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DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1)

 DP13A_HUMAN             Reviewed;         709 AA.
Q9UKG1; Q9P2B9;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 151.
RecName: Full=DCC-interacting protein 13-alpha;
Short=Dip13-alpha;
AltName: Full=Adapter protein containing PH domain, PTB domain and leucine zipper motif 1;
Name=APPL1;
Synonyms=APPL {ECO:0000312|EMBL:AAH28599.1}, DIP13A,
KIAA1428 {ECO:0000312|EMBL:BAA92666.2};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF04012.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INTERACTION WITH AKT2 AND PIK3CA.
PubMed=10490823; DOI=10.1038/sj.onc.1203080;
Mitsuuchi Y., Johnson S.W., Sonoda G., Tanno S., Golemis E.A.,
Testa J.R.;
"Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an
adaptor molecule that interacts with the oncoprotein-serine/threonine
kinase AKT2.";
Oncogene 18:4891-4898(1999).
[2] {ECO:0000305, ECO:0000312|EMBL:AAL17835.1}
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH DCC.
PubMed=12011067; DOI=10.1074/jbc.M204679200;
Liu J., Yao F., Wu R., Morgan M., Thorburn A., Finley R.L. Jr.,
Chen Y.Q.;
"Mediation of the DCC apoptotic signal by DIP13 alpha.";
J. Biol. Chem. 277:26281-26285(2002).
[3] {ECO:0000312|EMBL:BAA92666.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000312|EMBL:BAA92666.2};
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5] {ECO:0000312|EMBL:AAH28599.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis {ECO:0000312|EMBL:AAH28599.1};
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] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB5A AND NURD/MECP1
COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15016378; DOI=10.1016/S0092-8674(04)00117-5;
Miaczynska M., Christoforidis S., Giner A., Shevchenko A.,
Uttenweiler-Joseph S., Habermann B., Wilm M., Parton R.G., Zerial M.;
"APPL proteins link Rab5 to nuclear signal transduction via an
endosomal compartment.";
Cell 116:445-456(2004).
[7]
INTERACTION WITH OCRL, F&H MOTIF, PHOSPHORYLATION AT SER-410, AND
MUTAGENESIS OF SER-410.
PubMed=17765681; DOI=10.1016/j.devcel.2007.08.004;
Erdmann K.S., Mao Y., McCrea H.J., Zoncu R., Lee S., Paradise S.,
Modregger J., Biemesderfer D., Toomre D., De Camilli P.;
"A role of the Lowe syndrome protein OCRL in early steps of the
endocytic pathway.";
Dev. Cell 13:377-390(2007).
[8]
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 THR-399, 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].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
INTERACTION WITH OCRL, AND SUBCELLULAR LOCATION.
PubMed=20133602; DOI=10.1073/pnas.0914658107;
Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
"Two closely related endocytic proteins that share a common OCRL-
binding motif with APPL1.";
Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, 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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
INTERACTION WITH OCRL.
PubMed=21233288; DOI=10.1091/mbc.E10-08-0730;
Noakes C.J., Lee G., Lowe M.;
"The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling
in the endocytic pathway.";
Mol. Biol. Cell 22:606-623(2011).
[15]
INTERACTION WITH OCRL, AND F&H MOTIF.
PubMed=21666675; DOI=10.1038/nsmb.2071;
Pirruccello M., Swan L.E., Folta-Stogniew E., De Camilli P.;
"Recognition of the F&H motif by the Lowe syndrome protein OCRL.";
Nat. Struct. Mol. Biol. 18:789-795(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
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).
[18]
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).
[19]
FUNCTION, INVOLVEMENT IN MODY14, VARIANT MODY14 ASN-94, AND
CHARACTERIZATION OF VARIANT MODY14 ASN-94.
PubMed=26073777; DOI=10.1016/j.ajhg.2015.05.011;
Prudente S., Jungtrakoon P., Marucci A., Ludovico O.,
Buranasupkajorn P., Mazza T., Hastings T., Milano T., Morini E.,
Mercuri L., Bailetti D., Mendonca C., Alberico F., Basile G.,
Romani M., Miccinilli E., Pizzuti A., Carella M., Barbetti F.,
Pascarella S., Marchetti P., Trischitta V., Di Paola R., Doria A.;
"Loss-of-function mutations in APPL1 in familial diabetes mellitus.";
Am. J. Hum. Genet. 97:177-185(2015).
[20]
VARIANT [LARGE SCALE ANALYSIS] GLN-643.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Adapter protein that interacts with proteins involved in
different cellular signaling pathways. Required for the regulation
of cell proliferation in response to extracellular signals from an
early endosomal compartment. Links Rab5 to nuclear signal
transduction. Involved in the regulation of the insulin receptor
signaling pathway. {ECO:0000269|PubMed:10490823,
ECO:0000269|PubMed:15016378, ECO:0000269|PubMed:26073777}.
