FKB10_HUMAN
ID FKB10_HUMAN Reviewed; 582 AA.
AC Q96AY3; Q7Z3R4; Q9H3N3; Q9H6J3; Q9H6N5; Q9UF89;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP10;
DE Short=PPIase FKBP10;
DE EC=5.2.1.8;
DE AltName: Full=65 kDa FK506-binding protein;
DE Short=65 kDa FKBP;
DE Short=FKBP-65;
DE AltName: Full=FK506-binding protein 10;
DE Short=FKBP-10;
DE AltName: Full=Immunophilin FKBP65;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP10; Synonyms=FKBP65; ORFNames=PSEC0056;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Rulten S., Kinloch R.A., Robinson C., Gettins L., Kay J.E.;
RT "The human FK506-binding protein repertoire.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 82-582 (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrial tumor, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP GLYCOSYLATION AT ASN-182 AND ASN-407.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-182.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP VARIANT OI11 MET-107--117-LEU DEL.
RX PubMed=20362275; DOI=10.1016/j.ajhg.2010.02.022;
RA Alanay Y., Avaygan H., Camacho N., Utine G.E., Boduroglu K., Aktas D.,
RA Alikasifoglu M., Tuncbilek E., Orhan D., Bakar F.T., Zabel B.,
RA Superti-Furga A., Bruckner-Tuderman L., Curry C.J., Pyott S., Byers P.H.,
RA Eyre D.R., Baldridge D., Lee B., Merrill A.E., Davis E.C., Cohn D.H.,
RA Akarsu N., Krakow D.;
RT "Mutations in the gene encoding the RER protein FKBP65 cause autosomal-
RT recessive osteogenesis imperfecta.";
RL Am. J. Hum. Genet. 86:551-559(2010).
RN [12]
RP VARIANT BRKS1 GLN-115, AND INVOLVEMENT IN OI11.
RX PubMed=20839288; DOI=10.1002/jbmr.250;
RA Kelley B.P., Malfait F., Bonafe L., Baldridge D., Homan E., Symoens S.,
RA Willaert A., Elcioglu N., Van Maldergem L., Verellen-Dumoulin C.,
RA Gillerot Y., Napierala D., Krakow D., Beighton P., Superti-Furga A.,
RA De Paepe A., Lee B.;
RT "Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck
RT syndrome.";
RL J. Bone Miner. Res. 26:666-672(2011).
RN [13]
RP VARIANTS BRKS1 LYS-113; GLN-115 AND LEU-136, AND INVOLVEMENT IN OI11.
RX PubMed=22949511; DOI=10.1093/hmg/dds371;
RA Schwarze U., Cundy T., Pyott S.M., Christiansen H.E., Hegde M.R.,
RA Bank R.A., Pals G., Ankala A., Conneely K., Seaver L., Yandow S.M.,
RA Raney E., Babovic-Vuksanovic D., Stoler J., Ben-Neriah Z., Segel R.,
RA Lieberman S., Siderius L., Al-Aqeel A., Hannibal M., Hudgins L.,
RA McPherson E., Clemens M., Sussman M.D., Steiner R.D., Mahan J., Smith R.,
RA Anyane-Yeboa K., Wynn J., Chong K., Uster T., Aftimos S., Sutton V.R.,
RA Davis E.C., Kim L.S., Weis M.A., Eyre D., Byers P.H.;
RT "Mutations in FKBP10, which result in Bruck syndrome and recessive forms of
RT osteogenesis imperfecta, inhibit the hydroxylation of telopeptide lysines
RT in bone collagen.";
RL Hum. Mol. Genet. 22:1-17(2013).
CC -!- FUNCTION: PPIases accelerate the folding of proteins during protein
CC synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin, but not by
CC cyclosporin A. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96AY3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2372475, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96AY3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AY3-2; Sequence=VSP_056425, VSP_056426, VSP_056427,
CC VSP_056428;
CC -!- PTM: Glycosylated and phosphorylated. {ECO:0000250}.
CC -!- DISEASE: Osteogenesis imperfecta 11 (OI11) [MIM:610968]: A form of
CC osteogenesis imperfecta, a connective tissue disorder characterized by
CC low bone mass, bone fragility and susceptibility to fractures after
CC minimal trauma. Disease severity ranges from very mild forms without
CC fractures to intrauterine fractures and perinatal lethality.
CC Extraskeletal manifestations, which affect a variable number of
CC patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI11 is an autosomal recessive form.
