ABCD1_RAT
ID ABCD1_RAT Reviewed; 737 AA.
AC D3ZHR2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=ATP-binding cassette sub-family D member 1 {ECO:0000305};
DE EC=3.1.2.- {ECO:0000250|UniProtKB:P33897};
DE EC=7.6.2.- {ECO:0000269|PubMed:12176987};
DE AltName: Full=Adrenoleukodystrophy protein {ECO:0000250|UniProtKB:P33897};
DE Short=ALDP {ECO:0000250|UniProtKB:P33897};
GN Name=Abcd1 {ECO:0000312|RGD:1562128};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ABCD3, PHOSPHORYLATION, AND
RP ATP-BINDING.
RX PubMed=12176987; DOI=10.1074/jbc.m205079200;
RA Tanaka A.R., Tanabe K., Morita M., Kurisu M., Kasiwayama Y., Matsuo M.,
RA Kioka N., Amachi T., Imanaka T., Ueda K.;
RT "ATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding
RT cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1).";
RL J. Biol. Chem. 277:40142-40147(2002).
RN [4]
RP FUNCTION, INTERACTION WITH ABCD2, AND SUBCELLULAR LOCATION.
RX PubMed=25043761; DOI=10.1074/jbc.m114.575506;
RA Geillon F., Gondcaille C., Charbonnier S., Van Roermund C.W., Lopez T.E.,
RA Dias A.M., Pais de Barros J.P., Arnould C., Wanders R.J., Trompier D.,
RA Savary S.;
RT "Structure-function analysis of peroxisomal ATP-binding cassette
RT transporters using chimeric dimers.";
RL J. Biol. Chem. 289:24511-24520(2014).
RN [5]
RP SUBUNIT.
RX PubMed=28258215; DOI=10.1074/jbc.m116.772806;
RA Geillon F., Gondcaille C., Raas Q., Dias A.M.M., Pecqueur D., Truntzer C.,
RA Lucchi G., Ducoroy P., Falson P., Savary S., Trompier D.;
RT "Peroxisomal ATP-binding cassette transporters form mainly tetramers.";
RL J. Biol. Chem. 292:6965-6977(2017).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family involved in the transport of very long chain fatty acid (VLCFA)-
CC CoA from the cytosol to the peroxisome lumen (PubMed:12176987). Coupled
CC to the ATP-dependent transporter activity has also a fatty acyl-CoA
CC thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior
CC their ATP-dependent transport into peroxisomes, the ACOT activity is
CC essential during this transport process (By similarity). Thus, plays a
CC role in regulation of VLCFAs and energy metabolism namely, in the
CC degradation and biosynthesis of fatty acids by beta-oxidation,
CC mitochondrial function and microsomal fatty acid elongation
CC (PubMed:25043761). Involved in several processes; namely, controls the
CC active myelination phase by negatively regulating the microsomal fatty
CC acid elongation activity and may also play a role in axon and myelin
CC maintenance. Controls also the cellular response to oxidative stress by
CC regulating mitochondrial functions such as mitochondrial oxidative
CC phosphorylation and depolarization. And finally controls the
CC inflammatory response by positively regulating peroxisomal beta-
CC oxidation of VLCFAs (By similarity). {ECO:0000250|UniProtKB:P48410,
CC ECO:0000269|PubMed:12176987, ECO:0000269|PubMed:25043761}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very long-chain fatty acyl-CoA + H2O = a very long-chain
CC fatty acid + CoA + H(+); Xref=Rhea:RHEA:67072, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950,
CC ChEBI:CHEBI:138261; Evidence={ECO:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67073;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very long-chain fatty acid(in) + ATP + H2O = a very long-
CC chain fatty acid(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67080,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58950, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:12176987};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67081;
CC Evidence={ECO:0000305|PubMed:12176987};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate;
CC Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + tetracosanoate(in) = ADP + H(+) + phosphate +
CC tetracosanoate(out); Xref=Rhea:RHEA:67088, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:31014,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate;
CC Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + hexacosanoate(in) = ADP + H(+) +
CC hexacosanoate(out) + phosphate; Xref=Rhea:RHEA:67084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31013, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+);
CC Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + docosanoate(in) + H2O = ADP + docosanoate(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:67092, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:23858, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67093;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC -!- SUBUNIT: Can form homodimers and heterodimers with ABCD2 and ABCD3.
CC Dimerization is necessary to form an active transporter
CC (PubMed:12176987, PubMed:25043761, PubMed:28258215). The minimal
CC functional unit is a homodimer but the major oligomeric form in
CC peroxisomal membrane is a homotetramer. Forms heterotramers with ABCD2
CC (PubMed:28258215). Interacts with PEX19; facilitates ABCD1 insertion
CC into the peroxisome membrane (By similarity).
CC {ECO:0000250|UniProtKB:P33897, ECO:0000269|PubMed:12176987,
CC ECO:0000269|PubMed:25043761, ECO:0000269|PubMed:28258215}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P33897};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P33897}. Lysosome
CC membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P33897}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P33897}.