-!- SUBUNIT: Binds RAB5A/Rab5 through an N-terminal domain. This
interaction is essential for its recruitment to endosomal
membranes as well as its role in cell proliferation. Binds DCC and
the catalytic domain of the inactive form of AKT2 through its PID
domain. Binds PIK3CA and subunits of the NuRD/MeCP1 complex.
Interacts with OCRL and INPP5B. Interacts with NTRK2 (By
similarity). {ECO:0000250|UniProtKB:Q8K3H0,
ECO:0000269|PubMed:10490823, ECO:0000269|PubMed:12011067,
ECO:0000269|PubMed:15016378, ECO:0000269|PubMed:17765681,
ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:21233288,
ECO:0000269|PubMed:21666675}.
-!- INTERACTION:
Self; NbExp=10; IntAct=EBI-741243, EBI-741243;
P35609:ACTN2; NbExp=2; IntAct=EBI-741243, EBI-77797;
Q96A54:ADIPOR1; NbExp=6; IntAct=EBI-741243, EBI-1632076;
Q91VH1:Adipor1 (xeno); NbExp=3; IntAct=EBI-741243, EBI-992398;
Q86V24:ADIPOR2; NbExp=3; IntAct=EBI-741243, EBI-1769445;
P31749:AKT1; NbExp=2; IntAct=EBI-741243, EBI-296087;
Q8NEU8:APPL2; NbExp=9; IntAct=EBI-741243, EBI-741261;
Q03001:DST; NbExp=3; IntAct=EBI-741243, EBI-310758;
O75923:DYSF; NbExp=2; IntAct=EBI-741243, EBI-2799016;
P00533:EGFR; NbExp=2; IntAct=EBI-741243, EBI-297353;
O95363:FARS2; NbExp=7; IntAct=EBI-741243, EBI-2513774;
Q13547:HDAC1; NbExp=2; IntAct=EBI-741243, EBI-301834;
O15379:HDAC3; NbExp=2; IntAct=EBI-741243, EBI-607682;
P43362:MAGEA9B; NbExp=3; IntAct=EBI-741243, EBI-10209139;
P50221:MEOX1; NbExp=3; IntAct=EBI-741243, EBI-2864512;
Q9UL25:RAB21; NbExp=10; IntAct=EBI-741243, EBI-1056039;
P20339:RAB5A; NbExp=17; IntAct=EBI-741243, EBI-399437;
Q8TAI7:RHEBL1; NbExp=3; IntAct=EBI-741243, EBI-746555;
Q9Y3I0:RTCB; NbExp=3; IntAct=EBI-741243, EBI-2107208;
Q8WXH0:SYNE2; NbExp=3; IntAct=EBI-741243, EBI-2372294;
Q12933:TRAF2; NbExp=2; IntAct=EBI-741243, EBI-355744;
Q9C0C9:UBE2O; NbExp=5; IntAct=EBI-741243, EBI-2339946;
-!- SUBCELLULAR LOCATION: Early endosome membrane
{ECO:0000269|PubMed:15016378, ECO:0000269|PubMed:20133602};
Peripheral membrane protein {ECO:0000269|PubMed:15016378}. Nucleus
{ECO:0000269|PubMed:15016378}. Note=Early endosomal membrane-bound
and nuclear. Translocated into the nucleus upon release from
endosomal membranes following internalization of EGF.
{ECO:0000269|PubMed:15016378}.
-!- TISSUE SPECIFICITY: High levels in heart, ovary, pancreas and
skeletal muscle. {ECO:0000269|PubMed:10490823}.
-!- DOMAIN: Overexpression of an N-terminal domain (residues 1-319) or
a C-terminal region (residues 273-709) has a proapoptotic effect.
{ECO:0000269|PubMed:15016378}.
-!- DOMAIN: The F&H motif, an approximately 12-13 amino-acid sequence
centered around Phe and His residues, is essential for binding to
OCRL and INPP5B. {ECO:0000269|PubMed:21666675}.
-!- PTM: Phosphorylation at Ser-410 by PKA severely impairs binding to
OCRL. {ECO:0000269|PubMed:17765681}.
-!- DISEASE: Maturity-onset diabetes of the young 14 (MODY14)
[MIM:616511]: A form of diabetes that is characterized by an
autosomal dominant mode of inheritance, onset in childhood or
early adulthood (usually before 25 years of age), a primary defect
in insulin secretion and frequent insulin-independence at the
beginning of the disease. {ECO:0000269|PubMed:26073777}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
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EMBL; AF169797; AAF04012.1; -; mRNA.
EMBL; AF424738; AAL17835.1; -; mRNA.
EMBL; AB037849; BAA92666.2; -; mRNA.
EMBL; BC028599; AAH28599.1; -; mRNA.
