CRUM2_HUMAN
ID CRUM2_HUMAN Reviewed; 1285 AA.
AC Q5IJ48; A2A3N4; Q0QD46; Q5JS41; Q5JS43; Q6ZTA9; Q6ZWI6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein crumbs homolog 2 {ECO:0000305};
DE AltName: Full=Crumbs-like protein 2;
DE Flags: Precursor;
GN Name=CRB2 {ECO:0000312|HGNC:HGNC:18688};
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), TISSUE SPECIFICITY, AND VARIANTS
RP LEU-46; LEU-97; LEU-116; THR-145; ALA-159; ASP-187; THR-351; GLN-534;
RP TRP-610; ALA-709; GLN-746 AND MET-1110.
RX PubMed=15851977;
RA van den Hurk J.A.J.M., Rashbass P., Roepman R., Davis J., Voesenek K.E.J.,
RA Arends M.L., Zonneveld M.N., van Roekel M.H.G., Cameron K.,
RA Rohrschneider K., Heckenlively J.R., Koenekoop R.K., Hoyng C.B.,
RA Cremers F.P.M., den Hollander A.I.;
RT "Characterization of the crumbs homolog 2 (CRB2) gene and analysis of its
RT role in retinitis pigmentosa and Leber congenital amaurosis.";
RL Mol. Vis. 11:263-273(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP ASN-90; THR-145; ALA-159 AND ALA-709.
RC TISSUE=Cerebellum;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
RC TISSUE=Retina;
RA Roni V., Carpio R., Wissinger B.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH EPB41L5.
RX PubMed=17920587; DOI=10.1016/j.yexcr.2007.08.025;
RA Gosens I., Sessa A., den Hollander A.I., Letteboer S.J.F., Belloni V.,
RA Arends M.L., Le Bivic A., Cremers F.P.M., Broccoli V., Roepman R.;
RT "FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity
RT complex.";
RL Exp. Cell Res. 313:3959-3970(2007).
RN [6]
RP FUNCTION, INTERACTION WITH THE GAMMA-SECRETASE COMPLEX, INTERACTION WITH
RP PSEN1, GLYCOSYLATION, AND MUTAGENESIS OF TYR-1258; PRO-1260 AND GLU-1264.
RX PubMed=20299451; DOI=10.1074/jbc.m109.038760;
RA Mitsuishi Y., Hasegawa H., Matsuo A., Araki W., Suzuki T., Tagami S.,
RA Okochi M., Takeda M., Roepman R., Nishimura M.;
RT "Human CRB2 inhibits gamma-secretase cleavage of amyloid precursor protein
RT by binding to the presenilin complex.";
RL J. Biol. Chem. 285:14920-14931(2010).
RN [7]
RP INVOLVEMENT IN FSGS9, VARIANTS FSGS9 SER-620; CYS-628; SER-629 AND
RP GLN-1249, AND CHARACTERIZATION OF VARIANTS FSGS9 SER-620 AND SER-629.
RX PubMed=25557779; DOI=10.1016/j.ajhg.2014.11.014;
RA Ebarasi L., Ashraf S., Bierzynska A., Gee H.Y., McCarthy H.J., Lovric S.,
RA Sadowski C.E., Pabst W., Vega-Warner V., Fang H., Koziell A., Simpson M.A.,
RA Dursun I., Serdaroglu E., Levy S., Saleem M.A., Hildebrandt F.,
RA Majumdar A.;
RT "Defects of CRB2 cause steroid-resistant nephrotic syndrome.";
RL Am. J. Hum. Genet. 96:153-161(2015).
RN [8]
RP INVOLVEMENT IN VMCKD, AND VARIANTS VMCKD TRP-633; ALA-643; LYS-800 AND
RP 760-GLY--ILE-1285 DEL.
