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Peptidyl-prolyl cis-trans isomerase G (PPIase G) (Peptidyl-prolyl isomerase G) (EC 5.2.1.8) (CASP10) (Clk-associating RS-cyclophilin) (CARS-Cyp) (CARS-cyclophilin) (SR-cyclophilin) (SR-cyp) (SRcyp) (Cyclophilin G) (Rotamase G)

 PPIG_HUMAN              Reviewed;         754 AA.
Q13427; D3DPC5; D3DPC6; O00706; Q53R40; Q53SN4; Q96DG9;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
25-OCT-2017, entry version 161.
RecName: Full=Peptidyl-prolyl cis-trans isomerase G;
Short=PPIase G;
Short=Peptidyl-prolyl isomerase G;
EC=5.2.1.8;
AltName: Full=CASP10;
AltName: Full=Clk-associating RS-cyclophilin;
Short=CARS-Cyp;
Short=CARS-cyclophilin;
Short=SR-cyclophilin;
Short=SR-cyp;
Short=SRcyp;
AltName: Full=Cyclophilin G;
AltName: Full=Rotamase G;
Name=PPIG;
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 1), AND VARIANT ASP-699.
TISSUE=T-cell;
PubMed=8973360; DOI=10.1016/S0378-1119(96)00436-2;
Nestel F.P., Colwill K., Harper S., Pawson T., Anderson S.K.;
"RS cyclophilins: identification of an NK-TR1-related cyclophilin.";
Gene 180:151-155(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CLK1 AND RNA
POLYMERASE II, AND VARIANT ASP-699.
TISSUE=B-cell;
PubMed=9153302; DOI=10.1093/nar/25.11.2055;
Bourquin J.-P., Stagljar I., Meier P., Moosmann P., Silke J.,
Baechi T., Georgiev O., Schaffner W.;
"A serine/arginine-rich nuclear matrix cyclophilin interacts with the
C-terminal domain of RNA polymerase II.";
Nucleic Acids Res. 25:2055-2061(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[6]
INTERACTION WITH PNN, AND SUBCELLULAR LOCATION.
PubMed=15358154; DOI=10.1016/j.bbrc.2004.07.013;
Lin C.L., Leu S., Lu M.C., Ouyang P.;
"Over-expression of SR-cyclophilin, an interaction partner of nuclear
pinin, releases SR family splicing factors from nuclear speckles.";
Biochem. Biophys. Res. Commun. 321:638-647(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358 AND
SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-696, VARIANT
[LARGE SCALE ANALYSIS] ASP-699, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; SER-256; SER-257;
SER-259; SER-397 AND SER-687, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413; SER-415; SER-687;
SER-690; SER-696; THR-748 AND SER-753, VARIANT [LARGE SCALE ANALYSIS]
ASP-699, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358; SER-687;
SER-690 AND THR-748, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-358; SER-386;
SER-397; SER-687; SER-745 AND THR-748, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-744; SER-745
AND THR-748, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-392 AND LYS-693, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides. May be implicated in the folding, transport, and
assembly of proteins. May play an important role in the regulation
of pre-mRNA splicing.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ENZYME REGULATION: Cyclosporin A (CsA)-sensitive.
-!- SUBUNIT: Interacts with CLK1, PNN and with the phosphorylated C-
terminal domain of RNA polymerase II.
{ECO:0000269|PubMed:15358154, ECO:0000269|PubMed:9153302}.
-!- INTERACTION:
Q8N7W2-2:BEND7; NbExp=3; IntAct=EBI-396072, EBI-10181188;
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-396072, EBI-739624;
O75553:DAB1; NbExp=3; IntAct=EBI-396072, EBI-7875264;
Q9UI36-2:DACH1; NbExp=3; IntAct=EBI-396072, EBI-10186082;
Q96C98:FHL3; NbExp=3; IntAct=EBI-396072, EBI-10229248;
Q8NC69:KCTD6; NbExp=3; IntAct=EBI-396072, EBI-2511344;
P17931:LGALS3; NbExp=3; IntAct=EBI-396072, EBI-1170392;
Q6NVH9:LGALS3; NbExp=3; IntAct=EBI-396072, EBI-10187804;
Q15365:PCBP1; NbExp=2; IntAct=EBI-396072, EBI-946095;
Q9UL42:PNMA2; NbExp=3; IntAct=EBI-396072, EBI-302355;
Q96CD2:PPCDC; NbExp=3; IntAct=EBI-396072, EBI-724333;
Q14498:RBM39; NbExp=3; IntAct=EBI-396072, EBI-395290;
Q16637:SMN2; NbExp=4; IntAct=EBI-396072, EBI-395421;
Q12800:TFCP2; NbExp=3; IntAct=EBI-396072, EBI-717422;
Q9NVV9:THAP1; NbExp=3; IntAct=EBI-396072, EBI-741515;
-!- SUBCELLULAR LOCATION: Nucleus matrix
{ECO:0000269|PubMed:15358154}. Nucleus speckle
{ECO:0000269|PubMed:15358154}. Note=Colocalizes with RNA splicing
factors at nuclear speckles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13427-1; Sequence=Displayed;
Name=2;
IsoId=Q13427-2; Sequence=VSP_009662, VSP_009663;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The RS domain is required for the interaction with the
phosphorylated C-terminal domain of RNA polymerase II.
