ID   MTX1_HUMAN              Reviewed;         466 AA.
AC   Q13505; A0A0A0MRK6; B1AVR9; B1AVS0; B2R9P4; Q9BUU3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 3.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Metaxin-1;
DE   AltName: Full=Mitochondrial outer membrane import complex protein 1;
GN   Name=MTX1; Synonyms=MTX, MTXN;
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 [GENOMIC DNA / MRNA] (ISOFORM 3).
RX   PubMed=8660965; DOI=10.1006/geno.1996.0181;
RA   Long G.L., Winfield S.L., Adolph K.W., Ginns E.I., Bornstein P.;
RT   "Structure and organization of the human metaxin gene (MTX) and
RT   pseudogene.";
RL   Genomics 33:177-184(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RX   PubMed=9331372; DOI=10.1101/gr.7.10.1020;
RA   Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.;
RT   "Identification of three additional genes contiguous to the
RT   glucocerebrosidase locus on chromosome 1q21: implications for Gaucher
RT   disease.";
RL   Genome Res. 7:1020-1026(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
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] (ISOFORM 2).
RC   TISSUE=Placenta;
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   INTERACTION WITH MTX2.
RX   PubMed=10381257;
RX   DOI=10.1002/(sici)1097-4644(19990701)74:1<11::aid-jcb2>3.3.co;2-m;
RA   Armstrong L.C., Saenz A.J., Bornstein P.;
RT   "Metaxin 1 interacts with metaxin 2, a novel related protein associated
RT   with the mammalian mitochondrial outer membrane.";
RL   J. Cell. Biochem. 74:11-22(1999).
RN   [8]
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   [9]
RP   INTERACTION WITH THE MINOS/MITOS COMPLEX.
RX   PubMed=22114354; DOI=10.1091/mbc.e11-09-0774;
RA   Alkhaja A.K., Jans D.C., Nikolov M., Vukotic M., Lytovchenko O.,
RA   Ludewig F., Schliebs W., Riedel D., Urlaub H., Jakobs S., Deckers M.;
RT   "MINOS1 is a conserved component of mitofilin complexes and required for
RT   mitochondrial function and cristae organization.";
RL   Mol. Biol. Cell 23:247-257(2012).
RN   [10]
RP   INTERACTION WITH THE MICOS COMPLEX.
RX   PubMed=25997101; DOI=10.7554/elife.06265;
RA   Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA   Gygi S.P., Van Vactor D., Harper J.W.;
RT   "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT   and cristae morphology.";
RL   Elife 4:0-0(2015).
RN   [11]
RP   UBIQUITINATION AT LYS-187; LYS-190; LYS-227 AND LYS-317.
RX   PubMed=25621951; DOI=10.1038/ncb3097;
RA   Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
RA   Kirkpatrick D.S., Bingol B., Corn J.E.;
RT   "USP30 and parkin homeostatically regulate atypical ubiquitin chains on
RT   mitochondria.";
RL   Nat. Cell Biol. 17:160-169(2015).
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   INTERACTION WITH ARMC1.
RX   PubMed=31644573; DOI=10.1371/journal.pone.0218303;
RA   Wagner F., Kunz T.C., Chowdhury S.R., Thiede B., Fraunholz M., Eger D.,
RA   Kozjak-Pavlovic V.;
RT   "Armadillo repeat-containing protein 1 is a dual localization protein
RT   associated with mitochondrial intermembrane space bridging complex.";
RL   PLoS ONE 14:e0218303-e0218303(2019).
CC   -!- FUNCTION: Involved in transport of proteins into the mitochondrion.
CC       Essential for embryonic development (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MTX2/metaxin-2. Associates with the
CC       mitochondrial contact site and cristae organizing system (MICOS)
CC       complex, composed of at least MICOS10/MIC10, CHCHD3/MIC19,
CC       CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13.