RX PubMed=25557780; DOI=10.1016/j.ajhg.2014.11.013;
RA Slavotinek A., Kaylor J., Pierce H., Cahr M., DeWard S.J.,
RA Schneidman-Duhovny D., Alsadah A., Salem F., Schmajuk G., Mehta L.;
RT "CRB2 mutations produce a phenotype resembling congenital nephrosis,
RT Finnish type, with cerebral ventriculomegaly and raised alpha-
RT fetoprotein.";
RL Am. J. Hum. Genet. 96:162-169(2015).
RN [9]
RP VARIANT VMCKD LYS-800.
RX PubMed=26925547; DOI=10.1111/cge.12764;
RA Jaron R., Rosenfeld N., Zahdeh F., Carmi S., Beni-Adani L., Doviner V.,
RA Picard E., Segel R., Zeligson S., Carmel L., Renbaum P., Levy-Lahad E.;
RT "Expanding the phenotype of CRB2 mutations - A new ciliopathy syndrome?";
RL Clin. Genet. 90:540-544(2016).
RN [10]
RP VARIANTS FSGS9 CYS-498; ALA-643; LYS-800; ALA-1076; CYS-1115; ARG-1129 AND
RP 1098-CYS--ILE-1285 DEL.
RX PubMed=27004616; DOI=10.1038/ejhg.2016.24;
RA Lamont R.E., Tan W.H., Innes A.M., Parboosingh J.S., Schneidman-Duhovny D.,
RA Rajkovic A., Pappas J., Altschwager P., DeWard S., Fulton A., Gray K.J.,
RA Krall M., Mehta L., Rodan L.H., Saller D.N. Jr., Steele D., Stein D.,
RA Yatsenko S.A., Bernier F.P., Slavotinek A.M.;
RT "Expansion of phenotype and genotypic data in CRB2-related syndrome.";
RL Eur. J. Hum. Genet. 24:1436-1444(2016).
RN [11]
RP VARIANT FSGS9 THR-1184, AND TISSUE SPECIFICITY.
RX PubMed=27942854; DOI=10.1007/s00467-016-3549-4;
RA Udagawa T., Jo T., Yanagihara T., Shimizu A., Mitsui J., Tsuji S.,
RA Morishita S., Onai R., Miura K., Kanda S., Kajiho Y., Tsurumi H., Oka A.,
RA Hattori M., Harita Y.;
RT "Altered expression of Crb2 in podocytes expands a variation of CRB2
RT mutations in steroid-resistant nephrotic syndrome.";
RL Pediatr. Nephrol. 32:801-809(2017).
RN [12]
RP VARIANTS FSGS9 149-GLU--ILE-1285 DEL; MET-902 AND SER-1064.
RX PubMed=30212996; DOI=10.1097/md.0000000000012362;
RA Fan J., Fu R., Ren F., He J., Wang S., Gou M.;
RT "A case report of CRB2 mutation identified in a Chinese boy with focal
RT segmental glomerulosclerosis.";
RL Medicine (Baltimore) 97:e12362-e12362(2018).
RN [13]
RP VARIANTS FSGS9 CYS-628 AND TRP-839, AND TISSUE SPECIFICITY.
RX PubMed=29473663; DOI=10.1111/nep.13244;
RA Watanabe S., Aizawa T., Tsukaguchi H., Tsugawa K., Tsuruga K., Shono A.,
RA Nozu K., Iijima K., Joh K., Tanaka H.;
RT "Long-term clinicopathologic observation in a case of steroid-resistant
RT nephrotic syndrome caused by a novel Crumbs homolog 2 mutation.";
RL Nephrology 23:697-702(2018).
RN [14]
RP VARIANT RP GLY-1249, AND CHARACTERIZATION OF VARIANT GLY-1249.
RX PubMed=30593785; DOI=10.1016/j.exer.2018.12.018;
RA Chen X., Jiang C., Yang D., Sun R., Wang M., Sun H., Xu M., Zhou L.,
RA Chen M., Xie P., Yan B., Liu Q., Zhao C.;
RT "CRB2 mutation causes autosomal recessive retinitis pigmentosa.";
RL Exp. Eye Res. 180:164-173(2019).
RN [15]
RP VARIANT PRO-654.
