CD2AP_MOUSE
ID CD2AP_MOUSE Reviewed; 637 AA.
AC Q9JLQ0; E9QL86; O88903; Q8K4Z1; Q8VCI9;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=CD2-associated protein;
DE AltName: Full=Mesenchyme-to-epithelium transition protein with SH3 domains 1;
DE Short=METS-1;
GN Name=Cd2ap; Synonyms=Mets1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CD2.
RX PubMed=9741631; DOI=10.1016/s0092-8674(00)81608-6;
RA Dustin M.L., Olszowy M.W., Holdorf A.D., Li J., Bromley S., Desai N.,
RA Widder P., Rosenberger F., van der Merwe P.A., Allen P.M., Shaw A.S.;
RT "A novel adaptor protein orchestrates receptor patterning and cytoskeletal
RT polarity in T-cell contacts.";
RL Cell 94:667-677(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PKD2.
RX PubMed=10913159; DOI=10.1074/jbc.m006624200;
RA Lehtonen S., Ora A., Olkkonen V.M., Geng L., Zerial M., Somlo S.,
RA Lehtonen E.;
RT "In vivo interaction of the adapter protein CD2-associated protein with the
RT type 2 polycystic kidney disease protein, polycystin-2.";
RL J. Biol. Chem. 275:32888-32893(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Meton I., Le Marchand-Brustel Y., Cormont M.;
RT "Role of the interaction between CD2AP and c-Cbl.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-637.
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPHS1, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10514378; DOI=10.1126/science.286.5438.312;
RA Shih N.Y., Li J., Karpitskii V., Nguyen A., Dustin M.L., Kanagawa O.,
RA Miner J.H., Shaw A.S.;
RT "Congenital nephrotic syndrome in mice lacking CD2-associated protein.";
RL Science 286:312-315(1999).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NPHS1.
RX PubMed=11733379; DOI=10.1016/s0002-9440(10)63080-5;
RA Shih N.Y., Li J., Cotran R., Mundel P., Miner J.H., Shaw A.S.;
RT "CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-
RT terminal domain.";
RL Am. J. Pathol. 159:2303-2308(2001).
RN [8]
RP INTERACTION WITH NPHS1 AND NPHS2.
RX PubMed=11733557; DOI=10.1172/jci200112849;
RA Schwarz K., Simons M., Reiser J., Saleem M.A., Faul C., Kriz W., Shaw A.S.,
RA Holzman L.B., Mundel P.;
RT "Podocin, a raft-associated component of the glomerular slit diaphragm,
RT interacts with CD2AP and nephrin.";
RL J. Clin. Invest. 108:1621-1629(2001).
RN [9]
RP INTERACTION WITH F-ACTIN.
RX PubMed=12217865; DOI=10.1152/ajprenal.00312.2001;
RA Lehtonen S., Zhao F., Lehtonen E.;
RT "CD2-associated protein directly interacts with the actin cytoskeleton.";
RL Am. J. Physiol. 283:F734-F743(2002).
RN [10]
RP INTERACTION WITH WTIP.
RX PubMed=14736876; DOI=10.1074/jbc.m314155200;
RA Srichai M.B., Konieczkowski M., Padiyar A., Konieczkowski D.J.,
RA Mukherjee A., Hayden P.S., Kamat S., El-Meanawy M.A., Khan S., Mundel P.,
RA Lee S.B., Bruggeman L.A., Schelling J.R., Sedor J.R.;
RT "A WT1 co-regulator controls podocyte phenotype by shuttling between
RT adhesion structures and nucleus.";
RL J. Biol. Chem. 279:14398-14408(2004).
RN [11]
RP INTERACTION WITH DDN.
RX PubMed=17537921; DOI=10.1073/pnas.0700917104;
RA Asanuma K., Campbell K.N., Kim K., Faul C., Mundel P.;
RT "Nuclear relocation of the nephrin and CD2AP-binding protein dendrin
RT promotes apoptosis of podocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10134-10139(2007).
