BCAP_HUMAN
ID BCAP_HUMAN Reviewed; 805 AA.
AC Q6ZUJ8; Q5TB56; Q5VXJ9; Q8N6J6; Q8NAC8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Phosphoinositide 3-kinase adapter protein 1;
DE AltName: Full=B-cell adapter for phosphoinositide 3-kinase;
DE AltName: Full=B-cell phosphoinositide 3-kinase adapter protein 1;
GN Name=PIK3AP1; Synonyms=BCAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LYS-21.
RC TISSUE=Spleen, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-83.
RC TISSUE=Fetal liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [5]
RP FUNCTION, INTERACTION WITH ABI1, AND PHOSPHORYLATION AT TYR-513; TYR-553;
RP TYR-570; TYR-594 AND TYR-694.
RX PubMed=15893754; DOI=10.1016/j.febslet.2005.04.052;
RA Maruoka M., Suzuki J., Kawata S., Yoshida K., Hirao N., Sato S., Goff S.P.,
RA Takeya T., Tani K., Shishido T.;
RT "Identification of B cell adaptor for PI3-kinase (BCAP) as an Abl
RT interactor 1-regulated substrate of Abl kinases.";
RL FEBS Lett. 579:2986-2990(2005).
RN [6]
RP INTERACTION WITH PIK3R1, AND TISSUE SPECIFICITY.
RX PubMed=18337558; DOI=10.1182/blood-2007-08-107847;
RA Macfarlane A.W. IV, Yamazaki T., Fang M., Sigal L.J., Kurosaki T.,
RA Campbell K.S.;
RT "Enhanced NK cell development and function in BCAP-deficient mice.";
RL Blood 112:131-140(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Signaling adapter that contributes to B-cell development by
CC linking B-cell receptor (BCR) signaling to the phosphoinositide 3-
CC kinase (PI3K)-Akt signaling pathway. Has a complementary role to the
CC BCR coreceptor CD19, coupling BCR and PI3K activation by providing a
CC docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-
CC like receptor (TLR) signaling to PI3K activation, a process preventing
CC excessive inflammatory cytokine production. Also involved in the
CC activation of PI3K in natural killer cells. May be involved in the
CC survival of mature B-cells via activation of REL.
CC {ECO:0000269|PubMed:15893754}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts (phosphorylated on
CC tyrosine residues within YXXM motifs) with PIK3R1 (via SH2 domain);
CC required for BCR- and TLR-mediated activation of phosphoinositide 3-
CC kinase. Interacts (via polyproline C-terminal region) with ABI1 (via
CC SH3 domain); the interaction promotes phosphorylation of PIK3AP1 by
CC ABL1. May interact with MYD88 and TIRAP (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q6ZUJ8; P62993: GRB2; NbExp=5; IntAct=EBI-2654168, EBI-401755;
CC Q6ZUJ8-3; P16333: NCK1; NbExp=3; IntAct=EBI-11981743, EBI-389883;
CC Q6ZUJ8-3; O43639: NCK2; NbExp=7; IntAct=EBI-11981743, EBI-713635;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=BCAP-L;
CC IsoId=Q6ZUJ8-1; Sequence=Displayed;
CC Name=2; Synonyms=BCAP-S;
CC IsoId=Q6ZUJ8-2; Sequence=VSP_034238;
CC Name=3;
CC IsoId=Q6ZUJ8-3; Sequence=VSP_034239, VSP_034240;
CC -!- TISSUE SPECIFICITY: Expressed in natural killer (NK) cells.
CC {ECO:0000269|PubMed:18337558}.
CC -!- DOMAIN: The DBB domain is required for dimerization. {ECO:0000250}.
CC -!- PTM: Constitutively phosphorylated. Phosphorylated on tyrosine residues
CC in C-terminal region by ABL1. Phosphorylated on tyrosine residues
CC within the YXXM motifs by BTK and SYK (By similarity). Isoform 1 and
CC isoform 2 are phosphorylated on tyrosine residues, most likely within
CC the YXXM motifs, via CD19 activation (By similarity). Toll-like
CC receptor activation induces appearance of a phosphorylated form
CC associated with membranes (By similarity). {ECO:0000250}.
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DR EMBL; AK092883; BAC03996.1; -; mRNA.
DR EMBL; AK125635; BAC86227.1; -; mRNA.
DR EMBL; BX648550; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL358235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029917; AAH29917.1; -; mRNA.