RX PubMed=32051522; DOI=10.1038/s10038-020-0731-0;
RA Zhang L., Zhang Z., Bi X., Mao Y., Cheng Y., Zhu P., Xu S., Wang Y.,
RA Zhan X., Fan J., Yuan Y., Bi H., Wu X.;
RT "Genetic and preimplantation diagnosis of cystic kidney disease with
RT ventriculomegaly.";
RL J. Hum. Genet. 65:455-459(2020).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-9 IN COMPLEX WITH DYRK1A.
RG Structural genomics consortium (SGC);
RT "The crystal structure of the human dual specificity tyrosine-
RT phosphorylation-regulated kinase 1A.";
RL Submitted (AUG-2009) to the PDB data bank.
CC -!- FUNCTION: Apical polarity protein that plays a central role during the
CC epithelial-to-mesenchymal transition (EMT) at gastrulation, when newly
CC specified mesodermal cells move inside the embryo (By similarity). Acts
CC by promoting cell ingression, the process by which cells leave the
CC epithelial epiblast and move inside the embryo to form a new tissue
CC layer (By similarity). The anisotropic distribution of CRB2 and
CC MYH10/myosin-IIB at cell edges define which cells will ingress: cells
CC with high apical CRB2 are probably extruded from the epiblast by
CC neighboring cells with high levels of apical MYH10/myosin-IIB (By
CC similarity). Plays a role in the maintenance of retinal neuroepithelium
CC organization, structural integrity, adhesion, photoreceptor polarity
CC and retinal photoreceptor layer thickness (By similarity). May play a
CC role in determining the length of cone photoreceptor outer segments and
CC proliferation of late-born progenitor cells (By similarity). Also
CC required for maintenance of the apical polarity complex during
CC development of the cortex (By similarity). Inhibits gamma-secretase-
CC dependent cleavage of APP and secretion of amyloid-beta peptide 40 and
CC amyloid-beta peptide 42, and thereby inhibits gamma-secretase-dependent
CC Notch transcription (PubMed:20299451). {ECO:0000250|UniProtKB:Q80YA8,
CC ECO:0000269|PubMed:20299451}.
CC -!- SUBUNIT: Associates with the gamma-secretase complex via interaction
CC (via the transmembrane domain) with PSEN1/PS1 (PubMed:20299451).
CC Interacts (via intracellular domain) with EPB41L5 (PubMed:17920587).
CC Interacts with PALS1 (By similarity). {ECO:0000250|UniProtKB:Q80YA8,
CC ECO:0000269|PubMed:17920587, ECO:0000269|PubMed:20299451}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q80YA8}; Single-pass type I membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q80YA8}. Cell junction
CC {ECO:0000250|UniProtKB:Q80YA8}. Note=O-glucosylation is required for
CC localization at the apical plasma membrane (By similarity). Distributed
CC in a complex anisotropic pattern on apical cell edges: the level of
CC CRB2 on a cell edge is inversely correlated with the level of
CC MYH10/myosin-IIB (By similarity). {ECO:0000250|UniProtKB:Q80YA8}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5IJ48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5IJ48-2; Sequence=VSP_014739, VSP_014740;
CC Name=3;
CC IsoId=Q5IJ48-3; Sequence=VSP_014737, VSP_014738;
CC -!- TISSUE SPECIFICITY: Expressed in glomeruli, podocytes of the glomerular
CC capillary loops, and parietal glomerular epithelial cells in the kidney
CC (at protein level) (PubMed:29473663, PubMed:27942854). Expressed in
CC retina, fetal eye and brain (PubMed:15851977). Also expressed in
CC kidney, RPE/choroid, and at low levels in lung, placenta, and heart
CC (PubMed:15851977). {ECO:0000269|PubMed:15851977,
CC ECO:0000269|PubMed:27942854, ECO:0000269|PubMed:29473663}.
