COX15_HUMAN
ID COX15_HUMAN Reviewed; 410 AA.
AC Q7KZN9; A8K6I9; O60556; O75878; Q5TD00; Q5TD01; Q7Z3Q3; Q9NTN0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cytochrome c oxidase assembly protein COX15 homolog;
GN Name=COX15;
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] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=9878253; DOI=10.1006/geno.1998.5580;
RA Petruzzella V., Tiranti V., Fernandez P., Ianna P., Carrozzo R.,
RA Zeviani M.;
RT "Identification and characterization of human cDNAs specific to BCS1,
RT PET112, SCO1, COX15, and COX11, five genes involved in the formation and
RT function of the mitochondrial respiratory chain.";
RL Genomics 54:494-504(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT MC4DN6
RP TRP-217.
RX PubMed=12474143; DOI=10.1086/345489;
RA Antonicka H., Mattman A., Carlson C.G., Glerum D.M., Hoffbuhr K.C.,
RA Leary S.C., Kennaway N.G., Shoubridge E.A.;
RT "Mutations in COX15 produce a defect in the mitochondrial heme biosynthetic
RT pathway, causing early-onset fatal hypertrophic cardiomyopathy.";
RL Am. J. Hum. Genet. 72:101-114(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrial tumor;
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Skin;
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 [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 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 [11]
RP VARIANT MC4DN6 TRP-217.
RX PubMed=15235026; DOI=10.1136/jmg.2003.017426;
RA Oquendo C.E., Antonicka H., Shoubridge E.A., Reardon W., Brown G.K.;
RT "Functional and genetic studies demonstrate that mutation in the COX15 gene
RT can cause Leigh syndrome.";
RL J. Med. Genet. 41:540-544(2004).
RN [12]
RP VARIANT MC4DN6 PRO-344.
RX PubMed=15863660; DOI=10.1136/jmg.2004.029926;
RA Bugiani M., Tiranti V., Farina L., Uziel G., Zeviani M.;
RT "Novel mutations in COX15 in a long surviving Leigh syndrome patient with
RT cytochrome c oxidase deficiency.";
RL J. Med. Genet. 42:E28-E28(2005).
RN [13]
RP VARIANT MC4DN6 TRP-217.
RX PubMed=21412973; DOI=10.1002/ajmg.a.33881;
RA Alfadhel M., Lillquist Y.P., Waters P.J., Sinclair G., Struys E.,
RA McFadden D., Hendson G., Hyams L., Shoffner J., Vallance H.D.;
RT "Infantile cardioencephalopathy due to a COX15 gene defect: report and
RT review.";
RL Am. J. Med. Genet. A 155:840-844(2011).
CC -!- FUNCTION: May be involved in the biosynthesis of heme A.
CC {ECO:0000269|PubMed:12474143}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; heme A biosynthesis;
CC heme A from heme O: step 1/1.
CC -!- INTERACTION:
CC Q7KZN9; P30041: PRDX6; NbExp=3; IntAct=EBI-3248549, EBI-2255129;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:9878253}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9878253}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=COX15.1;
CC IsoId=Q7KZN9-1; Sequence=Displayed;
CC Name=2; Synonyms=COX15.2;
CC IsoId=Q7KZN9-2; Sequence=VSP_011281;
CC -!- TISSUE SPECIFICITY: Predominantly found in tissues characterized by
CC high rates of oxidative phosphorylation (OxPhos), including muscle,
CC heart, and brain. {ECO:0000269|PubMed:9878253}.
CC -!- DISEASE: Mitochondrial complex IV deficiency, nuclear type 6 (MC4DN6)
CC [MIM:615119]: An autosomal recessive multisystem disorder with variable
CC manifestations. Some patients present in the neonatal period with
CC encephalomyopathic features, whereas others present later in the first
CC year of life with developmental regression. Clinical features include
CC microcephaly, encephalopathy, hypertrophic cardiomyopathy, persistent
CC lactic acidosis, respiratory distress, hypotonia and seizures. Serum
CC lactate is increased, and laboratory studies show decreased
CC mitochondrial complex IV protein and activity levels.
