SKAP2_MOUSE
ID SKAP2_MOUSE Reviewed; 358 AA.
AC Q3UND0; Q8BK74; Q9Z2K4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Src kinase-associated phosphoprotein 2;
DE AltName: Full=Pyk2/RAFTK-associated protein;
DE AltName: Full=SKAP55 homolog;
DE Short=SKAP-HOM;
DE AltName: Full=Src family-associated phosphoprotein 2;
DE AltName: Full=Src kinase-associated phosphoprotein 55-related protein;
DE AltName: Full=Src-associated adapter protein with PH and SH3 domains;
GN Name=Skap2; Synonyms=Prap, Ra70, Saps, Scap2, Skap55r;
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] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INDUCTION, POSSIBLE INTERACTION WITH FYN; HCK AND LYN,
RP PHOSPHORYLATION AT TYR-260, MUTAGENESIS OF TYR-260, AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=11063873; DOI=10.1016/s0301-472x(00)00537-3;
RA Curtis D.J., Jane S.M., Hilton D.J., Dougherty L., Bodine D.M.,
RA Begley C.G.;
RT "Adaptor protein SKAP55R is associated with myeloid differentiation and
RT growth arrest.";
RL Exp. Hematol. 28:1250-1259(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Lee J.-S., Suh K.S., Burr J.G.;
RT "Mouse Saps, Src-associated adaptor protein with PH and SH3 domain.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Momoi T., Urase K., Mukasa T., Fujita E., Kouroku Y., Miho Y., Soyama A.,
RA Momoi M.Y.;
RT "RA70, retinoic acid responsive gene, is expressed specifically in
RT spermatocyte in mouse testis.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lymph node;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 PROTEIN SEQUENCE OF 1-12.
RC TISSUE=T-cell;
RX PubMed=9755858; DOI=10.1016/s0014-5793(98)01040-0;
RA Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.;
RT "SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein
RT SKAP55.";
RL FEBS Lett. 435:55-60(1998).
RN [7]
RP PROTEIN SEQUENCE OF 93-114; 129-139 AND 147-158, PHOSPHORYLATION,
RP INTERACTION WITH FYB1, IDENTIFICATION IN A COMPLEX WITH FYB1 AND PTPNS1,
RP AND IDENTIFICATION IN A COMPLEX WITH FYB1 AND LILRB3.
RX PubMed=11207596; DOI=10.1046/j.1462-5822.2000.00061.x;
RA Black D.S., Marie-Cardine A., Schraven B., Bliska J.B.;
RT "The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated
RT signalling complex in macrophages.";
RL Cell. Microbiol. 2:401-414(2000).
RN [8]
RP INTERACTION WITH PTPNS1, AND IDENTIFICATION IN A COMPLEX WITH FYB1 AND
RP PTPNS1.
RX PubMed=10469599; DOI=10.1016/s0960-9822(99)80401-1;
RA Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E.,
RA Schraven B., Neel B.G.;
RT "SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-
RT protein complexes in macrophages.";
RL Curr. Biol. 9:927-930(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12893833; DOI=10.1074/jbc.m213217200;
RA Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H., Avraham H.,
RA Avraham S., Yasuda M., Matsumoto M.;
RT "Identification and characterization of a novel Pyk2/related adhesion focal
RT tyrosine kinase-associated protein that inhibits alpha-synuclein
RT phosphorylation.";
RL J. Biol. Chem. 278:42225-42233(2003).
RN [10]
RP TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH ACTIN, AND FUNCTION.
RX PubMed=15894167; DOI=10.1016/j.cellsig.2004.11.009;
RA Bourette R.P., Therier J., Mouchiroud G.;
RT "Macrophage colony-stimulating factor receptor induces tyrosine
RT phosphorylation of SKAP55R adaptor and its association with actin.";
RL Cell. Signal. 17:941-949(2005).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16135797; DOI=10.1128/mcb.25.18.8052-8063.2005;
RA Togni M., Swanson K.D., Reimann S., Kliche S., Pearce A.C., Simeoni L.,
RA Reinhold D., Wienands J., Neel B.G., Schraven B., Gerber A.;
RT "Regulation of in vitro and in vivo immune functions by the cytosolic
RT adaptor protein SKAP-HOM.";
RL Mol. Cell. Biol. 25:8052-8063(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75 AND TYR-260, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP INTERACTION WITH FYB1.
