OGDHL_HUMAN
ID OGDHL_HUMAN Reviewed; 1010 AA.
AC Q9ULD0; A8K2G1; B4DKG2; B4E193; Q8TAN9; Q9NVA0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=2-oxoglutarate dehydrogenase-like, mitochondrial {ECO:0000250|UniProtKB:D3ZQD3};
DE EC=1.2.4.2 {ECO:0000250|UniProtKB:D3ZQD3};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E1-like {ECO:0000303|PubMed:23152800};
DE Short=OGDC-E1-like {ECO:0000303|PubMed:23152800};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase-like;
DE Flags: Precursor;
GN Name=OGDHL {ECO:0000312|HGNC:HGNC:25590}; Synonyms=KIAA1290;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP SEQUENCE REVISION.
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP MET-637.
RC TISSUE=Kidney, and Thalamus;
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=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LEU-511
RP AND ASN-573.
RC TISSUE=Brain;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23152800; DOI=10.1371/journal.pone.0048770;
RA Sen T., Sen N., Noordhuis M.G., Ravi R., Wu T.C., Ha P.K., Sidransky D.,
RA Hoque M.O.;
RT "OGDHL is a modifier of AKT-dependent signaling and NF-kappaB function.";
RL PLoS ONE 7:e48770-e48770(2012).
RN [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND REPRESSION BY MIR-214.
RX PubMed=31175094; DOI=10.1158/1078-0432.ccr-18-4113;
RA Liu Y., Meng F., Wang J., Liu M., Yang G., Song R., Zheng T., Liang Y.,
RA Zhang S., Yin D., Wang J., Yang H., Pan S., Sun B., Han J., Sun J., Lan Y.,
RA Wang Y., Liu X., Zhu M., Cui Y., Zhang B., Wu D., Liang S., Liu Y.,
RA Song X., Lu Z., Yang J., Li M., Liu L.;
RT "A Novel Oxoglutarate Dehydrogenase-Like Mediated miR-214/TWIST1 Negative
RT Feedback Loop Inhibits Pancreatic Cancer Growth and Metastasis.";
RL Clin. Cancer Res. 25:5407-5421(2019).
CC -!- FUNCTION: 2-oxoglutarate dehydrogenase (E1-like) component of the 2-
CC oxoglutarate dehydrogenase multienzyme complex (OGDHC) which mediates
CC the decarboxylation of alpha-ketoglutarate in the tricarboxylic acid
CC cycle. The OGDHC complex catalyzes the overall conversion of 2-
CC oxoglutarate to succinyl-CoA and CO(2) while reducing NAD(+) to NADH
CC (By similarity). The OGDHC complex is mainly active in the
CC mitochondrion (By similarity). Involved in the inhibition of cell
CC proliferation and in apoptosis (PubMed:23152800, PubMed:31175094).
CC {ECO:0000250|UniProtKB:D3ZQD3, ECO:0000269|PubMed:23152800,
CC ECO:0000269|PubMed:31175094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83120; EC=1.2.4.2;
CC Evidence={ECO:0000250|UniProtKB:D3ZQD3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12189;
CC Evidence={ECO:0000250|UniProtKB:D3ZQD3};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:Q02218};
CC -!- SUBUNIT: The OGDHC complex comprises multiple copies of three catalytic
CC enzyme components, the 2-oxoglutarate dehydrogenase (OGDH/E1), the
CC dihydrolipoamide dehydrogenase (DLST/E2) and the dihydrolipoamide
CC dehydrogenase (DLD/E3). OGDHL/E1-like isoenzyme may replace OGDH in the
CC OGDHC complex in the brain. The presence of either ODGH/E1 or ODGHL/E1-
CC like isoenzyme in the complex may depend on its tissular distribution.
CC {ECO:0000250|UniProtKB:D3ZQD3}.
CC -!- INTERACTION:
CC Q9ULD0; P11802: CDK4; NbExp=3; IntAct=EBI-3940481, EBI-295644;
CC Q9ULD0; P40763: STAT3; NbExp=2; IntAct=EBI-3940481, EBI-518675;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:23152800}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ULD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULD0-2; Sequence=VSP_041350;
CC Name=3;
CC IsoId=Q9ULD0-3; Sequence=VSP_041351;
CC -!- TISSUE SPECIFICITY: Expressed in the brain and the liver.
CC {ECO:0000269|PubMed:23152800, ECO:0000269|PubMed:31175094}.