CC -!- PTM: O-glucosylated by POGLUT1 at Ser-267; consists of an O-glucose
CC trisaccharide, in which the O-glucose is elongated by the addition of
CC two xylose residues. O-glucosylation is required for localization at
CC the plasma membrane. {ECO:0000250|UniProtKB:Q80YA8}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20299451}.
CC -!- DISEASE: Focal segmental glomerulosclerosis 9 (FSGS9) [MIM:616220]: A
CC renal pathology defined by the presence of segmental sclerosis in
CC glomeruli and resulting in proteinuria, reduced glomerular filtration
CC rate and progressive decline in renal function. Renal insufficiency
CC often progresses to end-stage renal disease, a highly morbid state
CC requiring either dialysis therapy or kidney transplantation.
CC {ECO:0000269|PubMed:25557779, ECO:0000269|PubMed:27004616,
CC ECO:0000269|PubMed:27942854, ECO:0000269|PubMed:29473663,
CC ECO:0000269|PubMed:30212996}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Retinitis pigmentosa (RP) [MIM:268000]: A retinal dystrophy
CC belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:30593785}.
CC Note=Disease susceptibility may be associated with variants affecting
CC the gene represented in this entry.
CC -!- DISEASE: Ventriculomegaly with cystic kidney disease (VMCKD)
CC [MIM:219730]: A severe autosomal recessive developmental disorder
CC manifesting in utero. It is characterized by cerebral ventriculomegaly,
CC echogenic kidneys, microscopic renal tubular cysts and findings of
CC congenital nephrosis. {ECO:0000269|PubMed:25557780,
CC ECO:0000269|PubMed:26925547}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}.
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DR EMBL; AY720432; AAU14134.1; -; mRNA.
DR EMBL; AK123000; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK126775; BAC86684.1; -; mRNA.
DR EMBL; AL445489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ426866; ABD90532.1; -; mRNA.
DR CCDS; CCDS6852.2; -. [Q5IJ48-1]
DR RefSeq; NP_775960.4; NM_173689.6. [Q5IJ48-1]
DR RefSeq; XP_005251991.1; XM_005251934.2. [Q5IJ48-3]
DR PDB; 2WO6; X-ray; 2.50 A; C=4-9.
DR PDBsum; 2WO6; -.
DR AlphaFoldDB; Q5IJ48; -.
DR SMR; Q5IJ48; -.
DR BioGRID; 130332; 2.
DR ComplexPortal; CPX-6180; CRUMBS2-PALS1-PATJ cell polarity complex.
DR IntAct; Q5IJ48; 1.
DR STRING; 9606.ENSP00000362734; -.
DR TCDB; 9.B.87.1.30; the selenoprotein p receptor (selp-receptor) family.
DR GlyConnect; 2063; 1 N-Linked glycan (1 site).
DR GlyGen; Q5IJ48; 15 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q5IJ48; -.
DR PhosphoSitePlus; Q5IJ48; -.
DR BioMuta; CRB2; -.
DR DMDM; 116241316; -.
DR EPD; Q5IJ48; -.
DR jPOST; Q5IJ48; -.
DR MassIVE; Q5IJ48; -.
DR PaxDb; Q5IJ48; -.
DR PeptideAtlas; Q5IJ48; -.
DR PRIDE; Q5IJ48; -.
DR ProteomicsDB; 62975; -. [Q5IJ48-1]
DR ProteomicsDB; 62976; -. [Q5IJ48-2]
DR ProteomicsDB; 62977; -. [Q5IJ48-3]
DR Antibodypedia; 48144; 132 antibodies from 22 providers.
DR DNASU; 286204; -.
DR Ensembl; ENST00000359999.7; ENSP00000353092.3; ENSG00000148204.12. [Q5IJ48-2]
DR Ensembl; ENST00000373631.8; ENSP00000362734.3; ENSG00000148204.12. [Q5IJ48-1]
DR Ensembl; ENST00000460253.1; ENSP00000435279.1; ENSG00000148204.12. [Q5IJ48-3]
DR GeneID; 286204; -.
DR KEGG; hsa:286204; -.