DR CCDS; CCDS31259.1; -. [Q6ZUJ8-1]
DR RefSeq; NP_689522.2; NM_152309.2. [Q6ZUJ8-1]
DR RefSeq; XP_005269555.1; XM_005269498.1. [Q6ZUJ8-2]
DR RefSeq; XP_005269556.1; XM_005269499.1. [Q6ZUJ8-2]
DR PDB; 5FOR; X-ray; 2.50 A; A=7-142.
DR PDB; 6SWS; X-ray; 3.00 A; A/B/C/D/E=179-288.
DR PDBsum; 5FOR; -.
DR PDBsum; 6SWS; -.
DR AlphaFoldDB; Q6ZUJ8; -.
DR SMR; Q6ZUJ8; -.
DR BioGRID; 125621; 23.
DR IntAct; Q6ZUJ8; 10.
DR MINT; Q6ZUJ8; -.
DR STRING; 9606.ENSP00000339826; -.
DR iPTMnet; Q6ZUJ8; -.
DR PhosphoSitePlus; Q6ZUJ8; -.
DR BioMuta; PIK3AP1; -.
DR DMDM; 205830907; -.
DR EPD; Q6ZUJ8; -.
DR jPOST; Q6ZUJ8; -.
DR MassIVE; Q6ZUJ8; -.
DR MaxQB; Q6ZUJ8; -.
DR PaxDb; Q6ZUJ8; -.
DR PeptideAtlas; Q6ZUJ8; -.
DR PRIDE; Q6ZUJ8; -.
DR ProteomicsDB; 68334; -. [Q6ZUJ8-1]
DR ProteomicsDB; 68335; -. [Q6ZUJ8-2]
DR ProteomicsDB; 68336; -. [Q6ZUJ8-3]
DR Antibodypedia; 30771; 379 antibodies from 24 providers.
DR DNASU; 118788; -.
DR Ensembl; ENST00000339364.10; ENSP00000339826.5; ENSG00000155629.15. [Q6ZUJ8-1]
DR Ensembl; ENST00000371109.3; ENSP00000360150.3; ENSG00000155629.15. [Q6ZUJ8-3]
DR Ensembl; ENST00000371110.6; ENSP00000360151.2; ENSG00000155629.15. [Q6ZUJ8-2]
DR GeneID; 118788; -.
DR KEGG; hsa:118788; -.
DR MANE-Select; ENST00000339364.10; ENSP00000339826.5; NM_152309.3; NP_689522.2.
DR UCSC; uc001kmo.4; human. [Q6ZUJ8-1]
DR CTD; 118788; -.
DR DisGeNET; 118788; -.
DR GeneCards; PIK3AP1; -.
DR HGNC; HGNC:30034; PIK3AP1.
DR HPA; ENSG00000155629; Tissue enhanced (liver, lymphoid tissue, salivary gland).
DR MIM; 607942; gene.
DR neXtProt; NX_Q6ZUJ8; -.
DR OpenTargets; ENSG00000155629; -.
DR PharmGKB; PA134979629; -.
DR VEuPathDB; HostDB:ENSG00000155629; -.
DR eggNOG; ENOG502QS94; Eukaryota.
DR GeneTree; ENSGT00390000008787; -.
DR HOGENOM; CLU_012993_0_0_1; -.
DR InParanoid; Q6ZUJ8; -.
DR OMA; IIMKCKL; -.
DR PhylomeDB; Q6ZUJ8; -.
DR TreeFam; TF328570; -.
DR PathwayCommons; Q6ZUJ8; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; Q6ZUJ8; -.
DR SIGNOR; Q6ZUJ8; -.
DR BioGRID-ORCS; 118788; 8 hits in 1076 CRISPR screens.
DR ChiTaRS; PIK3AP1; human.
DR GeneWiki; PIK3AP1; -.
DR GenomeRNAi; 118788; -.
DR Pharos; Q6ZUJ8; Tbio.
DR PRO; PR:Q6ZUJ8; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q6ZUJ8; protein.
DR Bgee; ENSG00000155629; Expressed in parotid gland and 151 other tissues.
DR Genevisible; Q6ZUJ8; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034154; P:toll-like receptor 7 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR017893; DBB_domain.
DR InterPro; IPR041340; PIK3AP1_TIR.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF14545; DBB; 1.
DR Pfam; PF18567; TIR_3; 1.
DR SMART; SM01282; DBB; 1.
