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Tripartite motif-containing protein 5 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM5) (TRIM5alpha)

 TRIM5_MACMU             Reviewed;         497 AA.
Q0PF16; Q0PF17; Q2YEN1; Q6GX25; Q6QWE9; Q6QWF0;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 96.
RecName: Full=Tripartite motif-containing protein 5;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase TRIM5 {ECO:0000305};
AltName: Full=TRIM5alpha;
Name=TRIM5;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=15249690; DOI=10.1073/pnas.0402876101;
Yap M.W., Nisole S., Lynch C., Stoye J.P.;
"Trim5alpha protein restricts both HIV-1 and murine leukemia virus.";
Proc. Natl. Acad. Sci. U.S.A. 101:10786-10791(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=16226405; DOI=10.1016/j.gene.2005.06.045;
Liu H.L., Wang Y.Q., Liao C.H., Kuang Y.Q., Zheng Y.T., Su B.;
"Adaptive evolution of primate TRIM5alpha, a gene restricting HIV-1
infection.";
Gene 362:109-116(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=17142324; DOI=10.1073/pnas.0605838103;
Newman R.M., Hall L., Connole M., Chen G.L., Sato S., Yuste E.,
Diehl W., Hunter E., Kaur A., Miller G.M., Johnson W.E.;
"Balancing selection and the evolution of functional polymorphism in
Old World monkey TRIM5alpha.";
Proc. Natl. Acad. Sci. U.S.A. 103:19134-19139(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Stremlau M.H., Sodroski J.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Miller C.J., Dutra J.C.;
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
TRIMERIZATION.
PubMed=16254380; DOI=10.1128/JVI.79.22.14446-14450.2005;
Mische C.C., Javanbakht H., Song B., Diaz-Griffero F., Stremlau M.,
Strack B., Si Z., Sodroski J.;
"Retroviral restriction factor TRIM5alpha is a trimer.";
J. Virol. 79:14446-14450(2005).
[7]
TRIMERIZATION.
PubMed=16808955; DOI=10.1016/j.virol.2006.05.017;
Javanbakht H., Yuan W., Yeung D.F., Song B., Diaz-Griffero F., Li Y.,
Li X., Stremlau M., Sodroski J.;
"Characterization of TRIM5alpha trimerization and its contribution to
human immunodeficiency virus capsid binding.";
Virology 353:234-246(2006).
[8]
SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=17156811; DOI=10.1016/j.virol.2006.10.035;
Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y.,
Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C.,
Dean M., Sodroski J.;
"Unique features of TRIM5alpha among closely related human TRIM family
members.";
Virology 360:419-433(2007).
[9]
INTERACTION WITH HSPA1A/B AND HSPA8, AND AUTOUBIQUITINATION.
PubMed=20053985; DOI=10.1074/jbc.M109.040618;
Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S.,
Song B.;
"Hsp70 interacts with the retroviral restriction factor TRIM5alpha and
assists the folding of TRIM5alpha.";
J. Biol. Chem. 285:7827-7837(2010).
[10]
INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
PubMed=20357094; DOI=10.1128/JVI.02412-09;
O'Connor C., Pertel T., Gray S., Robia S.L., Bakowska J.C., Luban J.,
Campbell E.M.;
"p62/sequestosome-1 associates with and sustains the expression of
retroviral restriction factor TRIM5alpha.";
J. Virol. 84:5997-6006(2010).
[11]
REVIEW.
PubMed=21247355; DOI=10.1089/AID.2010.0367;
Sastri J., Campbell E.M.;
"Recent insights into the mechanism and consequences of TRIM5alpha
retroviral restriction.";
AIDS Res. Hum. Retroviruses 27:231-238(2011).
[12]
INTERACTION WITH TRIM6 AND TRIM34, MUTAGENESIS OF ILE-165; TRP-172;
ILE-176; LEU-194; LEU-202; LEU-205; LEU-216; SER-219; MET-230;
ILE-234; LEU-237 AND 247-ASP--LEU-249, AND DOMAIN.