CC {ECO:0000269|PubMed:20362275, ECO:0000269|PubMed:20839288,
CC ECO:0000269|PubMed:22949511}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Bruck syndrome 1 (BRKS1) [MIM:259450]: A disease characterized
CC by generalized osteopenia, congenital joint contractures, fragile bones
CC with onset of fractures in infancy or early childhood, short stature,
CC severe limb deformity, progressive scoliosis, and pterygia.
CC {ECO:0000269|PubMed:20839288, ECO:0000269|PubMed:22949511}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15220.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD97695.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database;
CC Note=Peptidyl-prolyl cis-trans isomerase FKBP10;
CC URL="http://oi.gene.le.ac.uk/home.php?select_db=FKBP10";
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DR EMBL; AF337909; AAM15770.1; -; mRNA.
DR EMBL; AK025694; BAB15220.1; ALT_INIT; mRNA.
DR EMBL; AK025874; BAB15266.1; -; mRNA.
DR EMBL; AB045981; BAB20974.1; -; mRNA.
DR EMBL; BX537452; CAD97695.1; ALT_INIT; mRNA.
DR EMBL; AL133116; CAB61418.1; -; mRNA.
DR EMBL; AC091172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016467; AAH16467.1; -; mRNA.
DR CCDS; CCDS11409.1; -. [Q96AY3-1]
DR PIR; T42709; T42709.
DR RefSeq; NP_068758.3; NM_021939.3. [Q96AY3-1]
DR AlphaFoldDB; Q96AY3; -.
DR SMR; Q96AY3; -.
DR BioGRID; 121955; 95.
DR CORUM; Q96AY3; -.
DR IntAct; Q96AY3; 18.
DR MINT; Q96AY3; -.
DR STRING; 9606.ENSP00000317232; -.
DR DrugCentral; Q96AY3; -.
DR GlyConnect; 1597; 12 N-Linked glycans (6 sites).
DR GlyGen; Q96AY3; 8 sites, 17 N-linked glycans (6 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q96AY3; -.
DR MetOSite; Q96AY3; -.
DR PhosphoSitePlus; Q96AY3; -.
DR SwissPalm; Q96AY3; -.
DR BioMuta; FKBP10; -.
DR DMDM; 23396594; -.
DR EPD; Q96AY3; -.
DR jPOST; Q96AY3; -.
DR MassIVE; Q96AY3; -.
DR MaxQB; Q96AY3; -.
DR PaxDb; Q96AY3; -.
DR PeptideAtlas; Q96AY3; -.
DR PRIDE; Q96AY3; -.
DR ProteomicsDB; 76020; -. [Q96AY3-1]
DR ProteomicsDB; 80989; -.
DR TopDownProteomics; Q96AY3-1; -. [Q96AY3-1]
DR Antibodypedia; 28953; 279 antibodies from 30 providers.
DR DNASU; 60681; -.
DR Ensembl; ENST00000321562.9; ENSP00000317232.4; ENSG00000141756.19. [Q96AY3-1]
DR GeneID; 60681; -.
DR KEGG; hsa:60681; -.
DR MANE-Select; ENST00000321562.9; ENSP00000317232.4; NM_021939.4; NP_068758.3.
DR UCSC; uc002hxv.3; human. [Q96AY3-1]
DR CTD; 60681; -.
DR DisGeNET; 60681; -.
DR GeneCards; FKBP10; -.
DR HGNC; HGNC:18169; FKBP10.
DR HPA; ENSG00000141756; Low tissue specificity.
DR MalaCards; FKBP10; -.
DR MIM; 259450; phenotype.
DR MIM; 607063; gene.
DR MIM; 610968; phenotype.
DR neXtProt; NX_Q96AY3; -.
DR OpenTargets; ENSG00000141756; -.
DR Orphanet; 2771; Bruck syndrome.
DR Orphanet; 1149; Kuskokwim syndrome.
DR Orphanet; 216812; Osteogenesis imperfecta type 3.
DR Orphanet; 216820; Osteogenesis imperfecta type 4.
DR PharmGKB; PA28152; -.
DR VEuPathDB; HostDB:ENSG00000141756; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000156331; -.
DR HOGENOM; CLU_034907_0_0_1; -.
DR InParanoid; Q96AY3; -.
DR OMA; SYNRKQT; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; Q96AY3; -.
DR TreeFam; TF105296; -.
DR PathwayCommons; Q96AY3; -.
DR SignaLink; Q96AY3; -.
DR BioGRID-ORCS; 60681; 16 hits in 1075 CRISPR screens.
