MIRO1_MOUSE
ID MIRO1_MOUSE Reviewed; 631 AA.
AC Q8BG51; Q3TJB7; Q3UGU4; Q5SYC3; Q5SYC6; Q8BLW3; Q8BMH1; Q922N0; Q9D2R1;
AC Q9JKB9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Mitochondrial Rho GTPase 1;
DE Short=MIRO-1;
DE EC=3.6.5.-;
DE AltName: Full=Ras homolog gene family member T1;
GN Name=Rhot1; Synonyms=Arht1;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Aorta, Cecum, Forelimb, Ovary, Skin, Stomach, Thymus, and Vein;
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], AND ALTERNATIVE SPLICING
RP (ISOFORM 4).
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), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 240-633 (ISOFORM 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 392-631.
RA Guo H., Cai Q., Schroeder R., Kuo P.C.;
RT "LNAME-inducible ANA-1 cells mRNA expression.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP INTERACTION WITH ARMCX1.
RX PubMed=28009275; DOI=10.1016/j.neuron.2016.10.060;
RA Cartoni R., Norsworthy M.W., Bei F., Wang C., Li S., Zhang Y., Gabel C.V.,
RA Schwarz T.L., He Z.;
RT "The mammalian-specific protein Armcx1 regulates mitochondrial transport
RT during axon regeneration.";
RL Neuron 92:1294-1307(2016).
CC -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking.
CC Probably involved in control of anterograde transport of mitochondria
CC and their subcellular distribution. Promotes mitochondrial fission
CC during high calcium conditions (By similarity).
CC {ECO:0000250|UniProtKB:Q8IXI2}.
CC -!- SUBUNIT: Interacts with the kinesin-binding proteins TRAK1/OIP106 and
CC TRAK2/GRIF1, forming a link between mitochondria and the trafficking
CC apparatus of the microtubules (By similarity). Interacts with RAP1GDS1
CC (By similarity). Interacts with ARMCX1 (PubMed:28009275). Found in a
CC complex with KIF5B, OGT, RHOT2 and TRAK1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IXI2, ECO:0000269|PubMed:28009275}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8IXI2}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q8IXI2}. Note=Colocalizes with MGARP and RHOT2
CC at the mitochondria. {ECO:0000250|UniProtKB:Q8IXI2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BG51-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BG51-2; Sequence=VSP_019159;
CC Name=3;
CC IsoId=Q8BG51-3; Sequence=VSP_019160;
CC Name=4;
CC IsoId=Q8BG51-4; Sequence=VSP_019161;
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IXI2}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF64187.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAI25296.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK019059; BAB31529.2; -; mRNA.
DR EMBL; AK028597; BAC26025.1; -; mRNA.
DR EMBL; AK031139; BAC27274.1; ALT_INIT; mRNA.
DR EMBL; AK041119; BAC30828.1; -; mRNA.
DR EMBL; AK054472; BAC35792.1; -; mRNA.
DR EMBL; AK078955; BAC37478.1; -; mRNA.
DR EMBL; AK138830; BAE23792.1; -; mRNA.
DR EMBL; AK141621; BAE24771.1; -; mRNA.
DR EMBL; AK147749; BAE28113.1; -; mRNA.
DR EMBL; AK147801; BAE28148.1; -; mRNA.
DR EMBL; AK167502; BAE39578.1; -; mRNA.
DR EMBL; AL591426; CAI25293.1; -; Genomic_DNA.
DR EMBL; AL591426; CAI25294.1; -; Genomic_DNA.
DR EMBL; AL591426; CAI25295.1; -; Genomic_DNA.
DR EMBL; AL591426; CAI25296.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC006918; AAH06918.1; -; mRNA.
DR EMBL; BC046785; AAH46785.1; -; mRNA.
DR EMBL; BC058350; AAH58350.1; -; mRNA.
DR EMBL; AF244542; AAF64187.1; ALT_INIT; mRNA.
DR CCDS; CCDS25130.1; -. [Q8BG51-1]
DR CCDS; CCDS48861.1; -. [Q8BG51-2]
DR CCDS; CCDS48862.1; -. [Q8BG51-3]
DR CCDS; CCDS88206.1; -. [Q8BG51-4]
DR RefSeq; NP_001156826.1; NM_001163354.1. [Q8BG51-2]
DR RefSeq; NP_001156827.1; NM_001163355.1. [Q8BG51-3]
DR RefSeq; NP_067511.4; NM_021536.7. [Q8BG51-1]
DR RefSeq; XP_011247470.1; XM_011249168.2.
DR AlphaFoldDB; Q8BG51; -.
DR SMR; Q8BG51; -.
DR BioGRID; 208504; 5.
DR IntAct; Q8BG51; 1.
DR STRING; 10090.ENSMUSP00000017831; -.
DR iPTMnet; Q8BG51; -.
DR PhosphoSitePlus; Q8BG51; -.
DR SwissPalm; Q8BG51; -.
DR EPD; Q8BG51; -.
DR jPOST; Q8BG51; -.
DR MaxQB; Q8BG51; -.
DR PeptideAtlas; Q8BG51; -.
DR PRIDE; Q8BG51; -.
DR ProteomicsDB; 295613; -. [Q8BG51-1]
DR ProteomicsDB; 295614; -. [Q8BG51-2]
DR ProteomicsDB; 295615; -. [Q8BG51-3]
DR ProteomicsDB; 295616; -. [Q8BG51-4]
DR Antibodypedia; 2419; 246 antibodies from 26 providers.
DR DNASU; 59040; -.