PubMed=21680743; DOI=10.1074/jbc.M111.260406;
Li X., Yeung D.F., Fiegen A.M., Sodroski J.;
"Determinants of the higher order association of the restriction
factor TRIM5alpha and other tripartite motif (TRIM) proteins.";
J. Biol. Chem. 286:27959-27970(2011).
[13]
FUNCTION, DOMAIN RING, SUBUNIT, AND AUTOUBIQUITINATION.
PubMed=21734049; DOI=10.1128/JVI.00497-11;
Lienlaf M., Hayashi F., Di Nunzio F., Tochio N., Kigawa T.,
Yokoyama S., Diaz-Griffero F.;
"Contribution of E3-ubiquitin ligase activity to HIV-1 restriction by
TRIM5alpha(rh): structure of the RING domain of TRIM5alpha.";
J. Virol. 85:8725-8737(2011).
[14]
SUBUNIT.
PubMed=21187419; DOI=10.1073/pnas.1013426108;
Ganser-Pornillos B.K., Chandrasekaran V., Pornillos O., Sodroski J.G.,
Sundquist W.I., Yeager M.;
"Hexagonal assembly of a restricting TRIM5alpha protein.";
Proc. Natl. Acad. Sci. U.S.A. 108:534-539(2011).
[15]
INTERACTION WITH PSMC2; PSMC4; PSMC5 AND PSMD7, AND SUBCELLULAR
LOCATION.
PubMed=22078707; DOI=10.1186/1742-4690-8-93;
Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
Luban J., Campbell E.M.;
"TRIM5alpha associates with proteasomal subunits in cells while in
complex with HIV-1 virions.";
Retrovirology 8:93-93(2011).
[16]
FUNCTION.
PubMed=21035162; DOI=10.1016/j.virol.2010.09.018;
Tareen S.U., Emerman M.;
"Human Trim5alpha has additional activities that are uncoupled from
retroviral capsid recognition.";
Virology 409:113-120(2011).
[17]
REVIEW.
PubMed=21994740; DOI=10.3390/v3050423;
Diaz-Griffero F.;
"Caging the beast: TRIM5-binding to the HIV-1 core.";
Viruses 3:423-428(2011).
[18]
REVIEW.
PubMed=22482711; DOI=10.1016/j.coviro.2012.02.003;
Gruetter M.G., Luban J.;
"TRIM5 structure, HIV-1 capsid recognition, and innate immune
signaling.";
Curr. Opin. Virol. 2:142-150(2012).
[19]
REVIEW, AND FUNCTION.
PubMed=22291694; DOI=10.3389/fmicb.2012.00013;
Nakayama E.E., Shioda T.;
"TRIM5alpha and species tropism of HIV/SIV.";
Front. Microbiol. 3:13-13(2012).
[20]
REVIEW.
PubMed=22701176; DOI=10.1155/2012/426840;
Luban J.;
"TRIM5 and the regulation of HIV-1 infectivity.";
Mol. Biol. Int. 2012:426840-426840(2012).
[21]
FUNCTION, INTERACTION WITH BECN1; SQSTM1 AND GABARAP, AND SUBCELLULAR
LOCATION.
PubMed=25127057; DOI=10.1016/j.devcel.2014.06.013;
Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T.,
Dinkins C., Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y.,
Levine B., Johansen T., Deretic V.;
"TRIM proteins regulate autophagy and can target autophagic substrates
by direct recognition.";
Dev. Cell 30:394-409(2014).
[22]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 292-497.
PubMed=22847415; DOI=10.1073/pnas.1203536109;
Biris N., Yang Y., Taylor A.B., Tomashevski A., Guo M., Hart P.J.,
Diaz-Griffero F., Ivanov D.N.;
"Structure of the rhesus monkey TRIM5alpha PRYSPRY domain, the HIV
capsid recognition module.";
Proc. Natl. Acad. Sci. U.S.A. 109:13278-13283(2012).
