at Lys-280. {ECO:0000250|UniProtKB:P34897}.
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000250|UniProtKB:P34897}.
CC -!- SUBUNIT: Homotetramer; in the presence of bound pyridoxal 5'-phosphate.
CC Homodimer; in the absence of bound pyridoxal 5'-phosphate. Pyridoxal
CC 5'-phosphate binding mediates an important conformation change that is
CC required for tetramerization. Interacts with ABRAXAS2; the interaction
CC is direct. Identified in a complex with ABRAXAS2 and the other subunits
CC of the BRISC complex, at least composed of the ABRAXAS2, BRCC3/BRCC36,
CC BABAM2 and BABAM1/NBA1. Identified in a complex with ABRAXAS2 and
CC IFNAR1. Interacts with KIRREL3. {ECO:0000250|UniProtKB:P34897}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P34897}.
CC Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000250|UniProtKB:P34897}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P34897}. Cytoplasm
CC {ECO:0000250|UniProtKB:P34897}. Nucleus {ECO:0000250|UniProtKB:P34897}.
CC Note=Mainly localizes in the mitochondrion. Also found in the cytoplasm
CC and nucleus as part of the BRISC complex.
CC {ECO:0000250|UniProtKB:P34897}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CZN7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZN7-2; Sequence=VSP_059519;
CC -!- DEVELOPMENTAL STAGE: Present in the placenta, brain and liver during
CC embryonic development (at protein level).
CC {ECO:0000269|PubMed:29323231}.
CC -!- PTM: Succinylation at Lys-280 inhibits the hydroxymethyltransferase
CC activity. Desuccinylation by SIRT5 restores the activity, leading to
CC promote cell proliferation. {ECO:0000250|UniProtKB:P34897}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality after 13.5 days post coitum
CC (dpc) due to mitochondrial respiration defects and retardation of cell
CC growth. Mitochondrial respiration defects are due to reduction of
CC mitochondrial translation. {ECO:0000269|PubMed:29323231}.
CC -!- MISCELLANEOUS: In eukaryotes there are two forms of the enzymes: a
CC cytosolic one and a mitochondrial one. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; AK012355; BAB28184.1; -; mRNA.
DR EMBL; AK037339; BAC29790.1; -; mRNA.
DR EMBL; AK051207; BAC34556.1; -; mRNA.
DR EMBL; AK162421; BAE36907.1; -; mRNA.
DR EMBL; AK169192; BAE40968.1; -; mRNA.
DR EMBL; AC167719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004825; AAH04825.1; -; mRNA.
DR EMBL; BC051396; AAH51396.1; -; mRNA.
DR CCDS; CCDS24244.1; -. [Q9CZN7-1]
DR CCDS; CCDS88105.1; -. [Q9CZN7-2]
DR RefSeq; NP_001239245.1; NM_001252316.1. [Q9CZN7-2]
DR RefSeq; NP_082506.1; NM_028230.4. [Q9CZN7-1]
DR AlphaFoldDB; Q9CZN7; -.
DR SMR; Q9CZN7; -.
DR IntAct; Q9CZN7; 2.
DR MINT; Q9CZN7; -.
DR STRING; 10090.ENSMUSP00000026470; -.
DR iPTMnet; Q9CZN7; -.
DR PhosphoSitePlus; Q9CZN7; -.
DR SwissPalm; Q9CZN7; -.
DR jPOST; Q9CZN7; -.
DR MaxQB; Q9CZN7; -.
DR PaxDb; Q9CZN7; -.
DR PRIDE; Q9CZN7; -.
DR ProteomicsDB; 338698; -. [Q9CZN7-1]
DR ProteomicsDB; 342776; -.
DR Antibodypedia; 16145; 259 antibodies from 30 providers.
DR DNASU; 108037; -.
DR Ensembl; ENSMUST00000026470; ENSMUSP00000026470; ENSMUSG00000025403. [Q9CZN7-1]
DR Ensembl; ENSMUST00000219239; ENSMUSP00000151616; ENSMUSG00000025403. [Q9CZN7-2]
DR GeneID; 108037; -.