DR Ensembl; ENSMUST00000017831; ENSMUSP00000017831; ENSMUSG00000017686. [Q8BG51-2]
DR Ensembl; ENSMUST00000055056; ENSMUSP00000057669; ENSMUSG00000017686. [Q8BG51-3]
DR Ensembl; ENSMUST00000077451; ENSMUSP00000076664; ENSMUSG00000017686. [Q8BG51-4]
DR Ensembl; ENSMUST00000092857; ENSMUSP00000090533; ENSMUSG00000017686. [Q8BG51-1]
DR GeneID; 59040; -.
DR KEGG; mmu:59040; -.
DR UCSC; uc007klo.2; mouse. [Q8BG51-1]
DR UCSC; uc007klp.2; mouse. [Q8BG51-2]
DR UCSC; uc007klq.2; mouse. [Q8BG51-3]
DR CTD; 55288; -.
DR MGI; MGI:1926078; Rhot1.
DR VEuPathDB; HostDB:ENSMUSG00000017686; -.
DR eggNOG; KOG1707; Eukaryota.
DR GeneTree; ENSGT00940000155641; -.
DR HOGENOM; CLU_014255_3_1_1; -.
DR InParanoid; Q8BG51; -.
DR OMA; HVSVTWN; -.
DR OrthoDB; 538388at2759; -.
DR PhylomeDB; Q8BG51; -.
DR TreeFam; TF300814; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-9013425; RHOT1 GTPase cycle.
DR BioGRID-ORCS; 59040; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Rhot1; mouse.
DR PRO; PR:Q8BG51; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BG51; protein.
DR Bgee; ENSMUSG00000017686; Expressed in retinal neural layer and 255 other tissues.
DR ExpressionAtlas; Q8BG51; baseline and differential.
DR Genevisible; Q8BG51; MM.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019725; P:cellular homeostasis; ISS:UniProtKB.
DR GO; GO:0034640; P:establishment of mitochondrion localization by microtubule attachment; IEA:Ensembl.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISO:MGI.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR013566; EF_hand_assoc_1.
DR InterPro; IPR013567; EF_hand_assoc_2.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR021181; Miro.
DR InterPro; IPR029506; Miro-1.
DR InterPro; IPR020860; MIRO_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR PANTHER; PTHR24072:SF124; PTHR24072:SF124; 1.
DR Pfam; PF08355; EF_assoc_1; 1.
DR Pfam; PF08356; EF_assoc_2; 1.
DR Pfam; PF00071; Ras; 2.
DR PIRSF; PIRSF037488; Mt_Rho_GTPase; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51423; MIRO; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; GTP-binding; Hydrolase; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..631
FT /note="Mitochondrial Rho GTPase 1"
FT /id="PRO_0000239314"
FT TOPO_DOM 1..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..628
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 629..631
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 15..181
FT /note="Miro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT DOMAIN 197..232
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 317..352
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 429..592
FT /note="Miro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 70..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 438..445
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 476..480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 540..543
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT VAR_SEQ 593
FT /note="P -> PEDHYRGSLSRDMGSTDRIENLRKIWVFLKTAL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019159"
FT VAR_SEQ 593
FT /note="P -> PHARLRCMCTCNRCTFCICQNFLNSDLLQSVKNKIFTAVLNR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_019160"
FT VAR_SEQ 593
FT /note="P -> PEDHYRGSLSRDMGSTDRIENLRKIWVFLKTAFHARLRCMCTCNRCT
FT FCICQNFLNSDLLQSVKNKIFTAVLNR (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_019161"
FT CONFLICT 263
FT /note="G -> D (in Ref. 1; BAC30828)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="K -> Q (in Ref. 4; AAF64187)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="C -> F (in Ref. 1; BAB31529)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="C -> S (in Ref. 1; BAC27274)"
FT /evidence="ECO:0000305"
FT CONFLICT Q8BG51-2:593
FT /note="P -> T (in Ref. 1; BAE28113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 72242 MW; C6B1BA3DDE904DF3 CRC64;
MRAGRVRPLR ASDMKKDVRI LLVGEPRVGK TSLIMSLVSE EFPEEVPPRA EEITIPADVT
PERVPTHIVD YSEAEQSDEQ LHQEISQANV ICIVYAVNNK HSIDKVTSRW IPLINERTDK
DSRLPLILVG NKSDLVEYSS METILPIMNQ YTEIETCVEC SAKNLKNISE LFYYAQKAVL
HPTGPLYCPE EKEMKPACIK ALTRIFKISD QDNDGTLNDA ELNFFQRICF NTPLAPQALE
DVKNVVRKHL SDGVADSGLT LRGFLFLHTL FIQRGRHETT WTVLRRFGYD DDLDLTPEYL
FPLLKIPPDC TTELNHHAYL FLQSTFDKHD LDRDCALSPD ELKDLFQVFP YIPWGPDVNN
TVCTNERGWI TYQGFLSQWT LTTYLDVQRC LEYLGYLGYS ILTEQESQAS AITVTRDKKI
DLQKKQTQRN VFRCNVIGVK GCGKTGVLQS LLGRNLMRQK KIRDDHKSYY AINTVYVYGQ
EKYLLLHDIS ESEFLTEAET ICDVVCLVYD VTNPKSFEYC ARIFKQHFMD SRIPCLIVAA
KSDLHEVKQE HSISPTDFCR KHKMPPPQAF TCNTADAPSK DIFVKLTTMA MYPHVTQADL
KSSTFWLRAS FGATVFAVVG FAMYRALLKQ R
