SCP2_RABIT
ID SCP2_RABIT Reviewed; 547 AA.
AC O62742;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Sterol carrier protein 2;
DE Short=SCP-2;
DE AltName: Full=Acetyl-CoA C-myristoyltransferase;
DE EC=2.3.1.155 {ECO:0000250|UniProtKB:P11915};
DE AltName: Full=Non-specific lipid-transfer protein;
DE Short=NSL-TP;
DE AltName: Full=Propanoyl-CoA C-acyltransferase;
DE EC=2.3.1.176 {ECO:0000250|UniProtKB:P11915};
DE AltName: Full=SCP-2/3-oxoacyl-CoA thiolase;
DE AltName: Full=SCP-2/thiolase;
DE EC=2.3.1.16 {ECO:0000250|UniProtKB:P11915};
DE AltName: Full=SCP-chi;
DE AltName: Full=SCPX;
DE AltName: Full=Sterol carrier protein X;
DE Short=SCP-X;
GN Name=SCP2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SCPX AND SCP2), FUNCTION, AND
RP STRUCTURE BY NMR OF 405-547.
RC TISSUE=Intestinal epithelium;
RX PubMed=9711242; DOI=10.1007/s000180050203;
RA Weber F.E., Dyer J.H., Lopez Garcia F., Werder M., Szyperski T.,
RA Wuethrich K., Hauser H.;
RT "In pre-sterol carrier protein 2 (SCP2) in solution the leader peptide 1-20
RT is flexibly disordered, and residues 21-143 adopt the same globular fold as
RT in mature SCP2.";
RL Cell. Mol. Life Sci. 54:751-759(1998).
RN [2]
RP CRYSTALLIZATION.
RX PubMed=10417421; DOI=10.1107/s0907444999007106;
RA Choinowski T., Dyer J.H., Maderegger B., Winterhalter K.H., Hauser H.,
RA Piontek K.;
RT "Crystallization and initial X-ray analysis of rabbit mature sterol carrier
RT protein 2.";
RL Acta Crystallogr. D 55:1478-1480(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 425-547, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=10684638; DOI=10.1021/bi992742e;
RA Choinowski T., Hauser H., Piontek K.;
RT "Structure of sterol carrier protein 2 at 1.8 A resolution reveals a
RT hydrophobic tunnel suitable for lipid binding.";
RL Biochemistry 39:1897-1902(2000).
CC -!- FUNCTION: [Isoform SCPx]: Plays a crucial role in the peroxisomal
CC oxidation of branched-chain fatty acids. Catalyzes the last step of the
CC peroxisomal beta-oxidation of branched chain fatty acids and the side
CC chain of the bile acid intermediates di- and trihydroxycoprostanic
CC acids (DHCA and THCA) (By similarity). Also active with medium and long
CC straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of
CC 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine
CC and 7-dehydrocholesterol between membrances, in vitro (By similarity).
CC Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain
CC naturally occurring tetramethyl-branched fatty acyl-CoAs (By
CC similarity). {ECO:0000250|UniProtKB:P11915,
CC ECO:0000250|UniProtKB:P22307, ECO:0000250|UniProtKB:P32020}.
CC -!- FUNCTION: [Isoform SCP2]: Mediates the transfer of all common
CC phospholipids, cholesterol and gangliosides from the endoplasmic
CC reticulum to the plasma membrane (PubMed:9711242). May play a role in
CC regulating steroidogenesis (By similarity). Stimulates the microsomal
CC conversion of 7-dehydrocholesterol to cholesterol (By similarity). Also
CC binds fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-
CC CoA. Involved in the regulation phospholipid synthesis in endoplasmic
CC reticulum enhancing the incorporation of exogenous fatty acid into
CC glycerides. Seems to stimulate the rate-limiting step in phosphatidic
CC acid formation mediated by GPAT3. Isoforms SCP2 and SCPx cooperate in
CC peroxisomal oxidation of certain naturally occurring tetramethyl-
CC branched fatty acyl-CoAs (By similarity).
CC {ECO:0000250|UniProtKB:P11915, ECO:0000250|UniProtKB:P22307,
CC ECO:0000250|UniProtKB:P32020, ECO:0000269|PubMed:9711242}.
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha-
CC trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA;
CC Xref=Rhea:RHEA:16865, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58507; EC=2.3.1.176;
CC Evidence={ECO:0000250|UniProtKB:P22307};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16867;
CC Evidence={ECO:0000250|UniProtKB:P22307};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:62619, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA +
CC tetradecanedioyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=propanoyl-CoA + tetradecanoyl-CoA = 3-oxo-2-
CC methylhexadecanoyl-CoA + CoA; Xref=Rhea:RHEA:46344,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:86042; Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:46346;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31111, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:62418;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31087, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57386, ChEBI:CHEBI:62548;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:61430, ChEBI:CHEBI:62615;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:31091, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:62543;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=acetyl-CoA + hexadecanoyl-CoA = 3-oxooctadecanoyl-CoA + CoA;
CC Xref=Rhea:RHEA:35279, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:71407;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=3-oxo-(9Z-octadecenoyl)-CoA + CoA = (7Z)-hexadecenoyl-CoA +
CC acetyl-CoA; Xref=Rhea:RHEA:47400, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:87695, ChEBI:CHEBI:87698;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47401;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out);
CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCP2]:
CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out);
CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759;
CC Evidence={ECO:0000305|PubMed:9711242};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-
CC oxopristanoyl-CoA + CoA; Xref=Rhea:RHEA:10408, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57291, ChEBI:CHEBI:57351, ChEBI:CHEBI:57392;
CC EC=2.3.1.176; Evidence={ECO:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10410;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- SUBUNIT: [Isoform SCPx]: Interacts with PEX5; the interaction is
CC essential for peroxisomal import. {ECO:0000250|UniProtKB:P22307}.