RX PubMed=17003372; DOI=10.1182/blood-2006-05-022301;
RA Kasirer-Friede A., Moran B., Nagrampa-Orje J., Swanson K., Ruggeri Z.M.,
RA Schraven B., Neel B.G., Koretzky G., Shattil S.J.;
RT "ADAP is required for normal alphaIIb-beta3 activation by VWF/GP Ib-IX-V
RT and other agonists.";
RL Blood 109:1018-1025(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75; TYR-151 AND TYR-260, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-222, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19026786; DOI=10.1016/j.molcel.2008.09.022;
RA Swanson K.D., Tang Y., Ceccarelli D.F., Poy F., Sliwa J.P., Neel B.G.,
RA Eck M.J.;
RT "The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-
RT gated molecular switch.";
RL Mol. Cell 32:564-575(2008).
CC -!- FUNCTION: May be involved in B-cell and macrophage adhesion processes.
CC In B-cells, may act by coupling the B-cell receptor (BCR) to integrin
CC activation. May play a role in src signaling pathway.
CC {ECO:0000269|PubMed:11063873, ECO:0000269|PubMed:15894167,
CC ECO:0000269|PubMed:16135797}.
CC -!- SUBUNIT: Interacts with LAT, GRB2, PTK2B and PRAM1 (By similarity).
CC Homodimer. Interacts with FYB1, which is required for SKAP2 protein
CC stability. Interacts with PTPNS1. Part of a complex consisting of
CC SKAP2, FYB1 and PTPNS1. Part of a complex consisting of SKAP2, FYB1 and
CC LILRB3. May interact with actin. May interact with FYN, HCK and LYN.
CC Interacts with FASLG (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q3UND0; Q9Y2R2: PTPN22; Xeno; NbExp=2; IntAct=EBI-642769, EBI-1211241;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11063873,
CC ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:19026786}.
CC Note=Membrane ruffles of macrophages. Perikarya and dendrites from
CC neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UND0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UND0-2; Sequence=VSP_022184;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, lung, liver, spleen, bone
CC marrow and testis. Present in T-cells, B-cells, and all cells of the
CC myelomonocytic lineage. Present in all brain regions, with highest
CC levels in neurons from the Purkinje cell layer, hippocampal gyrus,
CC cortex and substantia nigra (at protein level).
CC {ECO:0000269|PubMed:11063873, ECO:0000269|PubMed:12893833,
CC ECO:0000269|PubMed:15894167, ECO:0000269|PubMed:16135797}.
CC -!- INDUCTION: By IL-6 in myeloid cells. {ECO:0000269|PubMed:11063873}.
CC -!- DOMAIN: The SH3 domain interacts with FYB1 and PTK2B. {ECO:0000250}.
CC -!- PTM: Dephosphorylated on Tyr-75 by PTPN22 (By similarity).
CC Phosphorylated by FYN on Tyr-260. In case of infection with
CC Y.pseudotuberculosis, dephosphorylated by bacterial phosphatase yopH.
CC {ECO:0000250, ECO:0000269|PubMed:11063873, ECO:0000269|PubMed:11207596,
CC ECO:0000269|PubMed:15894167}.
CC -!- DISRUPTION PHENOTYPE: Mice are healthy and do not display any obvious
CC abnormality. They have normal T-cell, platelet and macrophage function,
CC but show reduced levels of spontaneous immunoglobulins in the serum,
CC and defects in B-cell proliferation. {ECO:0000269|PubMed:16135797}.
CC -!- SIMILARITY: Belongs to the SKAP family. {ECO:0000305}.
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DR EMBL; AF051324; AAC99297.1; -; mRNA.
DR EMBL; AB014485; BAA77253.1; -; mRNA.
DR EMBL; AK076000; BAC36111.1; -; mRNA.
DR EMBL; AK144289; BAE25817.1; -; mRNA.
DR EMBL; BC003711; AAH03711.1; -; mRNA.
DR CCDS; CCDS20137.1; -. [Q3UND0-1]
DR RefSeq; NP_061243.1; NM_018773.2. [Q3UND0-1]
DR PDB; 1M0V; NMR; -; B=73-79.
DR PDB; 1U5E; X-ray; 2.60 A; A/B=14-222.
DR PDB; 1U5F; X-ray; 1.90 A; A=111-248.
DR PDB; 1U5G; X-ray; 2.10 A; A/B/C/D=103-222.
DR PDB; 2OTX; X-ray; 2.60 A; A/B=12-222.
DR PDBsum; 1M0V; -.
DR PDBsum; 1U5E; -.
DR PDBsum; 1U5F; -.
DR PDBsum; 1U5G; -.
DR PDBsum; 2OTX; -.
DR AlphaFoldDB; Q3UND0; -.
DR SMR; Q3UND0; -.