DR ChiTaRS; FKBP10; human.
DR GenomeRNAi; 60681; -.
DR Pharos; Q96AY3; Tbio.
DR PRO; PR:Q96AY3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96AY3; protein.
DR Bgee; ENSG00000141756; Expressed in stromal cell of endometrium and 106 other tissues.
DR ExpressionAtlas; Q96AY3; baseline and differential.
DR Genevisible; Q96AY3; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005528; F:FK506 binding; ISS:FlyBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:FlyBase.
DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IEA:Ensembl.
DR GO; GO:0018208; P:peptidyl-proline modification; ISS:FlyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.10.50.40; -; 4.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF00254; FKBP_C; 4.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disease variant; Endoplasmic reticulum;
KW Glycoprotein; Isomerase; Metal-binding; Osteogenesis imperfecta;
KW Phosphoprotein; Reference proteome; Repeat; Rotamase; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..582
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP10"
FT /id="PRO_0000025517"
FT DOMAIN 62..150
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 174..262
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 286..374
FT /note="PPIase FKBP-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 399..486
FT /note="PPIase FKBP-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 497..532
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 542..577
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 533..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 579..582
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 559..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 512
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 555
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 557
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 561
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 566
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT VAR_SEQ 2..177
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056425"
FT VAR_SEQ 184..212
FT /note="TLLDGTSFDTSYSKGGTYDTYVGSGWLIK -> SLMDGTLFDSSYSRNHTYN
FT TYIGQGYIIP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056426"
FT VAR_SEQ 219..303
FT /note="LGMCPGERRKIIIPPFLAYGEKGYGTVIPPQASLVFHVLLIDVHNPKDAVQL
FT ETLELPPGCVRRAGAGDFMRYHYNGSLMDGTLF -> QGACMGERRRITIPPHLAYGEN
FT GTDSIGFLQGSAPLRPFRSGEGQPSLGREGGYGKTEPAYPQDPAVLGASVSSPVKWASH
FT ADPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056427"
FT VAR_SEQ 304..354
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056428"
FT VARIANT 107..117
FT /note="Missing (in OI11)"
FT /id="VAR_063601"
FT VARIANT 113
FT /note="E -> K (in BRKS1; dbSNP:rs397514674)"
FT /evidence="ECO:0000269|PubMed:22949511"
FT /id="VAR_069902"
FT VARIANT 115
FT /note="R -> Q (in BRKS1; dbSNP:rs387906960)"
FT /evidence="ECO:0000269|PubMed:20839288,
FT ECO:0000269|PubMed:22949511"
FT /id="VAR_069903"
FT VARIANT 136
FT /note="P -> L (in BRKS1; dbSNP:rs782653042)"
FT /evidence="ECO:0000269|PubMed:22949511"
FT /id="VAR_069904"
FT VARIANT 197
FT /note="K -> R (in dbSNP:rs34764749)"
FT /id="VAR_050625"
FT CONFLICT 190
FT /note="S -> F (in Ref. 3; BAB20974)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="V -> L (in Ref. 4; CAD97695)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 64245 MW; 98257459158407C2 CRC64;
MFPAGPPSHS LLRLPLLQLL LLVVQAVGRG LGRASPAGGP LEDVVIERYH IPRACPREVQ
MGDFVRYHYN GTFEDGKKFD SSYDRNTLVA IVVGVGRLIT GMDRGLMGMC VNERRRLIVP
PHLGYGSIGL AGLIPPDATL YFDVVLLDVW NKEDTVQVST LLRPPHCPRM VQDGDFVRYH
YNGTLLDGTS FDTSYSKGGT YDTYVGSGWL IKGMDQGLLG MCPGERRKII IPPFLAYGEK
GYGTVIPPQA SLVFHVLLID VHNPKDAVQL ETLELPPGCV RRAGAGDFMR YHYNGSLMDG
TLFDSSYSRN HTYNTYIGQG YIIPGMDQGL QGACMGERRR ITIPPHLAYG ENGTGDKIPG
SAVLIFNVHV IDFHNPADVV EIRTLSRPSE TCNETTKLGD FVRYHYNCSL LDGTQLFTSH
DYGAPQEATL GANKVIEGLD TGLQGMCVGE RRQLIVPPHL AHGESGARGV PGSAVLLFEV
ELVSREDGLP TGYLFVWHKD PPANLFEDMD LNKDGEVPPE EFSTFIKAQV SEGKGRLMPG
QDPEKTIGDM FQNQDRNQDG KITVDELKLK SDEDEERVHE EL