CCDS; CCDS2882.1; -.
RefSeq; NP_036228.1; NM_012096.2.
UniGene; Hs.476415; -.
PDB; 2EJ8; X-ray; 1.84 A; A/B=492-644.
PDB; 2ELA; X-ray; 2.00 A; A/B=493-646.
PDB; 2ELB; X-ray; 2.60 A; A=1-376.
PDB; 2Q12; X-ray; 1.79 A; A=5-265.
PDB; 2Q13; X-ray; 2.05 A; A=5-385.
PDB; 2Z0N; X-ray; 1.95 A; A=1-275.
PDB; 2Z0O; X-ray; 2.58 A; A=1-385.
PDB; 5C5B; X-ray; 2.90 A; A/C=5-375.
PDBsum; 2EJ8; -.
PDBsum; 2ELA; -.
PDBsum; 2ELB; -.
PDBsum; 2Q12; -.
PDBsum; 2Q13; -.
PDBsum; 2Z0N; -.
PDBsum; 2Z0O; -.
PDBsum; 5C5B; -.
ProteinModelPortal; Q9UKG1; -.
SMR; Q9UKG1; -.
BioGrid; 117522; 74.
CORUM; Q9UKG1; -.
DIP; DIP-29322N; -.
ELM; Q9UKG1; -.
IntAct; Q9UKG1; 85.
MINT; MINT-1177965; -.
STRING; 9606.ENSP00000288266; -.
iPTMnet; Q9UKG1; -.
PhosphoSitePlus; Q9UKG1; -.
BioMuta; APPL1; -.
DMDM; 61213025; -.
EPD; Q9UKG1; -.
MaxQB; Q9UKG1; -.
PaxDb; Q9UKG1; -.
PeptideAtlas; Q9UKG1; -.
PRIDE; Q9UKG1; -.
Ensembl; ENST00000288266; ENSP00000288266; ENSG00000157500.
GeneID; 26060; -.
KEGG; hsa:26060; -.
UCSC; uc003dio.4; human.
CTD; 26060; -.
DisGeNET; 26060; -.
EuPathDB; HostDB:ENSG00000157500.10; -.
GeneCards; APPL1; -.
HGNC; HGNC:24035; APPL1.
HPA; HPA011138; -.
HPA; HPA073477; -.
MalaCards; APPL1; -.
MIM; 604299; gene.
MIM; 616511; phenotype.
neXtProt; NX_Q9UKG1; -.
OpenTargets; ENSG00000157500; -.
PharmGKB; PA162376755; -.
eggNOG; KOG0521; Eukaryota.
eggNOG; KOG3536; Eukaryota.
eggNOG; ENOG410ZWZQ; LUCA.
GeneTree; ENSGT00710000106752; -.
HOGENOM; HOG000285988; -.
HOVERGEN; HBG051394; -.
InParanoid; Q9UKG1; -.
KO; K08733; -.
OMA; SDVETMQ; -.
OrthoDB; EOG091G08AV; -.
PhylomeDB; Q9UKG1; -.
TreeFam; TF328669; -.
Reactome; R-HSA-418889; Ligand-independent caspase activation via DCC.
SignaLink; Q9UKG1; -.
SIGNOR; Q9UKG1; -.
ChiTaRS; APPL1; human.
EvolutionaryTrace; Q9UKG1; -.
GeneWiki; APPL1; -.
GenomeRNAi; 26060; -.
PRO; PR:Q9UKG1; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000157500; -.
CleanEx; HS_APPL1; -.
ExpressionAtlas; Q9UKG1; baseline and differential.
Genevisible; Q9UKG1; HS.
GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0012506; C:vesicle membrane; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043422; F:protein kinase B binding; IPI:BHF-UCL.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; TAS:Reactome.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:UniProtKB.
GO; GO:0046324; P:regulation of glucose import; IMP:BHF-UCL.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR006020; PTB/PI_dom.
Pfam; PF00169; PH; 1.
Pfam; PF00640; PID; 1.
SMART; SM00233; PH; 1.
SMART; SM00462; PTB; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50729; SSF50729; 2.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS01179; PID; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Coiled coil; Complete proteome;
Diabetes mellitus; Disease mutation; Endosome; Membrane; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 709 DCC-interacting protein 13-alpha.
/FTId=PRO_0000079985.
DOMAIN 277 375 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 496 656 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
REGION 1 428 Required for RAB5A binding.
COILED 215 259 {ECO:0000255}.
COILED 621 673 {ECO:0000255}.
MOTIF 403 414 F&H.
MOD_RES 399 399 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 410 410 Phosphoserine; by PKA.
{ECO:0000269|PubMed:17765681}.
MOD_RES 693 693 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K3H0}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K3H0}.