-!- FUNCTION: Capsid-specific restriction factor that prevents
infection from non-host-adapted retroviruses. Blocks viral
replication early in the life cycle, after viral entry but before
reverse transcription. In addition to acting as a capsid-specific
restriction factor, also acts as a pattern recognition receptor
that activates innate immune signaling in response to the
retroviral capsid lattice. Binding to the viral capsid triggers
its E3 ubiquitin ligase activity, and in concert with the
heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N
(also known as UBC13-UEV1A complex) generates 'Lys-63'-linked
polyubiquitin chains, which in turn are catalysts in the
autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1,
TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by
autophosphorylation results in the induction and expression of NF-
kappa-B and MAPK-responsive inflammatory genes, thereby leading to
an innate immune response in the infected cell. Restricts
infection by human immunodeficiency virus type 1 (HIV-1) and
simian immunodeficiency virus (SIV-agm). Plays a role in
regulating autophagy through activation of autophagy regulator
BECN1 by causing its dissociation from its inhibitors BCL2 and
TAB2 (PubMed:25127057). Also plays a role in autophagy by acting
as a selective autophagy receptor which recognizes and targets
HIV-1 capsid protein p24 for autophagic destruction
(PubMed:25127057). {ECO:0000269|PubMed:21035162,
ECO:0000269|PubMed:21734049, ECO:0000269|PubMed:22291694,
ECO:0000269|PubMed:25127057}.
-!- 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: Can form homodimers and homotrimers. In addition to
lower-order dimerization, also exhibits a higher-order
multimerization and both low- and high-order multimerizations are
essential for its restriction activity. Interacts with
MAP3K7/TAK1, TAB2 and TAB3 (By similarity). Interacts with
HSPA8/HSC70, PSMC2, PSMC4, PSMC5 and PSMD7 (PubMed:20053985,
PubMed:22078707). Interacts with SQSTM1 (PubMed:20357094,
PubMed:25127057). Interacts (via B30.2/SPRY domain) with HSPA1A/B.
Interacts with TRIM6 and TRIM34 (PubMed:21680743). Interacts with
BECN1; GABARAP (PubMed:25127057). Interacts with ULK1
(phosphorylated form), GABARAPL1, GABARAPL2, MAP1LC3A and MAP1LC3C
(By similarity). {ECO:0000250|UniProtKB:Q9C035,
ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:20053985,
ECO:0000269|PubMed:20357094, ECO:0000269|PubMed:21187419,
ECO:0000269|PubMed:21680743, ECO:0000269|PubMed:21734049,
ECO:0000269|PubMed:22078707, ECO:0000269|PubMed:25127057}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-923856, EBI-923856;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811,
ECO:0000269|PubMed:25127057}. Cytoplasm, P-body
{ECO:0000269|PubMed:20357094, ECO:0000269|PubMed:22078707}.
Nucleus {ECO:0000269|PubMed:17156811}. Note=Predominantly
cytoplasmic, and is only occasionally and partially localized in
the nucleus (PubMed:25127057, PubMed:17156811). Closely associates
with proteasomal subunits in cytoplasmic bodies (PubMed:22078707).
Colocalizes with SQSTM1 in cytoplasmic bodies (PubMed:20357094).
{ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:20357094,
ECO:0000269|PubMed:22078707, ECO:0000269|PubMed:25127057}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q0PF16-1; Sequence=Displayed;
Name=2;
IsoId=Q0PF16-2; Sequence=VSP_022569, VSP_022570;
Note=No experimental confirmation available.;
-!- DOMAIN: The B box-type zinc finger domain and the coiled-coil
domain contribute to the higher and low order multimerization
respectively which is essential for restriction activity (By
similarity). The coiled coil domain is important for higher order
multimerization by promoting the initial dimerization
(PubMed:21680743). {ECO:0000250|UniProtKB:Q9C035,
ECO:0000269|PubMed:21680743}.
-!- DOMAIN: The B30.2/SPRY domain acts as a capsid recognition domain.
Polymorphisms in this domain explain the observed species-specific
differences among orthologs. {ECO:0000269|PubMed:21734049}.
