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   24-JAN-2024, entry version 147.
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.
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; 25.
DR   IntAct; Q6ZUJ8; 11.
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; 9606-ENSP00000339826; -.
DR   PeptideAtlas; Q6ZUJ8; -.
DR   ProteomicsDB; 68334; -. [Q6ZUJ8-1]
DR   ProteomicsDB; 68335; -. [Q6ZUJ8-2]
DR   ProteomicsDB; 68336; -. [Q6ZUJ8-3]
DR   Pumba; Q6ZUJ8; -.
DR   Antibodypedia; 30771; 430 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   AGR; HGNC:30034; -.
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; YYTSMGE; -.
DR   OrthoDB; 2967820at2759; -.
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; 17 hits in 1158 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 153 other cell types or tissues.
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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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; Toll/interleukin-1 receptor homology (TIR) domain; 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   PANTHER; PTHR16267; BANK1/PIK3AP1 FAMILY MEMBER; 1.
DR   PANTHER; PTHR16267:SF12; PHOSPHOINOSITIDE 3-KINASE ADAPTER PROTEIN 1; 1.
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.
DR   Genevisible; Q6ZUJ8; HS.
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
//