DR BioGRID; 207619; 1.
DR CORUM; Q3UND0; -.
DR IntAct; Q3UND0; 3.
DR MINT; Q3UND0; -.
DR STRING; 10090.ENSMUSP00000077342; -.
DR iPTMnet; Q3UND0; -.
DR PhosphoSitePlus; Q3UND0; -.
DR EPD; Q3UND0; -.
DR jPOST; Q3UND0; -.
DR MaxQB; Q3UND0; -.
DR PaxDb; Q3UND0; -.
DR PeptideAtlas; Q3UND0; -.
DR PRIDE; Q3UND0; -.
DR ProteomicsDB; 261181; -. [Q3UND0-1]
DR ProteomicsDB; 261182; -. [Q3UND0-2]
DR Antibodypedia; 25901; 233 antibodies from 33 providers.
DR DNASU; 54353; -.
DR Ensembl; ENSMUST00000078214; ENSMUSP00000077342; ENSMUSG00000059182. [Q3UND0-2]
DR Ensembl; ENSMUST00000204778; ENSMUSP00000145462; ENSMUSG00000059182. [Q3UND0-1]
DR GeneID; 54353; -.
DR KEGG; mmu:54353; -.
DR UCSC; uc009bxv.1; mouse. [Q3UND0-1]
DR UCSC; uc009bxw.1; mouse. [Q3UND0-2]
DR CTD; 8935; -.
DR MGI; MGI:1889206; Skap2.
DR VEuPathDB; HostDB:ENSMUSG00000059182; -.
DR eggNOG; ENOG502QVFD; Eukaryota.
DR GeneTree; ENSGT00390000017856; -.
DR HOGENOM; CLU_062032_0_0_1; -.
DR InParanoid; Q3UND0; -.
DR OMA; KQGFPQD; -.
DR OrthoDB; 767446at2759; -.
DR PhylomeDB; Q3UND0; -.
DR TreeFam; TF331055; -.
DR Reactome; R-MMU-391160; Signal regulatory protein family interactions.
DR BioGRID-ORCS; 54353; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Skap2; mouse.
DR EvolutionaryTrace; Q3UND0; -.
DR PRO; PR:Q3UND0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3UND0; protein.
DR Bgee; ENSMUSG00000059182; Expressed in animal zygote and 258 other tissues.
DR ExpressionAtlas; Q3UND0; baseline and differential.
DR Genevisible; Q3UND0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR DisProt; DP02892; -.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR037781; SKAP_fam.
DR PANTHER; PTHR15129; PTHR15129; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00233; PH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; B-cell activation; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..358
FT /note="Src kinase-associated phosphoprotein 2"
FT /id="PRO_0000270180"
FT DOMAIN 116..219
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 296..357
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 14..64
FT /note="Homodimerization"
FT REGION 232..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75563"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 75
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:17947660"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 197
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75563"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 260
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000269|PubMed:11063873,
FT ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:17947660"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT VAR_SEQ 22..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022184"
FT MUTAGEN 260
FT /note="Y->F: Abolishes interaction with FYN,
FT phosphorylation by FYN, and effects on cell growth."
FT /evidence="ECO:0000269|PubMed:11063873"
FT CONFLICT 16
FT /note="E -> K (in Ref. 4; BAE25817)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="N -> P (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:1U5E"
FT TURN 30..34
FT /evidence="ECO:0007829|PDB:1U5E"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:1U5E"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1U5E"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1U5E"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1U5F"
FT STRAND 115..126
FT /evidence="ECO:0007829|PDB:1U5F"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1U5G"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1U5E"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:1U5F"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1U5F"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1U5F"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1U5F"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1U5E"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1U5F"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1U5F"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1U5E"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1U5F"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:1U5F"
SQ SEQUENCE 358 AA; 40712 MW; B66973A656E44E05 CRC64;
MPNPSCTSSP GPLPEEIRNL LADVETFVAD TLKGENLSKK AKEKRESLIK KIKDVKSVYL
QEFQDKGDAE DGDEYDDPFA GPADTISLAS ERYDKDDDGP SDGNQFPPIA AQDLPFVIKA
GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIDGYD VRMNNTLRKD
GKKDCCFEIC APDKRIYQFT AASPKDAEEW VQQLKFILQD LGSDVIPEDD EERGELYDDV
DHPAAVSSPQ RSQPIDDEIY EELPEEEEDT ASVKMDEQGK GSRDSVHHTS GDKSTDYANF
YQGLWDCTGA LSDELSFKRG DVIYILSKEY NRYGWWVGEM KGAIGLVPKA YLMEMYDI