DR KEGG; mmu:108037; -.
DR UCSC; uc007hju.2; mouse. [Q9CZN7-1]
DR UCSC; uc007hjv.2; mouse.
DR CTD; 6472; -.
DR MGI; MGI:1277989; Shmt2.
DR VEuPathDB; HostDB:ENSMUSG00000025403; -.
DR eggNOG; KOG2467; Eukaryota.
DR GeneTree; ENSGT00390000002762; -.
DR HOGENOM; CLU_022477_0_1_1; -.
DR InParanoid; Q9CZN7; -.
DR OMA; RCQHSEV; -.
DR OrthoDB; 372408at2759; -.
DR PhylomeDB; Q9CZN7; -.
DR TreeFam; TF314667; -.
DR Reactome; R-MMU-196757; Metabolism of folate and pterines.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR UniPathway; UPA00193; -.
DR BioGRID-ORCS; 108037; 10 hits in 74 CRISPR screens.
DR ChiTaRS; Shmt2; mouse.
DR PRO; PR:Q9CZN7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CZN7; protein.
DR Bgee; ENSMUSG00000025403; Expressed in left lobe of liver and 254 other tissues.
DR Genevisible; Q3TFD0; MM.
DR GO; GO:0070552; C:BRISC complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
DR GO; GO:0070905; F:serine binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006545; P:glycine biosynthetic process; ISO:MGI.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; ISO:MGI.
DR GO; GO:0006544; P:glycine metabolic process; ISS:UniProtKB.
DR GO; GO:0006564; P:L-serine biosynthetic process; ISO:MGI.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
DR GO; GO:0006730; P:one-carbon metabolic process; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISO:MGI.
DR GO; GO:0051262; P:protein tetramerization; ISO:MGI.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:1903715; P:regulation of aerobic respiration; IMP:UniProtKB.
DR GO; GO:0070129; P:regulation of mitochondrial translation; IMP:UniProtKB.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IMP:UniProtKB.
DR GO; GO:0034340; P:response to type I interferon; ISO:MGI.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IMP:MGI.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; ISO:MGI.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00051; SHMT; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion nucleoid; Nucleus;
KW One-carbon metabolism; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P14519"
FT CHAIN 30..504
FT /note="Serine hydroxymethyltransferase, mitochondrial"
FT /id="PRO_0000443804"
FT MOD_RES 103
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34897"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34897"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34897"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P34897"
FT MOD_RES 280
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P34897"
FT MOD_RES 464
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34897"
FT MOD_RES 469
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P34897"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34897"
FT MOD_RES 474
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 12..14
FT /note="Missing (in isoform 2)"
FT /id="VSP_059519"
FT CONFLICT 40
FT /note="A -> T (in Ref. 3; AAH04825/AAH51396)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="R -> K (in Ref. 3; AAH04825/AAH51396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 55759 MW; 38A380996F75EC3C CRC64;
MVSFSLLRTT RPLQRCGQLV CMAARAQHSK VAQTQAGEAA GGWTGQESLS DSDPEMWELL
QREKDRQCRG LELIASENFC SRAALEALGS CLNNKYSEGY PGKRYYGGAE VVDEIELLCQ
RRALEAFDLD PAQWGVNVQP YSGSPANLAA YTALLQPHDR IMGLDLPDGG HLTHGYMSDV
KRISATSIFF ESMPYKLNPQ TGLIDYDQLA LTARLFRPRL IIAGTSAYAR LIDYARMREV
CDEVRAHLLA DMAHISGLVA AKVIPSPFKY ADVVTTTTHK TLRGARSGLI FYRKGVRTVD
PKTGKEIPYT FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY SLQVLRNAQA
MADALLKRGY SLVSGGTDTH LVLVDLRPKG LDGARAERVL ELVSITANKN TCPGDRSAIT
PGGLRLGAPA LTSRQFREDD FRRVVDFIDE GVNIGLEVKR KTAKLQDFKS FLLKDPETSQ
RLANLRQQVE QFARGFPMPG FDER