RN [12]
RP INTERACTION WITH RET, AND TISSUE SPECIFICITY.
RX PubMed=18753381; DOI=10.1523/jneurosci.2738-08.2008;
RA Tsui C.C., Pierchala B.A.;
RT "CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the regulation
RT of ret signal transduction.";
RL J. Neurosci. 28:8789-8800(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-458; SER-510 AND
RP SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP STRUCTURE BY NMR OF 270-329.
RX PubMed=17922258; DOI=10.1007/s10858-007-9201-7;
RA Ortega Roldan J.L., Romero Romero M.L., Ora A., Ab E., Lopez Mayorga O.,
RA Azuaga A.I., van Nuland N.A.;
RT "The high resolution NMR structure of the third SH3 domain of CD2AP.";
RL J. Biomol. NMR 39:331-336(2007).
CC -!- FUNCTION: Seems to act as an adapter protein between membrane proteins
CC and the actin cytoskeleton (By similarity). In collaboration with CBLC,
CC modulates the rate of RET turnover and may act as regulatory checkpoint
CC that limits the potency of GDNF on neuronal survival. Controls CBLC
CC function, converting it from an inhibitor to a promoter of RET
CC degradation (By similarity). May play a role in receptor clustering and
CC cytoskeletal polarity in the junction between T-cell and antigen-
CC presenting cell (PubMed:9741631). May anchor the podocyte slit
CC diaphragm to the actin cytoskeleton in renal glomerolus
CC (PubMed:10514378). Also required for cytokinesis. Plays a role in
CC epithelial cell junctions formation (By similarity).
CC {ECO:0000250|UniProtKB:F1LRS8, ECO:0000250|UniProtKB:Q9Y5K6,
CC ECO:0000269|PubMed:10514378, ECO:0000269|PubMed:9741631}.
CC -!- SUBUNIT: Homodimer. Interacts with F-actin, PKD2, NPHS1 and NPHS2.
CC Interacts with WTIP. Interacts with DDN; interaction is direct.
CC Interacts (via SH3 2 domain) with CBL (via phosphorylated C-terminus).
CC Interacts with BCAR1/p130Cas (via SH3 domain). Interacts with MVB12A
CC and ARHGAP17. Interacts with ANLN, CD2 and CBLB. Interacts with PDCD6IP
CC and TSG101. Interacts with RIN3. Interacts directly with RET (inactive)
CC and CBLC; upon RET activation by GDNF suggested to dissociate from RET
CC as CBLC:CD2AP complex. Interacts with CGNL1 and SH3BP1; probably part
CC of a complex at cell junctions. Interacts with CAPZA1.
CC {ECO:0000250|UniProtKB:Q9Y5K6, ECO:0000269|PubMed:10514378,
CC ECO:0000269|PubMed:10913159, ECO:0000269|PubMed:11733379,
CC ECO:0000269|PubMed:11733557, ECO:0000269|PubMed:12217865,
CC ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:17537921,
CC ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:9741631, ECO:0000305}.
CC -!- INTERACTION:
CC Q9JLQ0; P22682: Cbl; NbExp=5; IntAct=EBI-644807, EBI-640919;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9Y5K6}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q9Y5K6}. Cell junction
CC {ECO:0000250|UniProtKB:Q9Y5K6}. Note=Colocalizes with F-actin and
CC BCAR1/p130Cas in membrane ruffles (By similarity). Located at podocyte
CC slit diaphragm between podocyte foot processes (PubMed:10514378,
CC PubMed:11733379). During late anaphase and telophase, concentrates in
CC the vicinity of the midzone microtubules and in the midbody in late
CC telophase (By similarity). {ECO:0000250|UniProtKB:Q9Y5K6,
CC ECO:0000269|PubMed:10514378, ECO:0000269|PubMed:11733379}.
CC -!- TISSUE SPECIFICITY: Expressed in podocytes (at protein level).
