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E3 ubiquitin-protein ligase TRIM23 (EC 2.3.2.27) (ADP-ribosylation factor domain-containing protein 1) (GTP-binding protein ARD-1) (RING finger protein 46) (RING-type E3 ubiquitin transferase TRIM23) (Tripartite motif-containing protein 23)

 TRI23_HUMAN             Reviewed;         574 AA.
P36406; Q9BZY4; Q9BZY5;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 175.
RecName: Full=E3 ubiquitin-protein ligase TRIM23;
EC=2.3.2.27;
AltName: Full=ADP-ribosylation factor domain-containing protein 1;
AltName: Full=GTP-binding protein ARD-1;
AltName: Full=RING finger protein 46;
AltName: Full=RING-type E3 ubiquitin transferase TRIM23 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 23;
Name=TRIM23; Synonyms=ARD1, ARFD1, RNF46;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
PubMed=8473324;
Mishima K., Tsuchiya M., Nightingale M.S., Moss J., Vaughan M.;
"ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-
terminal ADP-ribosylation factor domain.";
J. Biol. Chem. 268:8801-8807(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
Minucci S., Pelicci P.G., Ballabio A.;
"The tripartite motif family identifies cell compartments.";
EMBO J. 20:2140-2151(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION.
PubMed=9671726; DOI=10.1073/pnas.95.15.8613;
Vitale N., Horiba K., Ferrans V.J., Moss J., Vaughan M.;
"Localization of ADP-ribosylation factor domain protein 1 (ARD1) in
lysosomes and Golgi apparatus.";
Proc. Natl. Acad. Sci. U.S.A. 95:8613-8618(1998).
[5]
INTERACTION WITH PSCD1, AND MUTAGENESIS OF THR-418 AND LYS-458.
PubMed=10748148; DOI=10.1074/jbc.M909642199;
Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W.,
Moss J., Vaughan M.;
"Specific functional interaction of human cytohesin-1 and ADP-
ribosylation factor domain protein (ARD1).";
J. Biol. Chem. 275:21331-21339(2000).
[6]
FUNCTION, AND MUTAGENESIS OF CYS-34 AND HIS-53.
PubMed=15684077; DOI=10.1073/pnas.0409800102;
Vichi A., Payne D.M., Pacheco-Rodriguez G., Moss J., Vaughan M.;
"E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-
ribosylation factor domain protein 1).";
Proc. Natl. Acad. Sci. U.S.A. 102:1945-1950(2005).
[7]
INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL144.
PubMed=19176615; DOI=10.1128/JVI.02072-08;
Poole E., Groves I., MacDonald A., Pang Y., Alcami A., Sinclair J.;
"Identification of TRIM23 as a cofactor involved in the regulation of
NF-kappaB by human cytomegalovirus.";
J. Virol. 83:3581-3590(2009).
-!- FUNCTION: Acts as an E3 ubiquitin-protein ligase. In the presence
of the human cytomegalovirus (HCMV) protein UL144, participates in
'Lys-63'-linked auto-ubiquitination of TRAF6 resulting in the
virally controlled activation of NF-kappa-B at early time of
infection. The C-terminus can act as an allosteric activator of
the cholera toxin catalytic subunit.
{ECO:0000269|PubMed:15684077}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with PSCD1. Interacts with human
cytomegalovirus protein UL144; this interaction might causes auto-
ubiquitination of TRAF6, leading to NF-kappaB activation.