DR MANE-Select; ENST00000373631.8; ENSP00000362734.3; NM_173689.7; NP_775960.4.
DR UCSC; uc004bnw.3; human. [Q5IJ48-1]
DR CTD; 286204; -.
DR DisGeNET; 286204; -.
DR GeneCards; CRB2; -.
DR HGNC; HGNC:18688; CRB2.
DR HPA; ENSG00000148204; Group enriched (brain, choroid plexus, kidney, retina).
DR MalaCards; CRB2; -.
DR MIM; 219730; phenotype.
DR MIM; 268000; phenotype.
DR MIM; 609720; gene.
DR MIM; 616220; phenotype.
DR neXtProt; NX_Q5IJ48; -.
DR OpenTargets; ENSG00000148204; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR Orphanet; 443988; Ventriculomegaly-cystic kidney disease.
DR PharmGKB; PA134910460; -.
DR VEuPathDB; HostDB:ENSG00000148204; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00950000183101; -.
DR HOGENOM; CLU_000827_2_2_1; -.
DR InParanoid; Q5IJ48; -.
DR OMA; APCEDCT; -.
DR OrthoDB; 111153at2759; -.
DR PhylomeDB; Q5IJ48; -.
DR TreeFam; TF316224; -.
DR PathwayCommons; Q5IJ48; -.
DR SignaLink; Q5IJ48; -.
DR BioGRID-ORCS; 286204; 14 hits in 1065 CRISPR screens.
DR EvolutionaryTrace; Q5IJ48; -.
DR GenomeRNAi; 286204; -.
DR Pharos; Q5IJ48; Tbio.
DR PRO; PR:Q5IJ48; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5IJ48; protein.
DR Bgee; ENSG00000148204; Expressed in ventricular zone and 68 other tissues.
DR Genevisible; Q5IJ48; HS.
DR GO; GO:0043296; C:apical junction complex; IC:ComplexPortal.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0035003; C:subapical complex; IEA:Ensembl.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IMP:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:UniProtKB.
DR GO; GO:0072359; P:circulatory system development; ISS:CAFA.
DR GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0055111; P:ingression involved in gastrulation with mouth forming second; ISS:UniProtKB.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; ISS:CAFA.
DR GO; GO:0001707; P:mesoderm formation; ISS:CAFA.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0014028; P:notochord formation; ISS:CAFA.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:CAFA.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0010470; P:regulation of gastrulation; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0001895; P:retina homeostasis; ISS:UniProtKB.
DR GO; GO:0046549; P:retinal cone cell development; ISS:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; ISS:CAFA.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00110; LamG; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 12.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; SSF49899; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 7.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 5.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell junction; Cell membrane;
KW Cytoplasm; Developmental protein; Disease variant; Disulfide bond;
KW EGF-like domain; Gastrulation; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Retinitis pigmentosa; Secreted; Sensory transduction; Signal;
KW Transmembrane; Transmembrane helix; Vision.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1285
FT /note="Protein crumbs homolog 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007502"
FT TRANSMEM 1225..1245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 67..106
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 108..144
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 146..182
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 184..221
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 223..259
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 261..318
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 320..356
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 358..394
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 396..436
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 431..603
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 605..641
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 647..805
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 807..843
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 871..1054
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1056..1092
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1094..1130
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1134..1171
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1173..1209
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1..350
FT /note="Required for maximum inhibition of APP amyloid-beta
FT peptide secretion"
FT /evidence="ECO:0000269|PubMed:20299451"
FT REGION 1249..1285
FT /note="Interaction with EPB41L5"