CC {ECO:0000269|PubMed:12474143, ECO:0000269|PubMed:15235026,
CC ECO:0000269|PubMed:15863660, ECO:0000269|PubMed:21412973}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the COX15/CtaA family. {ECO:0000305}.
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DR EMBL; AF026850; AAD08639.1; -; mRNA.
DR EMBL; AF044323; AAD08646.1; -; mRNA.
DR EMBL; BT007129; AAP35793.1; -; mRNA.
DR EMBL; AK291654; BAF84343.1; -; mRNA.
DR EMBL; BX537557; CAD97781.1; -; mRNA.
DR EMBL; AL133353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49857.1; -; Genomic_DNA.
DR EMBL; BC002382; AAH02382.3; -; mRNA.
DR EMBL; BC013403; AAH13403.1; -; mRNA.
DR EMBL; BC078161; AAH78161.1; -; mRNA.
DR CCDS; CCDS7481.1; -. [Q7KZN9-2]
DR CCDS; CCDS7482.1; -. [Q7KZN9-1]
DR RefSeq; NP_001307903.1; NM_001320974.1.
DR RefSeq; NP_001307904.1; NM_001320975.1.
DR RefSeq; NP_001307905.1; NM_001320976.1.
DR RefSeq; NP_004367.2; NM_004376.6. [Q7KZN9-2]
DR RefSeq; NP_510870.1; NM_078470.5. [Q7KZN9-1]
DR AlphaFoldDB; Q7KZN9; -.
DR SMR; Q7KZN9; -.
DR BioGRID; 107747; 376.
DR CORUM; Q7KZN9; -.
DR IntAct; Q7KZN9; 203.
DR MINT; Q7KZN9; -.
DR STRING; 9606.ENSP00000016171; -.
DR TCDB; 8.A.174.1.1; the cytochrome c oxidase cox15 assembly protein (cox15) family.
DR GlyGen; Q7KZN9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7KZN9; -.
DR PhosphoSitePlus; Q7KZN9; -.
DR SwissPalm; Q7KZN9; -.
DR BioMuta; COX15; -.
DR DMDM; 51315906; -.
DR EPD; Q7KZN9; -.
DR jPOST; Q7KZN9; -.
DR MassIVE; Q7KZN9; -.
DR MaxQB; Q7KZN9; -.
DR PaxDb; Q7KZN9; -.
DR PeptideAtlas; Q7KZN9; -.
DR PRIDE; Q7KZN9; -.
DR ProteomicsDB; 68724; -. [Q7KZN9-1]
DR ProteomicsDB; 68725; -. [Q7KZN9-2]
DR TopDownProteomics; Q7KZN9-1; -. [Q7KZN9-1]
DR Antibodypedia; 17500; 179 antibodies from 28 providers.
DR DNASU; 1355; -.
DR Ensembl; ENST00000016171.6; ENSP00000016171.6; ENSG00000014919.13. [Q7KZN9-1]
DR Ensembl; ENST00000370483.9; ENSP00000359514.5; ENSG00000014919.13. [Q7KZN9-2]
DR GeneID; 1355; -.
DR KEGG; hsa:1355; -.
DR MANE-Select; ENST00000016171.6; ENSP00000016171.6; NM_078470.6; NP_510870.1.
DR UCSC; uc001kqb.5; human. [Q7KZN9-1]
DR CTD; 1355; -.
DR DisGeNET; 1355; -.
DR GeneCards; COX15; -.
DR HGNC; HGNC:2263; COX15.
DR HPA; ENSG00000014919; Low tissue specificity.
DR MalaCards; COX15; -.
DR MIM; 603646; gene.
DR MIM; 615119; phenotype.
DR neXtProt; NX_Q7KZN9; -.
DR OpenTargets; ENSG00000014919; -.
DR Orphanet; 1561; Fatal infantile cytochrome C oxidase deficiency.
DR Orphanet; 255241; Leigh syndrome with leukodystrophy.
DR PharmGKB; PA26779; -.
DR VEuPathDB; HostDB:ENSG00000014919; -.
DR eggNOG; KOG2725; Eukaryota.
DR GeneTree; ENSGT00390000002223; -.
DR HOGENOM; CLU_017627_0_1_1; -.
DR InParanoid; Q7KZN9; -.
DR OMA; YWWEWGH; -.