VARIANT 94 94 D -> N (in MODY14; no effect on protein
abundance; loss of function in insulin
receptor signaling pathway;
dbSNP:rs796065047).
{ECO:0000269|PubMed:26073777}.
/FTId=VAR_075857.
VARIANT 108 108 A -> V (in dbSNP:rs4381906).
/FTId=VAR_050958.
VARIANT 643 643 E -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035909.
VARIANT 700 700 E -> G (in dbSNP:rs11544593).
/FTId=VAR_050959.
MUTAGEN 410 410 S->D: Decreased interaction with OCRL.
{ECO:0000269|PubMed:17765681}.
HELIX 9 11 {ECO:0000244|PDB:2Q13}.
TURN 12 14 {ECO:0000244|PDB:2Q13}.
HELIX 16 66 {ECO:0000244|PDB:2Q12}.
HELIX 67 70 {ECO:0000244|PDB:2Q12}.
HELIX 81 110 {ECO:0000244|PDB:2Q12}.
HELIX 112 120 {ECO:0000244|PDB:2Q12}.
HELIX 122 151 {ECO:0000244|PDB:2Q12}.
STRAND 152 154 {ECO:0000244|PDB:2Q13}.
HELIX 157 217 {ECO:0000244|PDB:2Q12}.
HELIX 220 257 {ECO:0000244|PDB:2Q12}.
HELIX 259 261 {ECO:0000244|PDB:2Q13}.
STRAND 262 265 {ECO:0000244|PDB:2Q13}.
TURN 268 270 {ECO:0000244|PDB:2Q13}.
STRAND 281 286 {ECO:0000244|PDB:2Q13}.
STRAND 298 305 {ECO:0000244|PDB:2Q13}.
STRAND 308 312 {ECO:0000244|PDB:2Q13}.
STRAND 320 324 {ECO:0000244|PDB:2Q13}.
STRAND 329 333 {ECO:0000244|PDB:2Q13}.
STRAND 339 345 {ECO:0000244|PDB:2Q13}.
STRAND 348 350 {ECO:0000244|PDB:2ELB}.
STRAND 354 356 {ECO:0000244|PDB:5C5B}.
HELIX 360 374 {ECO:0000244|PDB:2Q13}.
STRAND 499 512 {ECO:0000244|PDB:2EJ8}.
HELIX 519 534 {ECO:0000244|PDB:2EJ8}.
STRAND 542 555 {ECO:0000244|PDB:2EJ8}.
TURN 557 559 {ECO:0000244|PDB:2EJ8}.
STRAND 562 567 {ECO:0000244|PDB:2EJ8}.
HELIX 568 570 {ECO:0000244|PDB:2EJ8}.
STRAND 571 577 {ECO:0000244|PDB:2EJ8}.
STRAND 580 590 {ECO:0000244|PDB:2EJ8}.
STRAND 600 610 {ECO:0000244|PDB:2EJ8}.
HELIX 612 629 {ECO:0000244|PDB:2EJ8}.
HELIX 634 643 {ECO:0000244|PDB:2ELA}.
SEQUENCE 709 AA; 79663 MW; 4CABECFCF4BB110D CRC64;
MPGIDKLPIE ETLEDSPQTR SLLGVFEEDA TAISNYMNQL YQAMHRIYDA QNELSAATHL
TSKLLKEYEK QRFPLGGDDE VMSSTLQQFS KVIDELSSCH AVLSTQLADA MMFPITQFKE
RDLKEILTLK EVFQIASNDH DAAINRYSRL SKKRENDKVK YEVTEDVYTS RKKQHQTMMH
YFCALNTLQY KKKIALLEPL LGYMQAQISF FKMGSENLNE QLEEFLANIG TSVQNVRREM
DSDIETMQQT IEDLEVASDP LYVPDPDPTK FPVNRNLTRK AGYLNARNKT GLVSSTWDRQ
FYFTQGGNLM SQARGDVAGG LAMDIDNCSV MAVDCEDRRY CFQITSFDGK KSSILQAESK
KDHEEWICTI NNISKQIYLS ENPEETAARV NQSALEAVTP SPSFQQRHES LRPAAGQSRP
PTARTSSSGS LGSESTNLAA LSLDSLVAPD TPIQFDIISP VCEDQPGQAK AFGQGGRRTN
PFGESGGSTK SETEDSILHQ LFIVRFLGSM EVKSDDHPDV VYETMRQILA ARAIHNIFRM
TESHLLVTCD CLKLIDPQTQ VTRLTFPLPC VVLYATHQEN KRLFGFVLRT SSGRSESNLS
SVCYIFESNN EGEKICDSVG LAKQIALHAE LDRRASEKQK EIERVKEKQQ KELNKQKQIE
KDLEEQSRLI AASSRPNQAS SEGQFVVLSS SQSEESDLGE GGKKRESEA


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