CC       This complex was also known under the names MINOS or MitOS complex. The
CC       MICOS complex associates with mitochondrial outer membrane proteins
CC       SAMM50, MTX1 and MTX2 (together described as components of the
CC       mitochondrial outer membrane sorting assembly machinery (SAM) complex)
CC       and DNAJC11, mitochondrial inner membrane protein TMEM11 and with
CC       HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a
CC       large protein complex spanning both membranes termed the mitochondrial
CC       intermembrane space bridging (MIB) complex. Interacts with ARMC1
CC       (PubMed:31644573). {ECO:0000269|PubMed:10381257,
CC       ECO:0000269|PubMed:22114354, ECO:0000269|PubMed:25997101,
CC       ECO:0000269|PubMed:31644573}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Mitochondrion outer membrane
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q13505-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13505-2; Sequence=VSP_035742;
CC       Name=3;
CC         IsoId=Q13505-3; Sequence=VSP_035741;
CC   -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC       and enhancement of mitophagy. Deubiquitinated by USP30.
CC       {ECO:0000269|PubMed:25621951}.
CC   -!- SIMILARITY: Belongs to the metaxin family. {ECO:0000305}.
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DR   EMBL; U46920; AAC50490.1; -; Genomic_DNA.
DR   EMBL; AF023268; AAC51819.1; -; Genomic_DNA.
DR   EMBL; AK313863; BAG36591.1; -; mRNA.
DR   EMBL; AC234582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW53106.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW53105.1; -; Genomic_DNA.
DR   EMBL; BC001906; AAH01906.2; -; mRNA.
DR   CCDS; CCDS1100.1; -. [Q13505-1]
DR   CCDS; CCDS1101.1; -. [Q13505-2]
DR   RefSeq; NP_002446.3; NM_002455.4. [Q13505-1]
DR   RefSeq; NP_942584.2; NM_198883.3. [Q13505-2]
DR   AlphaFoldDB; Q13505; -.
DR   SMR; Q13505; -.
DR   BioGRID; 110667; 157.
DR   ComplexPortal; CPX-6133; SAM mitochondrial sorting and assembly machinery complex.
DR   CORUM; Q13505; -.
DR   IntAct; Q13505; 38.
DR   MINT; Q13505; -.
DR   STRING; 9606.ENSP00000357360; -.
DR   iPTMnet; Q13505; -.
DR   PhosphoSitePlus; Q13505; -.
DR   SwissPalm; Q13505; -.
DR   BioMuta; MTX1; -.
DR   DMDM; 215274027; -.
DR   EPD; Q13505; -.
DR   jPOST; Q13505; -.
DR   MassIVE; Q13505; -.
DR   MaxQB; Q13505; -.
DR   PaxDb; 9606-ENSP00000357360; -.
DR   PeptideAtlas; Q13505; -.
DR   ProteomicsDB; 59499; -. [Q13505-1]
DR   ProteomicsDB; 59500; -. [Q13505-2]
DR   ProteomicsDB; 59501; -. [Q13505-3]
DR   Pumba; Q13505; -.
DR   TopDownProteomics; Q13505-1; -. [Q13505-1]
DR   TopDownProteomics; Q13505-3; -. [Q13505-3]
DR   Antibodypedia; 2611; 153 antibodies from 23 providers.
DR   DNASU; 4580; -.
DR   Ensembl; ENST00000316721.8; ENSP00000317106.4; ENSG00000173171.15. [Q13505-2]
DR   Ensembl; ENST00000368376.8; ENSP00000357360.3; ENSG00000173171.15. [Q13505-1]
DR   Ensembl; ENST00000609421.1; ENSP00000476632.1; ENSG00000173171.15. [Q13505-3]
DR   GeneID; 4580; -.
DR   KEGG; hsa:4580; -.
DR   MANE-Select; ENST00000368376.8; ENSP00000357360.3; NM_002455.5; NP_002446.3.
DR   UCSC; uc001fjb.4; human.
DR   UCSC; uc001fjc.4; human. [Q13505-1]
DR   AGR; HGNC:7504; -.
DR   CTD; 4580; -.
DR   DisGeNET; 4580; -.
DR   GeneCards; MTX1; -.
DR   HGNC; HGNC:7504; MTX1.
DR   HPA; ENSG00000173171; Low tissue specificity.
DR   MIM; 600605; gene.