-!- DOMAIN: The RING-type zinc finger domain confers E3 ubiquitin
ligase activity and is essential for retrovirus restriction
activity, autoubiquitination and higher-order multimerization.
{ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:21734049}.
-!- PTM: Degraded in a proteasome-independent fashion in the absence
of viral infection but in a proteasome-dependent fashion following
exposure to restriction sensitive virus. {ECO:0000250}.
-!- PTM: Autoubiquitinated in a RING finger- and UBE2D2-dependent
manner. Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia
YopJ. Ubiquitination may not lead to proteasomal degradation.
{ECO:0000269|PubMed:20053985, ECO:0000269|PubMed:21734049}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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EMBL; AY625001; AAT48102.1; -; mRNA.
EMBL; AY899886; AAX86682.1; -; Genomic_DNA.
EMBL; AY899880; AAX86682.1; JOINED; Genomic_DNA.
EMBL; AY899881; AAX86682.1; JOINED; Genomic_DNA.
EMBL; AY899882; AAX86682.1; JOINED; Genomic_DNA.
EMBL; AY899883; AAX86682.1; JOINED; Genomic_DNA.
EMBL; AY899884; AAX86682.1; JOINED; Genomic_DNA.
EMBL; AY899885; AAX86682.1; JOINED; Genomic_DNA.
EMBL; EF113914; ABL14041.1; -; mRNA.
EMBL; AY523632; AAS48505.1; -; mRNA.
EMBL; AY523633; AAS48506.1; -; mRNA.
EMBL; DQ842020; ABG67966.1; -; mRNA.
EMBL; DQ842021; ABG67967.1; -; mRNA.
RefSeq; NP_001028082.1; NM_001032910.1.
UniGene; Mmu.3751; -.
PDB; 2LM3; NMR; -; A=292-497.
PDB; 3UV9; X-ray; 1.55 A; A=292-325, A=350-497.
PDB; 4B3N; X-ray; 3.30 A; A/B=275-493.
PDB; 4TKP; X-ray; 2.08 A; B=2-92.
PDB; 5EIU; X-ray; 1.91 A; A/D=89-159, A/D=226-265.
PDB; 5F7T; X-ray; 2.29 A; E/F/H/L=89-159, E/F/H/L=226-265.
PDB; 5IEA; X-ray; 3.26 A; A/B/C/D/F/K=89-159, A/B/C/D/F/K=226-265.
PDB; 5K3Q; X-ray; 1.80 A; A/B/C/D=94-154, A/B/C/D=229-261.
PDBsum; 2LM3; -.
PDBsum; 3UV9; -.
PDBsum; 4B3N; -.
PDBsum; 4TKP; -.
PDBsum; 5EIU; -.
PDBsum; 5F7T; -.
PDBsum; 5IEA; -.
PDBsum; 5K3Q; -.
ProteinModelPortal; Q0PF16; -.
SMR; Q0PF16; -.
BioGrid; 695095; 11.
IntAct; Q0PF16; 1.
STRING; 9544.ENSMMUP00000000454; -.
Ensembl; ENSMMUT00000000490; ENSMMUP00000000454; ENSMMUG00000000335. [Q0PF16-1]
GeneID; 574288; -.
KEGG; mcc:574288; -.
CTD; 85363; -.
eggNOG; ENOG410ITG7; Eukaryota.
eggNOG; ENOG410XWDC; LUCA.
GeneTree; ENSGT00760000118893; -.
HOGENOM; HOG000234134; -.
HOVERGEN; HBG001357; -.
InParanoid; Q0PF16; -.
KO; K10648; -.
OMA; ICPDRVG; -.
OrthoDB; EOG091G04O8; -.
TreeFam; TF338674; -.
UniPathway; UPA00143; -.
Proteomes; UP000006718; Chromosome 14.
Bgee; ENSMMUG00000000335; -.
ExpressionAtlas; Q0PF16; baseline and differential.
GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:1990462; C:omegasome; IEA:Ensembl.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030674; F:protein binding, bridging; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0008329; F:signaling pattern recognition receptor activity; ISS:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0002218; P:activation of innate immune response; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR032917; TRIM5.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR24103:SF426; PTHR24103:SF426; 1.
Pfam; PF00622; SPRY; 1.
Pfam; PF00643; zf-B_box; 1.
Pfam; PF13445; zf-RING_UBOX; 1.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00336; BBOX; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 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; Acetylation; Alternative splicing; Antiviral defense;
Autophagy; Coiled coil; Complete proteome; Cytoplasm; Immunity;
Innate immunity; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9C035}.
CHAIN 2 497 Tripartite motif-containing protein 5.
/FTId=PRO_0000273465.
DOMAIN 283 497 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 15 60 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 92 133 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
REGION 187 200 Required for interaction with GABARAP and
for autophagy.
{ECO:0000269|PubMed:25127057}.
COILED 137 225 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9C035}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C035}.
VAR_SEQ 301 333 VDVTLAPNNISHAVIAEDKRQVSSRNPQIMYQA -> GKEK
SHYHQPPCGLSLLLSLSFRILYSLLGLVF (in isoform
2). {ECO:0000303|Ref.4}.
/FTId=VSP_022569.
VAR_SEQ 334 497 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_022570.
MUTAGEN 165 165 I->K: No effect on dimerization or higher
order self-association.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 172 172 W->K: No effect on dimerization or higher
order self-association; when associated
with K-176.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 176 176 I->K: No effect on dimerization or higher
order self-association; when associated
with K-172.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 194 194 L->K: Fails to dimerise and exhibits
reduced higher order self association.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 202 202 L->K: No effect on dimerization or higher
order self-association.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 205 205 L->K: No effect on dimerization or higher
order self-association.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 216 216 L->K: No effect on dimerization or higher
order self-association.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 219 219 S->K: No effect on dimerization or higher
order self-association.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 230 230 M->K: No effect on dimerization or higher
order self-association.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 234 234 I->K: No effect on dimerization or higher
order self-association.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 237 237 L->K: No effect on dimerization or higher
order self-association.
{ECO:0000269|PubMed:21680743}.
MUTAGEN 247 249 DLL->KDD: No effect on dimerization but
exhibits a 3-fold decrease in the
efficiency of higher order association.
{ECO:0000269|PubMed:21680743}.
CONFLICT 7 7 L -> V (in Ref. 1; AAT48102).
{ECO:0000305}.
CONFLICT 174 174 I -> T (in Ref. 2; AAX86682).
{ECO:0000305}.
CONFLICT 177 177 D -> Q (in Ref. 2; AAX86682).
{ECO:0000305}.
CONFLICT 184 184 S -> L (in Ref. 2; AAX86682).
{ECO:0000305}.
CONFLICT 192 192 E -> D (in Ref. 2; AAX86682).
{ECO:0000305}.
CONFLICT 218 218 K -> N (in Ref. 2; AAX86682).
{ECO:0000305}.
CONFLICT 221 221 T -> M (in Ref. 5; ABG67967).
{ECO:0000305}.
CONFLICT 229 230 YM -> SL (in Ref. 2; AAX86682).
{ECO:0000305}.
CONFLICT 236 236 E -> D (in Ref. 2; AAX86682 and 5;
ABG67966). {ECO:0000305}.
CONFLICT 307 307 P -> T (in Ref. 1; AAT48102, 3; ABL14041
and 4; AAS48505). {ECO:0000305}.
CONFLICT 333 333 A -> S (in Ref. 5; ABG67966).
{ECO:0000305}.
CONFLICT 339 341 TFP -> Q (in Ref. 5; ABG67966).
{ECO:0000305}.
HELIX 6 12 {ECO:0000244|PDB:4TKP}.
TURN 16 18 {ECO:0000244|PDB:4TKP}.
STRAND 23 27 {ECO:0000244|PDB:4TKP}.
STRAND 33 35 {ECO:0000244|PDB:4TKP}.