CC -!- INDUCTION: Post-transcriptionally repressed by microRNA miR-214 in
CC cancer cells. {ECO:0000269|PubMed:31175094}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86604.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB033116; BAA86604.2; ALT_INIT; mRNA.
DR EMBL; AK001713; BAA91855.1; -; mRNA.
DR EMBL; AK290226; BAF82915.1; -; mRNA.
DR EMBL; AK296551; BAG59174.1; -; mRNA.
DR EMBL; AK303729; BAG64705.1; -; mRNA.
DR EMBL; AC069546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026320; AAH26320.1; -; mRNA.
DR CCDS; CCDS44390.1; -. [Q9ULD0-2]
DR CCDS; CCDS44391.1; -. [Q9ULD0-3]
DR CCDS; CCDS7234.1; -. [Q9ULD0-1]
DR RefSeq; NP_001137468.1; NM_001143996.1. [Q9ULD0-2]
DR RefSeq; NP_001137469.1; NM_001143997.1. [Q9ULD0-3]
DR RefSeq; NP_001334748.1; NM_001347819.1. [Q9ULD0-1]
DR RefSeq; NP_001334749.1; NM_001347820.1. [Q9ULD0-2]
DR RefSeq; NP_001334750.1; NM_001347821.1. [Q9ULD0-3]
DR RefSeq; NP_001334751.1; NM_001347822.1. [Q9ULD0-3]
DR RefSeq; NP_060715.2; NM_018245.2. [Q9ULD0-1]
DR RefSeq; XP_011538248.1; XM_011539946.1. [Q9ULD0-1]
DR AlphaFoldDB; Q9ULD0; -.
DR SMR; Q9ULD0; -.
DR BioGRID; 120871; 57.
DR DIP; DIP-61552N; -.
DR IntAct; Q9ULD0; 9.
DR MINT; Q9ULD0; -.
DR STRING; 9606.ENSP00000363216; -.
DR iPTMnet; Q9ULD0; -.
DR PhosphoSitePlus; Q9ULD0; -.
DR BioMuta; OGDHL; -.
DR DMDM; 160419019; -.
DR EPD; Q9ULD0; -.
DR jPOST; Q9ULD0; -.
DR MassIVE; Q9ULD0; -.
DR MaxQB; Q9ULD0; -.
DR PaxDb; Q9ULD0; -.
DR PeptideAtlas; Q9ULD0; -.
DR PRIDE; Q9ULD0; -.
DR ProteomicsDB; 84986; -. [Q9ULD0-1]
DR ProteomicsDB; 84987; -. [Q9ULD0-2]
DR ProteomicsDB; 84988; -. [Q9ULD0-3]
DR Antibodypedia; 44978; 66 antibodies from 21 providers.
DR DNASU; 55753; -.
DR Ensembl; ENST00000374103.9; ENSP00000363216.4; ENSG00000197444.10. [Q9ULD0-1]
DR Ensembl; ENST00000419399.4; ENSP00000401356.1; ENSG00000197444.10. [Q9ULD0-2]
DR Ensembl; ENST00000432695.2; ENSP00000390240.1; ENSG00000197444.10. [Q9ULD0-3]
DR GeneID; 55753; -.
DR KEGG; hsa:55753; -.
DR MANE-Select; ENST00000374103.9; ENSP00000363216.4; NM_018245.3; NP_060715.2.
DR UCSC; uc001jie.4; human. [Q9ULD0-1]
DR CTD; 55753; -.
DR DisGeNET; 55753; -.
DR GeneCards; OGDHL; -.
DR HGNC; HGNC:25590; OGDHL.
DR HPA; ENSG00000197444; Tissue enhanced (choroid plexus, kidney, liver).
DR MIM; 617513; gene.
DR neXtProt; NX_Q9ULD0; -.
DR OpenTargets; ENSG00000197444; -.
DR PharmGKB; PA134878907; -.
DR VEuPathDB; HostDB:ENSG00000197444; -.
DR eggNOG; KOG0450; Eukaryota.
DR GeneTree; ENSGT00950000183125; -.
DR HOGENOM; CLU_004709_1_1_1; -.
DR InParanoid; Q9ULD0; -.
DR OMA; IMIDQYI; -.
DR OrthoDB; 134699at2759; -.
DR PhylomeDB; Q9ULD0; -.
DR TreeFam; TF300695; -.
DR BRENDA; 1.2.1.105; 2681.
DR PathwayCommons; Q9ULD0; -.