{ECO:0000269|PubMed:10748148, ECO:0000269|PubMed:19176615}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-740098, EBI-740098;
G2XKQ0:-; NbExp=3; IntAct=EBI-740098, EBI-10175576;
Q96IX9:ANKRD36BP1; NbExp=3; IntAct=EBI-740098, EBI-744859;
P29972:AQP1; NbExp=5; IntAct=EBI-740098, EBI-745213;
Q8N6T3:ARFGAP1; NbExp=3; IntAct=EBI-740098, EBI-716933;
Q9NR81:ARHGEF3; NbExp=3; IntAct=EBI-740098, EBI-10312733;
Q8N5M1:ATPAF2; NbExp=6; IntAct=EBI-740098, EBI-1166928;
Q99933:BAG1; NbExp=5; IntAct=EBI-740098, EBI-1030678;
Q0VDD7:C19orf57; NbExp=4; IntAct=EBI-740098, EBI-741210;
Q9H7E9:C8orf33; NbExp=3; IntAct=EBI-740098, EBI-715389;
Q9H257:CARD9; NbExp=3; IntAct=EBI-740098, EBI-751319;
Q8IYE0-2:CCDC146; NbExp=3; IntAct=EBI-740098, EBI-10247802;
Q86WR0:CCDC25; NbExp=3; IntAct=EBI-740098, EBI-2690264;
Q86Y33:CDC20B; NbExp=3; IntAct=EBI-740098, EBI-10260504;
Q01850:CDR2; NbExp=5; IntAct=EBI-740098, EBI-1181367;
Q96M91:CFAP53; NbExp=3; IntAct=EBI-740098, EBI-742422;
P10606:COX5B; NbExp=4; IntAct=EBI-740098, EBI-1053725;
Q02930-3:CREB5; NbExp=3; IntAct=EBI-740098, EBI-10192698;
O95715:CXCL14; NbExp=3; IntAct=EBI-740098, EBI-2798068;
O43602:DCX; NbExp=3; IntAct=EBI-740098, EBI-8646694;
Q14565:DMC1; NbExp=3; IntAct=EBI-740098, EBI-930865;
Q9NQL9:DMRT3; NbExp=3; IntAct=EBI-740098, EBI-9679045;
Q92608:DOCK2; NbExp=3; IntAct=EBI-740098, EBI-448771;
Q96CJ1:EAF2; NbExp=3; IntAct=EBI-740098, EBI-1245604;
O95208-2:EPN2; NbExp=4; IntAct=EBI-740098, EBI-12135243;
Q8N2X6:EXOC3-AS1; NbExp=5; IntAct=EBI-740098, EBI-749333;
Q9BTL3:FAM103A1; NbExp=5; IntAct=EBI-740098, EBI-744023;
Q9BQ89:FAM110A; NbExp=5; IntAct=EBI-740098, EBI-1752811;
Q8N9E0:FAM133A; NbExp=5; IntAct=EBI-740098, EBI-10268158;
Q96PV7-2:FAM193B; NbExp=3; IntAct=EBI-740098, EBI-10292648;
Q5VWN6-2:FAM208B; NbExp=3; IntAct=EBI-740098, EBI-10172380;
Q86UY5:FAM83A; NbExp=3; IntAct=EBI-740098, EBI-1384254;
Q86YD7:FAM90A1; NbExp=5; IntAct=EBI-740098, EBI-6658203;
Q8TES7-6:FBF1; NbExp=3; IntAct=EBI-740098, EBI-10244131;
C0H5X2:FLJ38668; NbExp=3; IntAct=EBI-740098, EBI-10176227;
P23769:GATA2; NbExp=3; IntAct=EBI-740098, EBI-2806671;
P55040:GEM; NbExp=5; IntAct=EBI-740098, EBI-744104;
Q8NEA9:GMCL1P1; NbExp=3; IntAct=EBI-740098, EBI-745707;
O95872:GPANK1; NbExp=7; IntAct=EBI-740098, EBI-751540;
Q92917:GPKOW; NbExp=3; IntAct=EBI-740098, EBI-746309;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-740098, EBI-2514791;
P09022:Hoxa1 (xeno); NbExp=2; IntAct=EBI-740098, EBI-3957603;
P09067:HOXB5; NbExp=5; IntAct=EBI-740098, EBI-3893317;
Q9UBY9:HSPB7; NbExp=3; IntAct=EBI-740098, EBI-739361;
Q8NA54:IQUB; NbExp=5; IntAct=EBI-740098, EBI-10220600;
Q15040:JOSD1; NbExp=3; IntAct=EBI-740098, EBI-2510602;