FT /evidence="ECO:0000269|PubMed:17920587"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000250|UniProtKB:Q80YA8"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 836
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 76..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 96..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 112..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 117..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 134..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 150..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 155..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 172..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 188..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 193..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 210..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 227..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 232..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 249..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 265..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 270..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 308..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 324..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 329..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 346..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 362..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 367..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 384..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 400..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 405..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 426..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 579..603
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 609..620
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 614..629
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 631..640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 766..805
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 811..822
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 816..831
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 833..842
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1013..1054
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1060..1071
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1065..1080
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1082..1091
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1098..1108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1103..1118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1120..1129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1138..1150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1144..1159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1161..1170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1177..1188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1182..1197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1199..1208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..332
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014737"
FT VAR_SEQ 333..351
FT /note="GHCQDLPNGFQCHCPDGYA -> MAMEPGALWTFLGHLWLLA (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014738"
FT VAR_SEQ 1131..1176
FT /note="LPVPSKECSLNVTCLDGSPCEGGSPAANCSCLEGLAGQRCQVPTLP -> WD
FT GWAGGWAANAPWGYGGAEKSARSVDESLPFPGPHVLICDMRRTV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014739"
FT VAR_SEQ 1177..1285
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014740"
FT VARIANT 46
FT /note="P -> L (in dbSNP:rs73571404)"
FT /evidence="ECO:0000269|PubMed:15851977"
FT /id="VAR_022984"
FT VARIANT 90
FT /note="T -> N (in dbSNP:rs2808415)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_048974"
FT VARIANT 97
FT /note="V -> L"
FT /evidence="ECO:0000269|PubMed:15851977"
FT /id="VAR_022985"
FT VARIANT 116
FT /note="P -> L (in dbSNP:rs542211566)"
FT /evidence="ECO:0000269|PubMed:15851977"
FT /id="VAR_022986"
FT VARIANT 145
FT /note="M -> T (in dbSNP:rs1105223)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15851977"
FT /id="VAR_022987"
FT VARIANT 149..1285
FT /note="Missing (in FSGS9; when associated in cis with M-902
FT and S-1064; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30212996"
FT /id="VAR_084122"
FT VARIANT 159
FT /note="G -> A (in dbSNP:rs1105222)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15851977"
FT /id="VAR_022988"
FT VARIANT 187
FT /note="E -> D"
FT /evidence="ECO:0000269|PubMed:15851977"
FT /id="VAR_022989"
FT VARIANT 351
FT /note="A -> T (in dbSNP:rs199679542)"
FT /evidence="ECO:0000269|PubMed:15851977"