CC {ECO:0000269|PubMed:18753381}.
CC -!- DOMAIN: Potential homodimerization is mediated by the coiled coil
CC domain. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues; probably by c-Abl, Fyn and c-
CC Src. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Death at 6 to 7 weeks of age from renal failure.
CC Mice show defects in epithelial foot processes, accompanied by
CC mesangial cell hyperplasia and extracellular matrix deposition.
CC {ECO:0000269|PubMed:10514378}.
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DR EMBL; AF077003; AAC36099.1; -; mRNA.
DR EMBL; AF149092; AAF73150.1; -; mRNA.
DR EMBL; AJ459109; CAD30510.1; -; mRNA.
DR EMBL; AC111082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019744; AAH19744.1; -; mRNA.
DR CCDS; CCDS50114.1; -.
DR RefSeq; NP_033977.3; NM_009847.3.
DR PDB; 2JTE; NMR; -; A=270-329.
DR PDB; 2KRM; NMR; -; A=2-58.
DR PDB; 2KRN; NMR; -; A=111-166.
DR PDB; 2KRO; NMR; -; A=270-329.
DR PDB; 2LZ6; NMR; -; B=270-329.
DR PDB; 2MCN; NMR; -; A=2-62.
DR PDBsum; 2JTE; -.
DR PDBsum; 2KRM; -.
DR PDBsum; 2KRN; -.
DR PDBsum; 2KRO; -.
DR PDBsum; 2LZ6; -.
DR PDBsum; 2MCN; -.
DR AlphaFoldDB; Q9JLQ0; -.
DR SMR; Q9JLQ0; -.
DR BioGRID; 198584; 92.
DR CORUM; Q9JLQ0; -.
DR IntAct; Q9JLQ0; 80.
DR MINT; Q9JLQ0; -.
DR STRING; 10090.ENSMUSP00000024709; -.
DR iPTMnet; Q9JLQ0; -.
DR PhosphoSitePlus; Q9JLQ0; -.
DR CPTAC; non-CPTAC-3968; -.
DR EPD; Q9JLQ0; -.
DR jPOST; Q9JLQ0; -.
DR MaxQB; Q9JLQ0; -.
DR PaxDb; Q9JLQ0; -.
DR PeptideAtlas; Q9JLQ0; -.
DR PRIDE; Q9JLQ0; -.
DR ProteomicsDB; 281264; -.
DR Antibodypedia; 1016; 190 antibodies from 33 providers.
DR Ensembl; ENSMUST00000024709; ENSMUSP00000024709; ENSMUSG00000061665.
DR GeneID; 12488; -.
DR KEGG; mmu:12488; -.
DR UCSC; uc008cot.1; mouse.
DR CTD; 23607; -.
DR MGI; MGI:1330281; Cd2ap.
DR VEuPathDB; HostDB:ENSMUSG00000061665; -.
DR eggNOG; KOG4348; Eukaryota.
DR GeneTree; ENSGT00940000157566; -.
DR HOGENOM; CLU_024255_2_0_1; -.
DR InParanoid; Q9JLQ0; -.
DR OMA; RSPGTIY; -.
DR OrthoDB; 1577081at2759; -.
DR PhylomeDB; Q9JLQ0; -.
DR TreeFam; TF350191; -.
DR BioGRID-ORCS; 12488; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Cd2ap; mouse.
DR EvolutionaryTrace; Q9JLQ0; -.
DR PRO; PR:Q9JLQ0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9JLQ0; protein.
DR Bgee; ENSMUSG00000061665; Expressed in metanephric cortical collecting duct and 273 other tissues.
DR ExpressionAtlas; Q9JLQ0; baseline and differential.
DR Genevisible; Q9JLQ0; MM.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:ARUK-UCL.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0005172; F:vascular endothelial growth factor receptor binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
DR GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; IGI:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IGI:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IGI:MGI.