CC -!- SUBCELLULAR LOCATION: [Isoform SCP2]: Peroxisome
CC {ECO:0000250|UniProtKB:P32020}. Cytoplasm
CC {ECO:0000250|UniProtKB:P22307}. Mitochondrion
CC {ECO:0000250|UniProtKB:P22307}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P32020}. Mitochondrion
CC {ECO:0000250|UniProtKB:P32020}.
CC -!- SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome
CC {ECO:0000250|UniProtKB:P11915}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=SCPx;
CC IsoId=O62742-1; Sequence=Displayed;
CC Name=SCP2;
CC IsoId=O62742-2; Sequence=VSP_018896;
CC -!- PTM: [Isoform SCP2]: preSCP2, a protein with a molecular mass of about
CC 15 kDa, is processed into its mature form (SCP2) by proteolytic
CC cleavage of a 20 residue leader sequence after translocation into
CC peroxisomes. {ECO:0000269|PubMed:9711242}.
CC -!- MISCELLANEOUS: [Isoform SCP2]: Contains a putative mitochondrial
CC transit peptide at positions 1-20. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the thiolase-like
CC superfamily. Thiolase family. {ECO:0000305}.
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DR EMBL; AF051897; AAC15422.1; -; mRNA.
DR RefSeq; NP_001075504.1; NM_001082035.1. [O62742-1]
DR PDB; 1C44; X-ray; 1.80 A; A=425-547.
DR PDBsum; 1C44; -.
DR AlphaFoldDB; O62742; -.
DR SMR; O62742; -.
DR STRING; 9986.ENSOCUP00000019823; -.
DR PRIDE; O62742; -.
DR GeneID; 100008683; -.
DR KEGG; ocu:100008683; -.
DR CTD; 6342; -.
DR eggNOG; KOG1406; Eukaryota.
DR eggNOG; KOG4170; Eukaryota.
DR InParanoid; O62742; -.
DR OrthoDB; 661265at2759; -.
DR EvolutionaryTrace; O62742; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0120020; F:cholesterol transfer activity; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS:UniProtKB.
DR GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.30.1050.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02036; SCP2; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF55718; SSF55718; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Alternative initiation;
KW Cytoplasm; Endoplasmic reticulum; Lipid metabolism; Lipid transport;
KW Lipid-binding; Mitochondrion; Peroxisome; Phosphoprotein;
KW Reference proteome; Transferase; Transport.
FT CHAIN 1..547
FT /note="Sterol carrier protein 2"
FT /id="PRO_0000034095"
FT DOMAIN 433..543
FT /note="SCP2"
FT MOTIF 545..547
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11915"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 132
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 132
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 168
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 183
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22307"
FT MOD_RES 183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 282
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 341
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 341
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 432
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 432
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 438
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22307"
FT MOD_RES 438
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 443
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 443
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 453
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 453
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 464
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 470
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22307"
FT MOD_RES 470
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 479
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 491
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 492
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 511
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 522
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 534
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 544
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT VAR_SEQ 1..404
FT /note="Missing (in isoform SCP2)"
FT /evidence="ECO:0000303|PubMed:9711242"
FT /id="VSP_018896"
FT HELIX 432..454
FT /evidence="ECO:0007829|PDB:1C44"
FT STRAND 457..465
FT /evidence="ECO:0007829|PDB:1C44"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:1C44"
FT STRAND 472..480
FT /evidence="ECO:0007829|PDB:1C44"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:1C44"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:1C44"
FT HELIX 501..508
FT /evidence="ECO:0007829|PDB:1C44"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:1C44"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:1C44"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:1C44"
FT SITE O62742-2:20..21
FT /note="Cleavage"
FT /evidence="ECO:0000305|PubMed:9711242"
SQ SEQUENCE 547 AA; 58904 MW; 32BE7F7DCBF9BCD7 CRC64;
MSSSARKLAP LPRVFVVGVG MTKFVKPGTE DARDYPDMAK EAGQKALADA QIPYSAVEQA
CIGYVYGDST CGQRAVYHSL GLTGIPIINV NNNCSTGSTA LFMGRQLIQG GMAECVLALG
FEKMERGSLG AKFPDRTNPM DKHLDVLINK YGLSAHPVAP QMFGSAGKEH MEKYGTKIEH
FAKIGWKNHK HSVNNPYSQF QKEYSLDEVM SSRPIFDFLT VLQCCPTSDG AAAAILASEE
FVKKYGLQSK AVEILAQEMV TDFPSSFEEK SIIKMVGFDM SKEAARRCYE KSGLRPSDID
VIELHDCFSA NELLTYEALG LCPEGKGGAL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT
GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGLGGAAVV TLYKMGFPEA ASSFRTHQIE
AAPTSSAGDG FKANLVFKEI EKKLEEEGEQ FVKKIGGIFA FKVKDGPGGK EATWVVDVKN
GKGSVLPNSD KKADCTITIA DSDLLALMTG KMNPQSAFFQ GKLKITGNMG LAMKLQNLQL
QPGKAKL