CC -!- DOMAIN: The NH2-terminal transmembrane domaine (TMD) is involved in the
CC recognition of substrates, and undergoes a conformational change upon
CC ATP binding to the COOH-terminal nucleotide binding domain (NBD).
CC {ECO:0000250|UniProtKB:P33897}.
CC -!- PTM: Tyrosine-phosphorylated. {ECO:0000269|PubMed:12176987}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family.
CC Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC096338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474099; EDL85026.1; -; Genomic_DNA.
DR RefSeq; NP_001102291.1; NM_001108821.1.
DR AlphaFoldDB; D3ZHR2; -.
DR SMR; D3ZHR2; -.
DR STRING; 10116.ENSRNOP00000025863; -.
DR GlyGen; D3ZHR2; 1 site.
DR PaxDb; D3ZHR2; -.
DR PeptideAtlas; D3ZHR2; -.
DR Ensembl; ENSRNOT00000084088; ENSRNOP00000070359; ENSRNOG00000056524.
DR GeneID; 363516; -.
DR KEGG; rno:363516; -.
DR CTD; 215; -.
DR RGD; 1562128; Abcd1.
DR eggNOG; KOG0064; Eukaryota.
DR GeneTree; ENSGT00950000182955; -.
DR HOGENOM; CLU_007587_1_1_1; -.
DR InParanoid; D3ZHR2; -.
DR OMA; IPRWNSK; -.
DR OrthoDB; 309052at2759; -.
DR PhylomeDB; D3ZHR2; -.
DR TreeFam; TF105205; -.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-RNO-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-RNO-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:D3ZHR2; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000056524; Expressed in liver and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISO:RGD.
DR GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0015607; F:ABC-type fatty-acyl-CoA transporter activity; ISS:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0043531; F:ADP binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; ISO:RGD.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; ISS:UniProtKB.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; ISS:UniProtKB.
DR GO; GO:0043217; P:myelin maintenance; ISO:RGD.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR GO; GO:1990535; P:neuron projection maintenance; ISO:RGD.
DR GO; GO:0007031; P:peroxisome organization; ISO:RGD.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:2001280; P:positive regulation of unsaturated fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; ISO:RGD.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; ISO:RGD.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; ISO:RGD.
DR GO; GO:0055092; P:sterol homeostasis; ISO:RGD.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IMP:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0036113; P:very long-chain fatty-acyl-CoA catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR031237; ALDP.
DR InterPro; IPR005283; FA_transporter.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11384:SF21; PTHR11384:SF21; 1.
DR Pfam; PF06472; ABC_membrane_2; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00954; 3a01203; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Glycoprotein; Hydrolase; Lysosome;
KW Membrane; Mitochondrion; Nucleotide-binding; Peroxisome;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..737
FT /note="ATP-binding cassette sub-family D member 1"
FT /id="PRO_0000445226"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 95..387
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 475..730
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 68..187
FT /note="Interaction with PEX19"
FT /evidence="ECO:0000250|UniProtKB:P33897"
FT REGION 68..85
FT /note="PEX19 binding site and required for peroxisomal
FT targeting"
FT /evidence="ECO:0000250|UniProtKB:P33897"
FT REGION 659..737
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P33897"
FT BINDING 508..515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 737 AA; 81938 MW; C399AAE141153D23 CRC64;
MPVLSTPSRP SRVTTLKRTA VVLALTAYGV HKIYPLVRQC LTPARGPQVP AGESTQEASG
ATTAKAGMNR VFLQRLLVLL RLLFPGVLCR ETGLLALHSA ALVSRTFLSV YVARLDGRLA
RCIVRKDPRA FSWQLLQWLL IALPATFINS AIRYLEGQLA LSFRSRLVAH AYGLYFSQQT
YYRVSNMDGR LRNPDQSLTE DMVAFAASVA HLYSNLTKPL LDVAVTSYTL LRAARSRGAG
TAWPSAIAGL VVFLTANVLR AFSPKFGELV AEEARRKGEL RYMHSRVVAN SEEIAFYGGH
EVELALLQHS YQDLASQINL ILLERLWYVM LEQFLMKYVW SASGLLMVAV PIITATGYAE
SDSEAMKKAA LEMKEEELVS ERTEAFTIAR NLLTAAADAT ERIMSSYKEV TELAGYTARV
YEMFQVFEDV QHCRFKRTGD LEEAQAGPGS MVHSGVHIEG PLKIQGQVVD VEQGIICENI
PIITPTGEVV VASLNIRVEE GMHLLITGPN GCGKSSLFRI LGGLWPTYSG VLYKPPPQRM
FYIPQRPYMS VGSLRDQVIY PDSAEDMRRK GCSEQQLEAI LGIVHLRHIL QREGGWEAVC
DWKDVLSGGE KQRIGMARMF YHRPKYALLD ECTSAVSIDV EGKIFQAAKD AGISLLSITH
RPSLWKYHTH LLQFDGEGGW KFEKLDSAAR LSLTEEKQRL EQQLAGIPKM QGRLQELRQI
LGEAAAPVQP LVPGIPT
