CPT1C_HUMAN
ID CPT1C_HUMAN Reviewed; 803 AA.
AC Q8TCG5; A8K0Z8; Q5K6N5; Q8N6Q9; Q8NDS6; Q8TE84;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Carnitine O-palmitoyltransferase 1, brain isoform;
DE Short=CPT1-B;
DE EC=2.3.1.21;
DE AltName: Full=CPT IC;
DE AltName: Full=Carnitine O-palmitoyltransferase I, brain isoform;
DE Short=CPTI-B;
DE AltName: Full=Carnitine palmitoyltransferase 1C;
GN Name=CPT1C; Synonyms=CATL1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Eye;
RX PubMed=12376098; DOI=10.1006/geno.2002.6845;
RA Price N., van der Leij F.R., Jackson V., Corstorphine C., Thomson R.,
RA Sorensen A., Zammit V.;
RT "A novel brain-expressed protein related to carnitine palmitoyltransferase
RT I.";
RL Genomics 80:433-442(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Scorilas A., Katsaros N.;
RT "Molecular characterization, chromosomal localization and expression
RT analysis of a gene, CATL1, encoding for a new member of the human carnitine
RT acyltransferase family.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Kidney epithelium, and Subthalamic nucleus;
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 375-803 (ISOFORM 3).
RC TISSUE=Brain;
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 [7]
RP FUNCTION, INTERACTION WITH ATL1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INVOLVEMENT IN SPG73, VARIANT SPG73 CYS-37, AND CHARACTERIZATION OF VARIANT
RP SPG73 CYS-37.
RX PubMed=25751282; DOI=10.1001/jamaneurol.2014.4769;
RA Rinaldi C., Schmidt T., Situ A.J., Johnson J.O., Lee P.R., Chen K.L.,
RA Bott L.C., Fado R., Harmison G.H., Parodi S., Grunseich C., Renvoise B.,
RA Biesecker L.G., De Michele G., Santorelli F.M., Filla A., Stevanin G.,
RA Duerr A., Brice A., Casals N., Traynor B.J., Blackstone C., Ulmer T.S.,
RA Fischbeck K.H.;
RT "Mutation in CPT1C Associated with pure autosomal dominant spastic
RT paraplegia.";
RL JAMA Neurol. 72:561-570(2015).
CC -!- FUNCTION: May play a role in lipid metabolic process.
CC {ECO:0000269|PubMed:25751282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:12661, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:17490, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=2.3.1.21;
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Peripherally associated with AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents, including CPT1C. Alone or in
CC combination, these auxiliary subunits control the gating and
CC pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing (By similarity). Interacts with ATL1
CC (PubMed:25751282). {ECO:0000250|UniProtKB:Q8BGD5,
CC ECO:0000269|PubMed:25751282}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Synapse
CC {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, dendrite
CC {ECO:0000269|PubMed:25751282}. Cell projection, axon
CC {ECO:0000269|PubMed:25751282}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8BGD5}. Note=Localized in the soma and
CC dendritic and axonal projections. {ECO:0000269|PubMed:25751282}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TCG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TCG5-2; Sequence=VSP_010677;
CC Name=3;
CC IsoId=Q8TCG5-3; Sequence=VSP_012457;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain and testis.
CC Expressed in motor neurons. {ECO:0000269|PubMed:12376098,
CC ECO:0000269|PubMed:25751282}.
CC -!- DISEASE: Spastic paraplegia 73, autosomal dominant (SPG73)
CC [MIM:616282]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body.
CC {ECO:0000269|PubMed:25751282}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85068.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD38561.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF357970; AAL99615.1; -; mRNA.
DR EMBL; AF331918; AAQ14875.1; -; Genomic_DNA.
DR EMBL; AK074389; BAB85068.1; ALT_INIT; mRNA.
DR EMBL; AK289713; BAF82402.1; -; mRNA.
DR EMBL; AK290092; BAF82781.1; -; mRNA.
DR EMBL; CH471177; EAW52524.1; -; Genomic_DNA.