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EMBL; U40763; AAB40347.1; -; mRNA.
EMBL; X99717; CAA68053.1; -; mRNA.
EMBL; AC093899; AAY24119.1; -; Genomic_DNA.
EMBL; AC016772; AAY24233.1; -; Genomic_DNA.
EMBL; CH471058; EAX11267.1; -; Genomic_DNA.
EMBL; CH471058; EAX11268.1; -; Genomic_DNA.
EMBL; CH471058; EAX11269.1; -; Genomic_DNA.
EMBL; CH471058; EAX11270.1; -; Genomic_DNA.
EMBL; BC001555; AAH01555.1; -; mRNA.
CCDS; CCDS2235.1; -. [Q13427-1]
PIR; JC5314; JC5314.
RefSeq; NP_004783.2; NM_004792.2. [Q13427-1]
RefSeq; XP_005247023.1; XM_005246966.1. [Q13427-1]
RefSeq; XP_005247024.1; XM_005246967.1. [Q13427-1]
UniGene; Hs.470544; -.
UniGene; Hs.593163; -.
PDB; 2GW2; X-ray; 1.80 A; A=1-179.
PDB; 2WFI; X-ray; 0.75 A; A=1-177.
PDB; 2WFJ; X-ray; 0.75 A; A=1-177.
PDBsum; 2GW2; -.
PDBsum; 2WFI; -.
PDBsum; 2WFJ; -.
ProteinModelPortal; Q13427; -.
SMR; Q13427; -.
BioGrid; 114761; 49.
IntAct; Q13427; 32.
MINT; MINT-1684213; -.
STRING; 9606.ENSP00000260970; -.
BindingDB; Q13427; -.
ChEMBL; CHEMBL3707467; -.
DrugBank; DB00172; L-Proline.
iPTMnet; Q13427; -.
PhosphoSitePlus; Q13427; -.
BioMuta; PPIG; -.
DMDM; 229462749; -.
EPD; Q13427; -.
MaxQB; Q13427; -.
PaxDb; Q13427; -.
PeptideAtlas; Q13427; -.
PRIDE; Q13427; -.
Ensembl; ENST00000260970; ENSP00000260970; ENSG00000138398. [Q13427-1]
Ensembl; ENST00000448752; ENSP00000407083; ENSG00000138398. [Q13427-1]
Ensembl; ENST00000462903; ENSP00000435987; ENSG00000138398. [Q13427-2]
GeneID; 9360; -.
KEGG; hsa:9360; -.
UCSC; uc002uez.4; human. [Q13427-1]
CTD; 9360; -.
DisGeNET; 9360; -.
EuPathDB; HostDB:ENSG00000138398.15; -.
GeneCards; PPIG; -.
H-InvDB; HIX0029914; -.
HGNC; HGNC:14650; PPIG.
HPA; HPA021788; -.
HPA; HPA057469; -.
MIM; 606093; gene.
neXtProt; NX_Q13427; -.
OpenTargets; ENSG00000138398; -.
PharmGKB; PA33585; -.
eggNOG; KOG0546; Eukaryota.
eggNOG; COG0652; LUCA.
GeneTree; ENSGT00550000074595; -.
HOVERGEN; HBG048162; -.
InParanoid; Q13427; -.
KO; K09566; -.
OMA; PPHWKHA; -.
OrthoDB; EOG091G0BGL; -.
PhylomeDB; Q13427; -.
TreeFam; TF318563; -.
BRENDA; 5.2.1.8; 2681.
ChiTaRS; PPIG; human.
EvolutionaryTrace; Q13427; -.
GeneWiki; PPIG_(gene); -.
GenomeRNAi; 9360; -.
PRO; PR:Q13427; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138398; -.
CleanEx; HS_PPIG; -.
ExpressionAtlas; Q13427; baseline and differential.
Genevisible; Q13427; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:ProtInc.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0016018; F:cyclosporin A binding; TAS:ProtInc.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
Gene3D; 2.40.100.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom.
InterPro; IPR024936; Cyclophilin-type_PPIase.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
PANTHER; PTHR11071; PTHR11071; 5.
Pfam; PF00160; Pro_isomerase; 1.