HELIX 36 38 {ECO:0000244|PDB:4TKP}.
TURN 57 59 {ECO:0000244|PDB:4TKP}.
HELIX 72 79 {ECO:0000244|PDB:4TKP}.
TURN 98 100 {ECO:0000244|PDB:5K3Q}.
STRAND 106 108 {ECO:0000244|PDB:5K3Q}.
TURN 109 112 {ECO:0000244|PDB:5K3Q}.
STRAND 113 115 {ECO:0000244|PDB:5K3Q}.
HELIX 117 121 {ECO:0000244|PDB:5K3Q}.
HELIX 123 125 {ECO:0000244|PDB:5K3Q}.
STRAND 130 132 {ECO:0000244|PDB:5K3Q}.
HELIX 133 159 {ECO:0000244|PDB:5EIU}.
HELIX 226 242 {ECO:0000244|PDB:5EIU}.
HELIX 245 249 {ECO:0000244|PDB:5EIU}.
HELIX 252 261 {ECO:0000244|PDB:5EIU}.
HELIX 292 296 {ECO:0000244|PDB:3UV9}.
HELIX 297 299 {ECO:0000244|PDB:3UV9}.
STRAND 319 323 {ECO:0000244|PDB:4B3N}.
STRAND 327 329 {ECO:0000244|PDB:2LM3}.
TURN 330 332 {ECO:0000244|PDB:2LM3}.
STRAND 334 336 {ECO:0000244|PDB:2LM3}.
STRAND 352 356 {ECO:0000244|PDB:4B3N}.
STRAND 360 368 {ECO:0000244|PDB:3UV9}.
STRAND 375 381 {ECO:0000244|PDB:3UV9}.
TURN 384 390 {ECO:0000244|PDB:3UV9}.
HELIX 391 394 {ECO:0000244|PDB:3UV9}.
HELIX 399 401 {ECO:0000244|PDB:3UV9}.
STRAND 403 409 {ECO:0000244|PDB:3UV9}.
TURN 410 412 {ECO:0000244|PDB:3UV9}.
STRAND 413 418 {ECO:0000244|PDB:3UV9}.
STRAND 429 432 {ECO:0000244|PDB:3UV9}.
STRAND 440 447 {ECO:0000244|PDB:3UV9}.
TURN 448 451 {ECO:0000244|PDB:3UV9}.
STRAND 452 457 {ECO:0000244|PDB:3UV9}.
TURN 458 462 {ECO:0000244|PDB:3UV9}.
STRAND 463 468 {ECO:0000244|PDB:3UV9}.
STRAND 477 482 {ECO:0000244|PDB:3UV9}.
STRAND 490 492 {ECO:0000244|PDB:4B3N}.
SEQUENCE 497 AA; 57299 MW; 950166879B2E1A6F CRC64;
MASGILLNVK EEVTCPICLE LLTEPLSLHC GHSFCQACIT ANHKKSMLYK EGERSCPVCR
ISYQPENIQP NRHVANIVEK LREVKLSPEE GQKVDHCARH GEKLLLFCQE DSKVICWLCE
RSQEHRGHHT FLMEEVAQEY HVKLQTALEM LRQKQQEAEK LEADIREEKA SWKIQIDYDK
TNVSADFEQL REILDWEESN ELQNLEKEEE DILKSLTKSE TEMVQQTQYM RELISELEHR
LQGSMMDLLQ GVDGIIKRIE NMTLKKPKTF HKNQRRVFRA PDLKGMLDMF RELTDARRYW
VDVTLAPNNI SHAVIAEDKR QVSSRNPQIM YQAPGTLFTF PSLTNFNYCT GVLGSQSITS
GKHYWEVDVS KKSAWILGVC AGFQSDAMYN IEQNENYQPK YGYWVIGLQE GVKYSVFQDG
SSHTPFAPFI VPLSVIICPD RVGVFVDYEA CTVSFFNITN HGFLIYKFSQ CSFSKPVFPY
LNPRKCTVPM TLCSPSS


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