DR   neXtProt; NX_Q13505; -.
DR   OpenTargets; ENSG00000173171; -.
DR   PharmGKB; PA31306; -.
DR   VEuPathDB; HostDB:ENSG00000173171; -.
DR   eggNOG; KOG3028; Eukaryota.
DR   GeneTree; ENSGT00950000182919; -.
DR   HOGENOM; CLU_044137_5_0_1; -.
DR   InParanoid; Q13505; -.
DR   OMA; TIDYDCA; -.
DR   OrthoDB; 2897805at2759; -.
DR   PhylomeDB; Q13505; -.
DR   TreeFam; TF313422; -.
DR   PathwayCommons; Q13505; -.
DR   Reactome; R-HSA-1268020; Mitochondrial protein import.
DR   Reactome; R-HSA-8949613; Cristae formation.
DR   Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR   SignaLink; Q13505; -.
DR   SIGNOR; Q13505; -.
DR   BioGRID-ORCS; 4580; 25 hits in 1161 CRISPR screens.
DR   ChiTaRS; MTX1; human.
DR   GeneWiki; MTX1; -.
DR   GenomeRNAi; 4580; -.
DR   Pharos; Q13505; Tbio.
DR   PRO; PR:Q13505; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q13505; Protein.
DR   Bgee; ENSG00000173171; Expressed in right testis and 100 other cell types or tissues.
DR   ExpressionAtlas; Q13505; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0140275; C:MIB complex; HDA:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; NAS:ComplexPortal.
DR   GO; GO:0001401; C:SAM complex; IPI:ComplexPortal.
DR   GO; GO:0007007; P:inner mitochondrial membrane organization; IC:UniProtKB.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; NAS:ComplexPortal.
DR   CDD; cd03212; GST_C_Metaxin1_3; 1.
DR   CDD; cd03078; GST_N_Metaxin1_like; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR033468; Metaxin_GST.
DR   InterPro; IPR019564; Sam37/metaxin_N.
DR   PANTHER; PTHR12289; METAXIN RELATED; 1.
DR   PANTHER; PTHR12289:SF34; METAXIN-1; 1.
DR   Pfam; PF17171; GST_C_6; 1.
DR   Pfam; PF10568; Tom37; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01180; SUF1; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   Genevisible; Q13505; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Isopeptide bond; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Protein transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..466
FT                   /note="Metaxin-1"
FT                   /id="PRO_0000220991"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        187
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   CROSSLNK        190
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   CROSSLNK        227
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   CROSSLNK        317
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:25621951"
FT   VAR_SEQ         1..149
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:8660965"
FT                   /id="VSP_035741"
FT   VAR_SEQ         227..257
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035742"
FT   VARIANT         63
FT                   /note="S -> T (in dbSNP:rs760077)"
FT                   /id="VAR_047376"
SQ   SEQUENCE   466 AA;  51463 MW;  2F98ABCA860F50E2 CRC64;
     MLLGGPPRSP RSGTSPKGPW SSTGHVQFGK SPQTWPRRTR PRSPEPAAPS GVRGSTWTRR
     RDSPRRAGPT ALSRYVGHLW MGRRPPSPEA RGPVPRSSAA SRARRSLASP GISPGPLTAT
     IGGAVAGGGP RQGRAEAHKE VFPGQRVGKM AAPMELFCWS GGWGLPSVDL DSLAVLTYAR
     FTGAPLKVHK ISNPWQSPSG TLPALRTSHG EVISVPHKII THLRKEKYNA DYDLSARQGA
     DTLAFMSLLE EKLLPVLVHT FWIDTKNYVE VTRKWYAEAM PFPLNFFLPG RMQRQYMERL
     QLLTGEHRPE DEEELEKELY REARECLTLL SQRLGSQKFF FGDAPASLDA FVFSYLALLL
     QAKLPSGKLQ VHLRGLHNLC AYCTHILSLY FPWDGAEVPP QRQTPAGPET EEEPYRRRNQ
     ILSVLAGLAA MVGYALLSGI VSIQRATPAR APGTRTLGMA EEDEEE
//