DR GO; GO:0048259; P:regulation of receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0032905; P:transforming growth factor beta1 production; IGI:MGI.
DR GO; GO:0016050; P:vesicle organization; ISO:MGI.
DR CDD; cd12053; SH3_CD2AP_1; 1.
DR CDD; cd12054; SH3_CD2AP_2; 1.
DR CDD; cd12056; SH3_CD2AP_3; 1.
DR InterPro; IPR028445; CD2AP.
DR InterPro; IPR035775; CD2AP_SH3_1.
DR InterPro; IPR035777; CD2AP_SH3_3.
DR InterPro; IPR035776; CD2AP_SH_2.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167:SF23; PTHR14167:SF23; 2.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 2.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell junction; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Mitosis;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; SH3-binding;
KW Ubl conjugation.
FT CHAIN 1..637
FT /note="CD2-associated protein"
FT /id="PRO_0000089436"
FT DOMAIN 1..59
FT /note="SH3 1; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 108..167
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 269..330
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..175
FT /note="Interaction with ANLN and localization to the
FT midbody"
FT /evidence="ECO:0000250"
FT REGION 166..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 578..636
FT /evidence="ECO:0000255"
FT MOTIF 336..352
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 378..397
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 410..422
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 358..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5K6"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5K6"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1LRS8"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 563
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5K6"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5K6"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5K6"
FT CROSSLNK 523
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5K6"
FT CONFLICT 78
FT /note="V -> E (in Ref. 2; AAF73150)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="Missing (in Ref. 1; AAC36099)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="K -> Q (in Ref. 1; AAC36099)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="P -> R (in Ref. 1; AAC36099)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..297
FT /note="IIH -> LS (in Ref. 1; AAC36099)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="P -> PTAPTKA (in Ref. 1; AAC36099)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="S -> P (in Ref. 2; AAF73150, 3; CAD30510 and 5;
FT AAH19744)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="R -> K (in Ref. 2; AAF73150, 3; CAD30510 and 5;
FT AAH19744)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:2KRM"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2MCN"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2KRM"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:2KRM"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2KRM"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2KRM"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2KRM"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2KRM"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2KRN"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:2KRN"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:2KRN"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:2KRN"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2KRN"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:2JTE"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:2JTE"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:2JTE"
FT STRAND 303..313
FT /evidence="ECO:0007829|PDB:2JTE"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:2JTE"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2JTE"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:2JTE"
SQ SEQUENCE 637 AA; 70450 MW; 0B618FE82AF12332 CRC64;
MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP DNFVKEIKRE
TEPKDDNLPI KRERQGNVAS LVQRISTYGL PAGGIQPHPQ TKAIKKKTKK RQCKVLFDYS
PQNEDELELI VGDVIDVIEE VEEGWWSGTL NNKLGLFPSN FVKELESTED GETHNAQEES
EVPLTGPTSP LPSPGNGSEP APGSVAQPKK IRGIGFGDIF KEGSVKLRTR TSSSETEEKK
TEKPLILQPL GSRTQNVEVT KPDVDGKIKA KEYCRTLFPY TGTNEDELTF REGEIIHLIS
KETGEAGWWK GELNGKEGVF PDNFAVQISE LDKDFPKPKK PPPPAKGPAP KPDLSAAEKK
AFPLKAEEKD EKSLLEQKPS KPAAPQVPPK KPTAPTKASN LLRSPGAVYP KRPEKPVPPP
PPAAKINGEV SIISSKIDTE PVSKPKLDPE QLPVRPKSVD LDAFVARNSK ETDDVNFDDI
ASSENLLHLT ANRPKMPGRR LPGRFNGGHS PTQSPEKTLK LPKEDDSGNL KPLEFKKDAS
YSSKSSLSTP SSASKVNTAA FLTPLELKAK AEADDGKRNS VDELRAQIIE LLCIVDALKK
DHGKELEKLR KELEEEKAMR SNLEVEIAKL KKAVLLS