DR SignaLink; Q9ULD0; -.
DR SIGNOR; Q9ULD0; -.
DR BioGRID-ORCS; 55753; 8 hits in 1071 CRISPR screens.
DR ChiTaRS; OGDHL; human.
DR GenomeRNAi; 55753; -.
DR Pharos; Q9ULD0; Tbio.
DR PRO; PR:Q9ULD0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9ULD0; protein.
DR Bgee; ENSG00000197444; Expressed in adult mammalian kidney and 121 other tissues.
DR Genevisible; Q9ULD0; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR Gene3D; 3.40.50.11610; -; 1.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR031717; KGD_C.
DR InterPro; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152; PTHR23152; 1.
DR Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF16870; OxoGdeHyase_C; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Glycolysis; Metal-binding; Mitochondrion;
KW Oxidoreductase; Reference proteome; Thiamine pyrophosphate;
KW Transit peptide.
FT TRANSIT 1..73
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 74..1010
FT /note="2-oxoglutarate dehydrogenase-like, mitochondrial"
FT /id="PRO_0000310983"
FT REGION 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02218"
FT VAR_SEQ 1..209
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041351"
FT VAR_SEQ 69..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041350"
FT VARIANT 511
FT /note="P -> L (in dbSNP:rs17856755)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037125"
FT VARIANT 573
FT /note="D -> N (in dbSNP:rs17852386)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037126"
FT VARIANT 623
FT /note="S -> C (in dbSNP:rs34877195)"
FT /id="VAR_037127"
FT VARIANT 637
FT /note="T -> M (in dbSNP:rs11101224)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_037128"
FT VARIANT 725
FT /note="N -> S (in dbSNP:rs2293239)"
FT /id="VAR_037129"
FT CONFLICT 97
FT /note="S -> G (in Ref. 3; BAA91855)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="Q -> R (in Ref. 3; BAA91855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1010 AA; 114481 MW; 95A836DE079E804C CRC64;
MSQLRLLPSR LGVQAARLLA AHDVPVFGWR SRSSGPPATF PSSKGGGGSS YMEEMYFAWL
ENPQSVHKSW DSFFREASEE AFSGSAQPRP PSVVHESRSA VSSRTKTSKL VEDHLAVQSL
IRAYQIRGHH VAQLDPLGIL DADLDSFVPS DLITTIDKLA FYDLQEADLD KEFQLPTTTF
IGGSENTLSL REIIRRLENT YCQHIGLEFM FINDVEQCQW IRQKFETPGV MQFSSEEKRT
LLARLVRSMR FEDFLARKWS SEKRFGLEGC EVMIPALKTI IDKSSEMGIE NVILGMPHRG
RLNVLANVIR KDLEQIFCQF DPKLEAADEG SGDVKYHLGM YHERINRVTN RNITLSLVAN
PSHLEAVDPV VQGKTKAEQF YRGDAQGKKV MSILVHGDAA FAGQGVVYET FHLSDLPSYT
TNGTVHVVVN NQIGFTTDPR MARSSPYPTD VARVVNAPIF HVNADDPEAV IYVCSVAAEW
RNTFNKDVVV DLVCYRRRGH NEMDEPMFTQ PLMYKQIHRQ VPVLKKYADK LIAEGTVTLQ
EFEEEIAKYD RICEEAYGRS KDKKILHIKH WLDSPWPGFF NVDGEPKSMT CPATGIPEDM
LTHIGSVASS VPLEDFKIHT GLSRILRGRA DMTKNRTVDW ALAEYMAFGS LLKEGIHVRL
SGQDVERGTF SHRHHVLHDQ EVDRRTCVPM NHLWPDQAPY TVCNSSLSEY GVLGFELGYA
MASPNALVLW EAQFGDFHNT AQCIIDQFIS TGQAKWVRHN GIVLLLPHGM EGMGPEHSSA
RPERFLQMSN DDSDAYPAFT KDFEVSQLYD CNWIVVNCST PANYFHVLRR QILLPFRKPL
IIFTPKSLLR HPEAKSSFDQ MVSGTSFQRV IPEDGAAARA PEQVQRLIFC TGKVYYDLVK
ERSSQDLEEK VAITRLEQIS PFPFDLIKQE AEKYPGAELA WCQEEHKNMG YYDYISPRFM
TILRRARPIW YVGRDPAAAP ATGNRNTHLV SLKKFLDTAF NLQAFEGKTF