PRINTS; PR00153; CSAPPISMRASE.
SUPFAM; SSF50891; SSF50891; 1.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Isomerase;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Rotamase; Ubl conjugation.
CHAIN 1 754 Peptidyl-prolyl cis-trans isomerase G.
/FTId=PRO_0000064150.
DOMAIN 11 176 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
COMPBIAS 180 192 Arg/Lys-rich (basic).
COMPBIAS 193 225 Asp/Glu/Ser-rich.
COMPBIAS 193 208 Poly-Ser.
COMPBIAS 226 253 Arg/Lys-rich (basic).
COMPBIAS 540 639 Arg/Ser-rich (RS domain).
COMPBIAS 621 626 Poly-Arg.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 358 358 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 386 386 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 687 687 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 690 690 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:20068231}.
MOD_RES 744 744 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 748 748 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 753 753 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CROSSLNK 392 392 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 693 693 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 340 357 RYRTPSRSRSRDRFRRSE -> VGDSFPRDLHNIAFVFLK
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009662.
VAR_SEQ 358 754 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009663.
VARIANT 445 445 D -> E (in dbSNP:rs1050354).
/FTId=VAR_055084.
VARIANT 699 699 N -> D (in dbSNP:rs8207).
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:8973360,
ECO:0000269|PubMed:9153302}.
/FTId=VAR_055085.
STRAND 9 16 {ECO:0000244|PDB:2WFI}.
STRAND 19 28 {ECO:0000244|PDB:2WFI}.
TURN 30 32 {ECO:0000244|PDB:2WFI}.
HELIX 34 45 {ECO:0000244|PDB:2WFI}.
TURN 46 48 {ECO:0000244|PDB:2WFJ}.
TURN 52 54 {ECO:0000244|PDB:2WFI}.
STRAND 56 58 {ECO:0000244|PDB:2WFI}.
STRAND 64 69 {ECO:0000244|PDB:2WFI}.
TURN 70 72 {ECO:0000244|PDB:2WFI}.
STRAND 73 76 {ECO:0000244|PDB:2WFI}.
TURN 79 81 {ECO:0000244|PDB:2WFI}.
STRAND 82 85 {ECO:0000244|PDB:2WFI}.
STRAND 109 112 {ECO:0000244|PDB:2WFI}.
STRAND 114 116 {ECO:0000244|PDB:2WFJ}.
STRAND 124 129 {ECO:0000244|PDB:2WFI}.
HELIX 132 134 {ECO:0000244|PDB:2WFI}.
TURN 135 137 {ECO:0000244|PDB:2WFI}.
STRAND 140 146 {ECO:0000244|PDB:2WFI}.
HELIX 148 155 {ECO:0000244|PDB:2WFI}.
STRAND 165 167 {ECO:0000244|PDB:2WFI}.
STRAND 169 176 {ECO:0000244|PDB:2WFI}.
SEQUENCE 754 AA; 88617 MW; D4884808D8060CD6 CRC64;
MGIKVQRPRC FFDIAINNQP AGRVVFELFS DVCPKTCENF RCLCTGEKGT GKSTQKPLHY
KSCLFHRVVK DFMVQGGDFS EGNGRGGESI YGGFFEDESF AVKHNKEFLL SMANRGKDTN
GSQFFITTKP TPHLDGHHVV FGQVISGQEV VREIENQKTD AASKPFAEVR ILSCGELIPK
SKVKKEEKKR HKSSSSSSSS SSDSDSSSDS QSSSDSSDSE SATEEKSKKR KKKHRKNSRK
HKKEKKKRKK SKKSASSESE AENLEAQPQS TVRPEEIPPI PENRFLMRKS PPKADEKERK
NREREREREC NPPNSQPASY QRRLLVTRSG RKIKGRGPRR YRTPSRSRSR DRFRRSETPP
HWRQEMQRAQ RMRVSSGERW IKGDKSELNE IKENQRSPVR VKERKITDHR NVSESPNRKN
EKEKKVKDHK SNSKERDIRR NSEKDDKYKN KVKKRAKSKS RSKSKEKSKS KERDSKHNRN
EEKRMRSRSK GRDHENVKEK EKQSDSKGKD QERSRSKEKS KQLESKSNEH DHSKSKEKDR
RAQSRSRECD ITKGKHSYNS RTRERSRSRD RSRRVRSRTH DRDRSRSKEY HRYREQEYRR
RGRSRSRERR TPPGRSRSKD RRRRRRDSRS SEREESQSRN KDKYRNQESK SSHRKENSES
EKRMYSKSRD HNSSNNSREK KADRDQSPFS KIKQSSQDNE LKSSMLKNKE DEKIRSSVEK
ENQKSKGQEN DHVHEKNKKF DHESSPGTDE DKSG


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