DR EMBL; BC029104; AAH29104.1; -; mRNA.
DR EMBL; AL831876; CAD38561.2; ALT_INIT; mRNA.
DR CCDS; CCDS12779.1; -. [Q8TCG5-1]
DR CCDS; CCDS46147.1; -. [Q8TCG5-2]
DR RefSeq; NP_001129524.1; NM_001136052.2. [Q8TCG5-2]
DR RefSeq; NP_001186681.1; NM_001199752.2. [Q8TCG5-1]
DR RefSeq; NP_001186682.1; NM_001199753.1. [Q8TCG5-1]
DR RefSeq; NP_689572.1; NM_152359.2. [Q8TCG5-1]
DR RefSeq; XP_005258562.1; XM_005258505.2.
DR RefSeq; XP_005258563.1; XM_005258506.4.
DR RefSeq; XP_011524740.1; XM_011526438.2.
DR RefSeq; XP_011524741.1; XM_011526439.2.
DR PDB; 2M76; NMR; -; A=1-50.
DR PDBsum; 2M76; -.
DR AlphaFoldDB; Q8TCG5; -.
DR BMRB; Q8TCG5; -.
DR SMR; Q8TCG5; -.
DR BioGRID; 125958; 4.
DR STRING; 9606.ENSP00000376303; -.
DR iPTMnet; Q8TCG5; -.
DR PhosphoSitePlus; Q8TCG5; -.
DR BioMuta; CPT1C; -.
DR DMDM; 57013809; -.
DR EPD; Q8TCG5; -.
DR jPOST; Q8TCG5; -.
DR MassIVE; Q8TCG5; -.
DR PaxDb; Q8TCG5; -.
DR PeptideAtlas; Q8TCG5; -.
DR PRIDE; Q8TCG5; -.
DR ProteomicsDB; 74135; -. [Q8TCG5-1]
DR ProteomicsDB; 74136; -. [Q8TCG5-2]
DR ProteomicsDB; 74137; -. [Q8TCG5-3]
DR Antibodypedia; 3052; 273 antibodies from 33 providers.
DR DNASU; 126129; -.
DR Ensembl; ENST00000323446.9; ENSP00000319343.4; ENSG00000169169.15. [Q8TCG5-1]
DR Ensembl; ENST00000392518.8; ENSP00000376303.4; ENSG00000169169.15. [Q8TCG5-1]
DR Ensembl; ENST00000405931.6; ENSP00000384465.2; ENSG00000169169.15. [Q8TCG5-2]
DR Ensembl; ENST00000598293.6; ENSP00000473028.1; ENSG00000169169.15. [Q8TCG5-1]
DR GeneID; 126129; -.
DR KEGG; hsa:126129; -.
DR MANE-Select; ENST00000598293.6; ENSP00000473028.1; NM_001199753.2; NP_001186682.1.
DR UCSC; uc002ppj.4; human. [Q8TCG5-1]
DR CTD; 126129; -.
DR DisGeNET; 126129; -.
DR GeneCards; CPT1C; -.
DR HGNC; HGNC:18540; CPT1C.
DR HPA; ENSG00000169169; Tissue enhanced (brain, pituitary gland).
DR MalaCards; CPT1C; -.
DR MIM; 608846; gene.
DR MIM; 616282; phenotype.
DR neXtProt; NX_Q8TCG5; -.
DR OpenTargets; ENSG00000169169; -.
DR Orphanet; 444099; Autosomal dominant spastic paraplegia type 73.
DR PharmGKB; PA134922321; -.
DR VEuPathDB; HostDB:ENSG00000169169; -.
DR eggNOG; KOG3716; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR HOGENOM; CLU_013513_2_1_1; -.
DR InParanoid; Q8TCG5; -.
DR OMA; VYSEQWQ; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; Q8TCG5; -.
DR TreeFam; TF313836; -.
DR BioCyc; MetaCyc:HS09892-MON; -.
DR BRENDA; 2.3.1.21; 2681.
DR PathwayCommons; Q8TCG5; -.
DR SignaLink; Q8TCG5; -.