Q92993:KAT5; NbExp=3; IntAct=EBI-740098, EBI-399080;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-740098, EBI-2125614;
Q9P2K6:KLHL42; NbExp=5; IntAct=EBI-740098, EBI-739890;
P02538:KRT6A; NbExp=8; IntAct=EBI-740098, EBI-702198;
O00214:LGALS8; NbExp=3; IntAct=EBI-740098, EBI-740058;
Q96FQ7:LINC00526; NbExp=3; IntAct=EBI-740098, EBI-10286106;
P25791:LMO2; NbExp=3; IntAct=EBI-740098, EBI-739696;
Q8NDC4:MORN4; NbExp=5; IntAct=EBI-740098, EBI-10269566;
Q9BYD3:MRPL4; NbExp=3; IntAct=EBI-740098, EBI-721368;
Q9BRJ2:MRPL45; NbExp=3; IntAct=EBI-740098, EBI-2514313;
Q6P444:MTFR2; NbExp=3; IntAct=EBI-740098, EBI-10252703;
P52179-2:MYOM1; NbExp=4; IntAct=EBI-740098, EBI-12010196;
Q9HC98:NEK6; NbExp=3; IntAct=EBI-740098, EBI-740364;
Q9UMS0:NFU1; NbExp=3; IntAct=EBI-740098, EBI-725252;
Q9NPJ8:NXT2; NbExp=3; IntAct=EBI-740098, EBI-752122;
O43189:PHF1; NbExp=3; IntAct=EBI-740098, EBI-530034;
O75928:PIAS2; NbExp=3; IntAct=EBI-740098, EBI-348555;
O00459:PIK3R2; NbExp=3; IntAct=EBI-740098, EBI-346930;
Q99569:PKP4; NbExp=3; IntAct=EBI-740098, EBI-726447;
Q9UGP5-2:POLL; NbExp=3; IntAct=EBI-740098, EBI-10320765;
Q13356:PPIL2; NbExp=3; IntAct=EBI-740098, EBI-7705988;
Q6NYC8:PPP1R18; NbExp=3; IntAct=EBI-740098, EBI-2557469;
P25786:PSMA1; NbExp=5; IntAct=EBI-740098, EBI-359352;
Q63HN8-6:RNF213; NbExp=3; IntAct=EBI-740098, EBI-10248548;
Q7L4I2-2:RSRC2; NbExp=3; IntAct=EBI-740098, EBI-10256202;
Q14D33:RTP5; NbExp=3; IntAct=EBI-740098, EBI-10217913;
Q9BWG6:SCNM1; NbExp=4; IntAct=EBI-740098, EBI-748391;
Q9H788:SH2D4A; NbExp=3; IntAct=EBI-740098, EBI-747035;
Q9H788-2:SH2D4A; NbExp=3; IntAct=EBI-740098, EBI-10308083;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-740098, EBI-747107;
P12236:SLC25A6; NbExp=3; IntAct=EBI-740098, EBI-356254;
Q9H0W8:SMG9; NbExp=5; IntAct=EBI-740098, EBI-2872322;
O95863:SNAI1; NbExp=5; IntAct=EBI-740098, EBI-1045459;
O43623:SNAI2; NbExp=3; IntAct=EBI-740098, EBI-9876238;
P14678-2:SNRPB; NbExp=3; IntAct=EBI-740098, EBI-372475;
O60504:SORBS3; NbExp=5; IntAct=EBI-740098, EBI-741237;
Q9NZD8:SPG21; NbExp=3; IntAct=EBI-740098, EBI-742688;
B7ZLI8:STK19; NbExp=3; IntAct=EBI-740098, EBI-10176124;
Q9NU19:TBC1D22B; NbExp=5; IntAct=EBI-740098, EBI-8787464;
Q0P5Q0:TMSB4X; NbExp=3; IntAct=EBI-740098, EBI-10226570;
P21580:TNFAIP3; NbExp=5; IntAct=EBI-740098, EBI-527670;
Q13077:TRAF1; NbExp=3; IntAct=EBI-740098, EBI-359224;
Q0P6H7:TRIM29; NbExp=3; IntAct=EBI-740098, EBI-10226710;
Q14134:TRIM29; NbExp=3; IntAct=EBI-740098, EBI-702370;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-740098, EBI-5235829;
Q12815:TROAP; NbExp=5; IntAct=EBI-740098, EBI-2349743;
Q63HK5:TSHZ3; NbExp=3; IntAct=EBI-740098, EBI-9053916;
Q86UY0:TXNDC5; NbExp=3; IntAct=EBI-740098, EBI-2825190;
Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-740098, EBI-10180829;
Q9Y2K6:USP20; NbExp=3; IntAct=EBI-740098, EBI-2511991;
Q9BRU9:UTP23; NbExp=3; IntAct=EBI-740098, EBI-5457544;
Q64LD2:WDR25; NbExp=3; IntAct=EBI-740098, EBI-744560;
Q53FD0:ZC2HC1C; NbExp=3; IntAct=EBI-740098, EBI-740767;
Q9H9D4:ZNF408; NbExp=4; IntAct=EBI-740098, EBI-347633;
Q8TBZ8:ZNF564; NbExp=5; IntAct=EBI-740098, EBI-10273713;
Q9P0T4:ZNF581; NbExp=6; IntAct=EBI-740098, EBI-745520;
-!- SUBCELLULAR LOCATION: Endomembrane system
{ECO:0000269|PubMed:9671726}. Golgi apparatus membrane
{ECO:0000269|PubMed:9671726}. Lysosome membrane
{ECO:0000269|PubMed:9671726}. Note=Membrane-associated with the
Golgi complex and lysosomal structures.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Alpha;
IsoId=P36406-1; Sequence=Displayed;
Name=Beta;
IsoId=P36406-2; Sequence=VSP_000296;
Name=Gamma;
IsoId=P36406-3; Sequence=VSP_000297;
-!- DOMAIN: The RING-type zinc finger domain is responsible for E3
ubiquitin ligase activity.
-!- SIMILARITY: In the C-terminal section; belongs to the small GTPase
superfamily. Arf family. {ECO:0000305}.
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EMBL; L04510; AAA35940.1; -; mRNA.
EMBL; AF230397; AAG50176.1; -; mRNA.
EMBL; AF230398; AAG50177.1; -; mRNA.
EMBL; AF230399; AAG50178.1; -; mRNA.
EMBL; BC022510; AAH22510.1; -; mRNA.
CCDS; CCDS3986.1; -. [P36406-3]
CCDS; CCDS3987.1; -. [P36406-1]
CCDS; CCDS43322.1; -. [P36406-2]
PIR; A46054; A46054.
RefSeq; NP_001647.1; NM_001656.3. [P36406-1]
RefSeq; NP_150230.1; NM_033227.2. [P36406-2]
RefSeq; NP_150231.1; NM_033228.2. [P36406-3]
RefSeq; XP_016864933.1; XM_017009444.1. [P36406-2]
UniGene; Hs.792; -.
PDB; 5VZV; X-ray; 1.81 A; A/B/C=1-123.
PDB; 5VZW; X-ray; 2.28 A; F/G=1-123.
PDBsum; 5VZV; -.
PDBsum; 5VZW; -.
ProteinModelPortal; P36406; -.
SMR; P36406; -.
BioGrid; 106868; 153.
CORUM; P36406; -.
IntAct; P36406; 193.
MINT; MINT-1442172; -.
STRING; 9606.ENSP00000231524; -.
iPTMnet; P36406; -.
PhosphoSitePlus; P36406; -.
BioMuta; TRIM23; -.
DMDM; 543839; -.
EPD; P36406; -.
MaxQB; P36406; -.
PaxDb; P36406; -.
PeptideAtlas; P36406; -.
PRIDE; P36406; -.
DNASU; 373; -.
Ensembl; ENST00000231524; ENSP00000231524; ENSG00000113595. [P36406-1]
Ensembl; ENST00000274327; ENSP00000274327; ENSG00000113595. [P36406-3]
Ensembl; ENST00000381018; ENSP00000370406; ENSG00000113595. [P36406-2]
GeneID; 373; -.
KEGG; hsa:373; -.
UCSC; uc003jtw.4; human. [P36406-1]
CTD; 373; -.
DisGeNET; 373; -.
EuPathDB; HostDB:ENSG00000113595.14; -.
GeneCards; TRIM23; -.
HGNC; HGNC:660; TRIM23.
HPA; HPA039605; -.
MIM; 601747; gene.
neXtProt; NX_P36406; -.
OpenTargets; ENSG00000113595; -.
PharmGKB; PA24943; -.
eggNOG; KOG0070; Eukaryota.
eggNOG; KOG4185; Eukaryota.
eggNOG; ENOG410ZGPK; LUCA.