DR PROSITE; PS51376; DBB; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..805
FT /note="Phosphoinositide 3-kinase adapter protein 1"
FT /id="PRO_0000341273"
FT DOMAIN 8..145
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 181..317
FT /note="DBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00707"
FT REGION 10..144
FT /note="Necessary and sufficient to mediate inhibition of
FT NF-kappa-B downstream of activated TLRs; may mediate
FT interaction with MYD88 and TIRAP"
FT /evidence="ECO:0000250"
FT REGION 145..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 645..667
FT /evidence="ECO:0000255"
FT COMPBIAS 654..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..805
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 263
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ32"
FT MOD_RES 419
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ32"
FT MOD_RES 444
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ32"
FT MOD_RES 459
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ32"
FT MOD_RES 513
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:15893754"
FT MOD_RES 553
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:15893754"
FT MOD_RES 570
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:15893754"
FT MOD_RES 594
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:15893754"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 694
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:15893754"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..178
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034238"
FT VAR_SEQ 1..57
FT /note="MAASGVPRGCDILIVYSPDAEEWCQYLQTLFLSSRQVRSQKILTHRLGPEAS
FT FSAED -> MRFFTSVACYGSCLFASELLIRCKDWLKGRPALFTALLACVLYLCEWTGA
FT KHVPGSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034239"
FT VAR_SEQ 58..458
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034240"
FT VARIANT 21
FT /note="E -> K (in dbSNP:rs17112076)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_044035"
FT VARIANT 83
FT /note="A -> S (in dbSNP:rs3748229)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_044036"
FT VARIANT 551
FT /note="E -> K (in dbSNP:rs3748233)"
FT /id="VAR_044037"
FT VARIANT 638
FT /note="K -> R (in dbSNP:rs12784975)"
FT /id="VAR_044038"
FT CONFLICT 726
FT /note="T -> P (in Ref. 1; BAC03996)"
FT /evidence="ECO:0000305"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5FOR"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5FOR"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:5FOR"
FT TURN 35..39
FT /evidence="ECO:0007829|PDB:5FOR"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:5FOR"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:5FOR"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:5FOR"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:5FOR"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:5FOR"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5FOR"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:5FOR"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:5FOR"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:5FOR"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:5FOR"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:5FOR"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6SWS"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:6SWS"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:6SWS"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:6SWS"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6SWS"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:6SWS"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:6SWS"
FT STRAND 241..252
FT /evidence="ECO:0007829|PDB:6SWS"
FT STRAND 254..263
FT /evidence="ECO:0007829|PDB:6SWS"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:6SWS"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6SWS"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:6SWS"
SQ SEQUENCE 805 AA; 90398 MW; DF1025A37905AEA7 CRC64;
MAASGVPRGC DILIVYSPDA EEWCQYLQTL FLSSRQVRSQ KILTHRLGPE ASFSAEDLSL
FLSTRCVVVL LSAELVQHFH KPALLPLLQR AFHPPHRVVR LLCGVRDSEE FLDFFPDWAH
WQELTCDDEP ETYVAAVKKA ISEDSGCDSV TDTEPEDEKV VSYSKQQNLP TVTSPGNLMV
VQPDRIRCGA ETTVYVIVRC KLDDRVATEA EFSPEDSPSV RMEAKVENEY TISVKAPNLS
SGNVSLKIYS GDLVVCETVI SYYTDMEEIG NLLSNAANPV EFMCQAFKIV PYNTETLDKL
LTESLKNNIP ASGLHLFGIN QLEEEDMMTN QRDEELPTLL HFAAKYGLKN LTALLLTCPG
ALQAYSVANK HGHYPNTIAE KHGFRDLRQF IDEYVETVDM LKSHIKEELM HGEEADAVYE
SMAHLSTDLL MKCSLNPGCD EDLYESMAAF VPAATEDLYV EMLQASTSNP IPGDGFSRAT
KDSMIRKFLE GNSMGMTNLE RDQCHLGQEE DVYHTVDDDE AFSVDLASRP PVPVPRPETT
APGAHQLPDN EPYIFKVFAE KSQERPGNFY VSSESIRKGP PVRPWRDRPQ SSIYDPFAGM
KTPGQRQLIT LQEQVKLGIV NVDEAVLHFK EWQLNQKKRS ESFRFQQENL KRLRDSITRR
QREKQKSGKQ TDLEITVPIR HSQHLPAKVE FGVYESGPRK SVIPPRTELR RGDWKTDSTS
STASSTSNRS STRSLLSVSS GMEGDNEDNE VPEVTRSRSP GPPQVDGTPT MSLERPPRVP
PRAASQRPPT RETFHPPPPV PPRGR