DR SIGNOR; Q8TCG5; -.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 126129; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; CPT1C; human.
DR GenomeRNAi; 126129; -.
DR Pharos; Q8TCG5; Tbio.
DR PRO; PR:Q8TCG5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8TCG5; protein.
DR Bgee; ENSG00000169169; Expressed in right hemisphere of cerebellum and 122 other tissues.
DR ExpressionAtlas; Q8TCG5; baseline and differential.
DR Genevisible; Q8TCG5; HS.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0009437; P:carnitine metabolic process; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR039551; Cho/carn_acyl_trans.
DR InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR InterPro; IPR032476; CPT_N.
DR PANTHER; PTHR22589; PTHR22589; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR Pfam; PF16484; CPT_N; 1.
DR PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Cell projection;
KW Disease variant; Endoplasmic reticulum; Fatty acid metabolism;
KW Hereditary spastic paraplegia; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Neurodegeneration; Reference proteome;
KW Synapse; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..803
FT /note="Carnitine O-palmitoyltransferase 1, brain isoform"
FT /id="PRO_0000210166"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..103
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..803
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 772..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 552..564
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 586
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT VAR_SEQ 258..268
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010677"
FT VAR_SEQ 623..711
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012457"
FT VARIANT 37
FT /note="R -> C (in SPG73; alters protein conformation;
FT dominant negative mutation; dbSNP:rs786204767)"
FT /evidence="ECO:0000269|PubMed:25751282"
FT /id="VAR_073433"
FT CONFLICT 58
FT /note="S -> G (in Ref. 3; BAF82402)"
FT /evidence="ECO:0000305"
FT CONFLICT 375..378
FT /note="HEEH -> RTRG (in Ref. 6; CAD38561)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="D -> G (in Ref. 3; BAB85068)"
FT /evidence="ECO:0000305"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2M76"
FT HELIX 25..48
FT /evidence="ECO:0007829|PDB:2M76"
SQ SEQUENCE 803 AA; 90989 MW; 96C2AE6ED0DEC705 CRC64;
MAEAHQAVGF RPSLTSDGAE VELSAPVLQE IYLSGLRSWK RHLSRFWNDF LTGVFPASPL
SWLFLFSAIQ LAWFLQLDPS LGLMEKIKEL LPDWGGQHHG LRGVLAAALF ASCLWGALIF
TLHVALRLLL SYHGWLLEPH GAMSSPTKTW LALVRIFSGR HPMLFSYQRS LPRQPVPSVQ
DTVRKYLESV RPILSDEDFD WTAVLAQEFL RLQASLLQWY LRLKSWWASN YVSDWWEEFV
YLRSRNPLMV NSNYYMMDFL YVTPTPLQAA RAGNAVHALL LYRHRLNRQE IPPTLLMGMR
PLCSAQYEKI FNTTRIPGVQ KDYIRHLHDS QHVAVFHRGR FFRMGTHSRN SLLSPRALEQ
QFQRILDDPS PACPHEEHLA ALTAAPRGTW AQVRTSLKTQ AAEALEAVEG AAFFVSLDAE
PAGLTREDPA ASLDAYAHAL LAGRGHDRWF DKSFTLIVFS NGKLGLSVEH SWADCPISGH
MWEFTLATEC FQLGYSTDGH CKGHPDPTLP QPQRLQWDLP DQIHSSISLA LRGAKILSEN
VDCHVVPFSL FGKSFIRRCH LSSDSFIQIA LQLAHFRDRG QFCLTYESAM TRLFLEGRTE
TVRSCTREAC NFVRAMEDKE KTDPQCLALF RVAVDKHQAL LKAAMSGQGV DRHLFALYIV
SRFLHLQSPF LTQVHSEQWQ LSTSQIPVQQ MHLFDVHNYP DYVSSGGGFG PADDHGYGVS
YIFMGDGMIT FHISSKKSST KTDSHRLGQH IEDALLDVAS LFQAGQHFKR RFRGSGKENS
RHRCGFLSRQ TGASKASMTS TDF