DR OrthoDB; 1181324at2759; -.
DR PhylomeDB; Q7KZN9; -.
DR TreeFam; TF105073; -.
DR PathwayCommons; Q7KZN9; -.
DR Reactome; R-HSA-189451; Heme biosynthesis.
DR SignaLink; Q7KZN9; -.
DR UniPathway; UPA00269; UER00713.
DR BioGRID-ORCS; 1355; 321 hits in 1073 CRISPR screens.
DR ChiTaRS; COX15; human.
DR GeneWiki; COX15; -.
DR GenomeRNAi; 1355; -.
DR Pharos; Q7KZN9; Tbio.
DR PRO; PR:Q7KZN9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q7KZN9; protein.
DR Bgee; ENSG00000014919; Expressed in caput epididymis and 211 other tissues.
DR Genevisible; Q7KZN9; HS.
DR GO; GO:0070069; C:cytochrome complex; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005746; C:mitochondrial respirasome; TAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; TAS:UniProtKB.
DR GO; GO:0020037; F:heme binding; TAS:ARUK-UCL.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:BHF-UCL.
DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IBA:GO_Central.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; TAS:Reactome.
DR GO; GO:0045333; P:cellular respiration; TAS:HGNC-UCL.
DR GO; GO:0006784; P:heme A biosynthetic process; IGI:HGNC-UCL.
DR GO; GO:0006783; P:heme biosynthetic process; TAS:Reactome.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; TAS:HGNC-UCL.
DR GO; GO:1902600; P:proton transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; IMP:HGNC-UCL.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; TAS:UniProtKB.
DR HAMAP; MF_01665; HemeA_synth_type2; 1.
DR InterPro; IPR003780; COX15/CtaA_fam.
DR InterPro; IPR023754; HemeA_Synthase_type2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR PANTHER; PTHR23289; PTHR23289; 1.
DR Pfam; PF02628; COX15-CtaA; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Leigh syndrome; Membrane;
KW Mitochondrion; Primary mitochondrial disease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..410
FT /note="Cytochrome c oxidase assembly protein COX15 homolog"
FT /id="PRO_0000183931"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 368..410
FT /note="VGLGISTLLMYVPTPLAATHQSGSLALLTGALWLMNELRRVPK -> GPVLF
FT NFTFKISDLDEGIRNI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9878253"
FT /id="VSP_011281"
FT VARIANT 217
FT /note="R -> W (in MC4DN6; dbSNP:rs28939711)"
FT /evidence="ECO:0000269|PubMed:12474143,
FT ECO:0000269|PubMed:15235026, ECO:0000269|PubMed:21412973"
FT /id="VAR_019596"
FT VARIANT 344
FT /note="S -> P (in MC4DN6; dbSNP:rs397514662)"
FT /evidence="ECO:0000269|PubMed:15863660"
FT /id="VAR_033117"
FT CONFLICT 28
FT /note="R -> K (in Ref. 1; AAD08639/AAD08646)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="T -> A (in Ref. 3; CAD97781)"
FT /evidence="ECO:0000305"
FT CONFLICT Q7KZN9-2:374
FT /note="F -> L (in Ref. 1; AAD08646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 46030 MW; 98E9FD9D1D28EFC0 CRC64;
MQRLLFPPLR ALKGRQYLPL LAPRAAPRAQ CDCIRRPLRP GQYSTISEVA LQSGRGTVSL
PSKAAERVVG RWLLVCSGTV AGAVILGGVT RLTESGLSMV DWHLIKEMKP PTSQEEWEAE
FQRYQQFPEF KILNHDMTLT EFKFIWYMEY SHRMWGRLVG LVYILPAAYF WRKGWLSRGM
KGRVLALCGL VCFQGLLGWY MVKSGLEEKS DSHDIPRVSQ YRLAAHLGSA LVLYCASLWT
SLSLLLPPHK LPETHQLLQL RRFAHGTAGL VFLTALSGAF VAGLDAGLVY NSFPKMGESW
IPEDLFTFSP ILRNVFENPT MVQFDHRILG ITSVTAITVL YFLSRRIPLP RRTKMAAVTL
LALAYTQVGL GISTLLMYVP TPLAATHQSG SLALLTGALW LMNELRRVPK