FT /id="VAR_022990"
FT VARIANT 498
FT /note="W -> C (in FSGS9; when associated in cis with A-
FT 1076; unknown pathological significance;
FT dbSNP:rs144803819)"
FT /evidence="ECO:0000269|PubMed:27004616"
FT /id="VAR_084123"
FT VARIANT 534
FT /note="R -> Q (in dbSNP:rs370059953)"
FT /evidence="ECO:0000269|PubMed:15851977"
FT /id="VAR_022991"
FT VARIANT 610
FT /note="R -> W (in dbSNP:rs145286619)"
FT /evidence="ECO:0000269|PubMed:15851977"
FT /id="VAR_022992"
FT VARIANT 620
FT /note="C -> S (in FSGS9; loss of function mutation;
FT dbSNP:rs879255250)"
FT /evidence="ECO:0000269|PubMed:25557779"
FT /id="VAR_073266"
FT VARIANT 628
FT /note="R -> C (in FSGS9; dbSNP:rs202128397)"
FT /evidence="ECO:0000269|PubMed:25557779,
FT ECO:0000269|PubMed:29473663"
FT /id="VAR_073267"
FT VARIANT 629
FT /note="C -> S (in FSGS9; moderate loss of function
FT mutation; dbSNP:rs879255252)"
FT /evidence="ECO:0000269|PubMed:25557779"
FT /id="VAR_073268"
FT VARIANT 633
FT /note="R -> W (in VMCKD; dbSNP:rs730880377)"
FT /evidence="ECO:0000269|PubMed:25557780"
FT /id="VAR_073269"
FT VARIANT 643
FT /note="E -> A (in VMCKD; when associated in cis with K-800;
FT unknown pathological significance. In FSGS9; when
FT associated in cis with K-800; unknown pathological
FT significance; dbSNP:rs730880300)"
FT /evidence="ECO:0000269|PubMed:25557780,
FT ECO:0000269|PubMed:27004616"
FT /id="VAR_073270"
FT VARIANT 654
FT /note="A -> P (found in a fetus with ventriculomegaly with
FT cystic kidney disease; unknown pathological significance;
FT dbSNP:rs372093386)"
FT /evidence="ECO:0000269|PubMed:32051522"
FT /id="VAR_084124"
FT VARIANT 709
FT /note="V -> A (in dbSNP:rs2488602)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15851977"
FT /id="VAR_061153"
FT VARIANT 746
FT /note="H -> Q (in dbSNP:rs757353722)"
FT /evidence="ECO:0000269|PubMed:15851977"
FT /id="VAR_022993"
FT VARIANT 760..1285
FT /note="Missing (in VMCKD; when associated in cis with K-
FT 800; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25557780"
FT /id="VAR_084125"
FT VARIANT 800
FT /note="N -> K (in VMCKD. In VMCKD; when associated in cis
FT with A-643; unknown pathological significance. In FSGS9;
FT when associated in cis with K-643; unknown pathological
FT significance; dbSNP:rs765676223)"
FT /evidence="ECO:0000269|PubMed:25557780,
FT ECO:0000269|PubMed:26925547, ECO:0000269|PubMed:27004616"
FT /id="VAR_073271"
FT VARIANT 839
FT /note="G -> W (in FSGS9; when associated in cis with C-628;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:29473663"
FT /id="VAR_084126"
FT VARIANT 902
FT /note="T -> M (in FSGS9; when associated in cis with S-1064
FT and 149-E--I-1285 del; unknown pathological significance;
FT dbSNP:rs1463148582)"
FT /evidence="ECO:0000269|PubMed:30212996"
FT /id="VAR_084127"
FT VARIANT 1064
FT /note="P -> S (in FSGS9; when associated in cis with M-902
FT and 149-E--I-1285 del; unknown pathological significance;
FT dbSNP:rs868484209)"
FT /evidence="ECO:0000269|PubMed:30212996"
FT /id="VAR_084128"
FT VARIANT 1076
FT /note="D -> A (in FSGS9; when associated in cis with C-498;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27004616"
FT /id="VAR_084129"
FT VARIANT 1098..1285
FT /note="Missing (in FSGS9; when associated in cis with C-
FT 1115; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27004616"
FT /id="VAR_084130"
FT VARIANT 1110
FT /note="T -> M (in dbSNP:rs73571431)"
FT /evidence="ECO:0000269|PubMed:15851977"
FT /id="VAR_022994"
FT VARIANT 1115
FT /note="R -> C (in FSGS9; when associated in cis with 1098-
FT C--I-1285 del; unknown pathological significance;
FT dbSNP:rs1219047251)"
FT /evidence="ECO:0000269|PubMed:27004616"
FT /id="VAR_084131"
FT VARIANT 1129
FT /note="C -> R (in FSGS9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27004616"
FT /id="VAR_084132"
FT VARIANT 1184
FT /note="N -> T (in FSGS9; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27942854"
FT /id="VAR_084133"
FT VARIANT 1249
FT /note="R -> G (in RP; unknown pathological significance;
FT reduces protein stability and expression)"
FT /evidence="ECO:0000269|PubMed:30593785"
FT /id="VAR_084134"
FT VARIANT 1249
FT /note="R -> Q (in FSGS9; dbSNP:rs147412276)"
FT /evidence="ECO:0000269|PubMed:25557779"
FT /id="VAR_073272"
FT MUTAGEN 1258
FT /note="Y->A: No effect on secretion of APP amyloid-beta
FT peptide 40 and amyloid-beta peptide 42; when associated
FT with P-1260 and E-1264."
FT /evidence="ECO:0000269|PubMed:20299451"
FT MUTAGEN 1260
FT /note="P->A: No effect on secretion of APP amyloid-beta
FT peptide 40 and amyloid-beta peptide 42; when associated
FT with Y-1258 and E-1264."