GeneTree; ENSGT00780000121855; -.
HOGENOM; HOG000008208; -.
HOVERGEN; HBG000551; -.
InParanoid; P36406; -.
KO; K07963; -.
OMA; TACLHCE; -.
OrthoDB; EOG091G05L6; -.
PhylomeDB; P36406; -.
TreeFam; TF320703; -.
UniPathway; UPA00143; -.
GeneWiki; TRIM23; -.
GenomeRNAi; 373; -.
PRO; PR:P36406; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113595; -.
CleanEx; HS_TRIM23; -.
ExpressionAtlas; P36406; baseline and differential.
Genevisible; P36406; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IDA:HGNC.
GO; GO:0005765; C:lysosomal membrane; IDA:HGNC.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO; GO:0019003; F:GDP binding; IDA:HGNC.
GO; GO:0005525; F:GTP binding; IDA:HGNC.
GO; GO:0003924; F:GTPase activity; IDA:HGNC.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:HGNC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0016567; P:protein ubiquitination; IDA:HGNC.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00021; BBOX; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR003649; Bbox_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR024156; Small_GTPase_ARF.
InterPro; IPR006689; Small_GTPase_ARF/SAR.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR013087; Znf_C2H2_type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00025; Arf; 1.
Pfam; PF00643; zf-B_box; 1.
Pfam; PF13445; zf-RING_UBOX; 1.
PRINTS; PR00328; SAR1GTPBP.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 2.
SMART; SM00184; RING; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51417; ARF; 1.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Golgi apparatus; GTP-binding; Host-virus interaction; Lysosome;
Membrane; Metal-binding; Nucleotide-binding; Polymorphism;
Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 574 E3 ubiquitin-protein ligase TRIM23.
/FTId=PRO_0000207483.
ZN_FING 31 76 RING-type; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 122 168 B box-type; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00024}.
NP_BIND 411 418 GTP. {ECO:0000250}.
NP_BIND 454 458 GTP. {ECO:0000250}.
NP_BIND 513 516 GTP. {ECO:0000250}.
REGION 390 574 ARF-like.
COILED 352 379 {ECO:0000255}.
VAR_SEQ 541 574 WYIQGCDARSGMGLYEGLDWLSRQLVAAGVLDVA -> CFS
DNM (in isoform Gamma).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_000297.
VAR_SEQ 551 574 GMGLYEGLDWLSRQLVAAGVLDVA -> VFQIICDQYTGKE
VVTEKG (in isoform Beta).
{ECO:0000303|PubMed:11331580}.
/FTId=VSP_000296.
VARIANT 480 480 D -> N (in dbSNP:rs34046496).
/FTId=VAR_048320.
MUTAGEN 34 34 C->A: Loss of E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:15684077}.
MUTAGEN 53 53 H->A: Loss of E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:15684077}.
MUTAGEN 418 418 T->N: Maintains GTPase activity.
Increases interaction with PSCD1.
{ECO:0000269|PubMed:10748148}.
MUTAGEN 458 458 K->I: Suppresses GTPase activity.
Decreases interaction with PSCD1.
{ECO:0000269|PubMed:10748148}.
TURN 32 34 {ECO:0000244|PDB:5VZV}.
STRAND 40 42 {ECO:0000244|PDB:5VZV}.
STRAND 46 48 {ECO:0000244|PDB:5VZV}.
STRAND 54 56 {ECO:0000244|PDB:5VZV}.
HELIX 57 62 {ECO:0000244|PDB:5VZV}.
STRAND 69 71 {ECO:0000244|PDB:5VZV}.
TURN 73 75 {ECO:0000244|PDB:5VZV}.
STRAND 78 80 {ECO:0000244|PDB:5VZV}.
HELIX 85 88 {ECO:0000244|PDB:5VZV}.
HELIX 93 103 {ECO:0000244|PDB:5VZV}.
SEQUENCE 574 AA; 64067 MW; CB85923B29BF0320 CRC64;
MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL
TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGPIGQY GAAEESIGIS
GESIIRCDED EAHLASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ
HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF
TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC
RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD CRVVLAKQEI
TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI
LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD
SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS
WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA


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