FT /evidence="ECO:0000269|PubMed:20299451"
FT MUTAGEN 1264
FT /note="E->A: No effect on secretion of APP amyloid-beta
FT peptide 40 and amyloid-beta peptide 42; when associated
FT with Y-1258 and P-1260."
FT /evidence="ECO:0000269|PubMed:20299451"
FT CONFLICT 430
FT /note="T -> A (in Ref. 2; BAC86684)"
FT /evidence="ECO:0000305"
FT CONFLICT 969
FT /note="T -> A (in Ref. 2; AK123000/BAC86684)"
FT /evidence="ECO:0000305"
FT CONFLICT 1153
FT /note="G -> R (in Ref. 2; BAC86684)"
FT /evidence="ECO:0000305"
FT CONFLICT 1239
FT /note="Missing (in Ref. 2; BAC86684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1285 AA; 134265 MW; C5B7E9D7A91CD703 CRC64;
MALARPGTPD PQALASVLLL LLWAPALSLL AGTVPSEPPS ACASDPCAPG TECQATESGG
YTCGPMEPRG CATQPCHHGA LCVPQGPDPT GFRCYCVPGF QGPRCELDID ECASRPCHHG
ATCRNLADRY ECHCPLGYAG VTCEMEVDEC ASAPCLHGGS CLDGVGSFRC VCAPGYGGTR
CQLDLDECQS QPCAHGGTCH DLVNGFRCDC AGTGYEGTHC EREVLECASA PCEHNASCLE
GLGSFRCLCW PGYSGELCEV DEDECASSPC QHGGRCLQRS DPALYGGVQA AFPGAFSFRH
AAGFLCHCPP GFEGADCGVE VDECASRPCL NGGHCQDLPN GFQCHCPDGY AGPTCEEDVD
ECLSDPCLHG GTCSDTVAGY ICRCPETWGG RDCSVQLTGC QGHTCPLAAT CIPIFESGVH
SYVCHCPPGT HGPFCGQNTT FSVMAGSPIQ ASVPAGGPLG LALRFRTTLP AGTLATRNDT
KESLELALVA ATLQATLWSY STTVLVLRLP DLALNDGHWH QVEVVLHLAT LELRLWHEGC
PARLCVASGP VALASTASAT PLPAGISSAQ LGDATFAGCL QDVRVDGHLL LPEDLGENVL
LGCERREQCR PLPCVHGGSC VDLWTHFRCD CARPHRGPTC ADEIPAATFG LGGAPSSASF
LLQELPGPNL TVSFLLRTRE SAGLLLQFAN DSAAGLTVFL SEGRIRAEVP GSPAVVLPGR
WDDGLRHLVM LSFGPDQLQD LGQHVHVGGR LLAADSQPWG GPFRGCLQDL RLDGCHLPFF
PLPLDNSSQP SELGGRQSWN LTAGCVSEDM CSPDPCFNGG TCLVTWNDFH CTCPANFTGP
TCAQQLWCPG QPCLPPATCE EVPDGFVCVA EATFREGPPA AFSGHNASSG RLLGGLSLAF
RTRDSEAWLL RAAAGALEGV WLAVRNGSLA GGVRGGHGLP GAVLPIPGPR VADGAWHRVR
LAMERPAATT SRWLLWLDGA ATPVALRGLA SDLGFLQGPG AVRILLAENF TGCLGRVALG
GLPLPLARPR PGAAPGAREH FASWPGTPAP ILGCRGAPVC APSPCLHDGA CRDLFDAFAC
ACGPGWEGPR CEAHVDPCHS APCARGRCHT HPDGRFECRC PPGFGGPRCR LPVPSKECSL
NVTCLDGSPC EGGSPAANCS CLEGLAGQRC QVPTLPCEAN PCLNGGTCRA AGGVSECICN
ARFSGQFCEV AKGLPLPLPF PLLEVAVPAA CACLLLLLLG LLSGILAARK RRQSEGTYSP
SQQEVAGARL EMDSVLKVPP EERLI
