KIRR1_HUMAN
ID KIRR1_HUMAN Reviewed; 757 AA.
AC Q96J84; Q5W0F8; Q5XKC6; Q7Z696; Q7Z7N8; Q8TB15; Q9H9N1; Q9NVA5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Kin of IRRE-like protein 1;
DE AltName: Full=Kin of irregular chiasm-like protein 1;
DE AltName: Full=Nephrin-like protein 1;
DE Flags: Precursor;
GN Name=KIRREL1 {ECO:0000312|HGNC:HGNC:15734}; Synonyms=KIRREL, NEPH1;
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] OF 1-606 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=11416156; DOI=10.1128/mcb.21.14.4829-4836.2001;
RA Donoviel D.B., Freed D.D., Vogel H., Potter D.G., Hawkins E., Barrish J.P.,
RA Mathur B.N., Turner C.A., Geske R., Montgomery C.A., Starbuck M.,
RA Brandt M., Gupta A., Ramirez-Solis R., Zambrowicz B.P., Powell D.R.;
RT "Proteinuria and perinatal lethality in mice lacking NEPH1, a novel protein
RT with homology to NEPHRIN.";
RL Mol. Cell. Biol. 21:4829-4836(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Shan Y.X., Huang C.Q., Yu L.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 251-757 (ISOFORM 2).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-757 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 303-757 (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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-622; TYR-625 AND TYR-724, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-297.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN NPHS23, VARIANTS NPHS23
RP CYS-440 AND LEU-573, AND CHARACTERIZATION OF VARIANTS NPHS23 CYS-440 AND
RP LEU-573.
RX PubMed=31472902; DOI=10.1016/j.kint.2019.06.016;
RA Solanki A.K., Widmeier E., Arif E., Sharma S., Daga A., Srivastava P.,
RA Kwon S.H., Hugo H., Nakayama M., Mann N., Majmundar A.J., Tan W., Gee H.Y.,
RA Sadowski C.E., Rinat C., Becker-Cohen R., Bergmann C., Rosen S., Somers M.,
RA Shril S., Huber T.B., Mane S., Hildebrandt F., Nihalani D.;
RT "Mutations in KIRREL1, a slit diaphragm component, cause steroid-resistant
RT nephrotic syndrome.";
RL Kidney Int. 96:883-889(2019).
CC -!- FUNCTION: Required for proper function of the glomerular filtration
CC barrier. It is involved in the maintenance of a stable podocyte
CC architecture with interdigitating foot processes connected by
CC specialized cell-cell junctions, known as the slit diaphragm
CC (PubMed:31472902). It is a signaling protein that needs the presence of
CC TEC kinases to fully trans-activate the transcription factor AP-1 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:31472902}.
CC -!- SUBUNIT: Interacts with TJP1/ZO-1 and with NPHS2/podocin (via the C-
CC terminus). Interacts with NPHS1/nephrin (via the Ig-like domains); this
CC interaction is dependent on KIRREL1 glycosylation. Homodimer (via the
CC Ig-like domains). Interacts when tyrosine-phosphorylated with GRB2 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96J84; Q07157: TJP1; NbExp=7; IntAct=EBI-3988456, EBI-79553;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31472902};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Predominantly
CC located at podocyte slit diaphragm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96J84-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96J84-2; Sequence=VSP_011733;
CC Name=3;
CC IsoId=Q96J84-3; Sequence=VSP_011732;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in kidney. Specifically
CC expressed in podocytes of kidney glomeruli.
CC {ECO:0000269|PubMed:11416156}.
CC -!- PTM: Phosphorylation probably regulates the interaction with NSH2.
CC Phosphorylated at Tyr-605 and Tyr-606 by FYN, leading to GRB2 binding
CC (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- DISEASE: Nephrotic syndrome 23 (NPHS23) [MIM:619201]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form that progresses to end-stage renal failure.
CC NPHS23 is an autosomal recessive form characterized by onset of
CC proteinuria in the first or second decade of life, and variable
CC outcome. Some patients have normal renal function after many years,
CC whereas others may progress to chronic kidney disease.
CC {ECO:0000269|PubMed:31472902}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP59845.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91850.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY017369; AAK00529.1; -; mRNA.
DR EMBL; AY302131; AAP59845.1; ALT_FRAME; mRNA.
DR EMBL; AL139010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52853.1; -; Genomic_DNA.
DR EMBL; BC025268; AAH25268.1; -; mRNA.
DR EMBL; BC051356; AAH51356.1; -; mRNA.
DR EMBL; BC067097; AAH67097.1; -; mRNA.
DR EMBL; BC082969; AAH82969.1; -; mRNA.
DR EMBL; BC109192; AAI09193.1; -; mRNA.
DR EMBL; BC109193; AAI09194.1; -; mRNA.
DR EMBL; AK001707; BAA91850.1; ALT_INIT; mRNA.
DR EMBL; AK022708; BAB14192.1; ALT_INIT; mRNA.
DR CCDS; CCDS1172.2; -. [Q96J84-1]
DR RefSeq; NP_001273278.1; NM_001286349.1.
DR RefSeq; NP_060710.3; NM_018240.6. [Q96J84-1]
DR RefSeq; XP_005245362.1; XM_005245305.4. [Q96J84-2]
DR AlphaFoldDB; Q96J84; -.
DR SMR; Q96J84; -.
DR BioGRID; 120534; 110.
DR IntAct; Q96J84; 35.
DR MINT; Q96J84; -.
DR STRING; 9606.ENSP00000352138; -.
DR GlyGen; Q96J84; 4 sites.
DR iPTMnet; Q96J84; -.
DR PhosphoSitePlus; Q96J84; -.
DR BioMuta; KIRREL1; -.
DR DMDM; 54036152; -.
DR EPD; Q96J84; -.
DR jPOST; Q96J84; -.
DR MassIVE; Q96J84; -.
DR MaxQB; Q96J84; -.
DR PaxDb; Q96J84; -.
DR PeptideAtlas; Q96J84; -.
DR PRIDE; Q96J84; -.
DR ProteomicsDB; 76896; -. [Q96J84-1]
DR ProteomicsDB; 76897; -. [Q96J84-2]
DR ProteomicsDB; 76898; -. [Q96J84-3]
DR Antibodypedia; 34235; 142 antibodies from 26 providers.
DR DNASU; 55243; -.
DR Ensembl; ENST00000359209.11; ENSP00000352138.6; ENSG00000183853.18. [Q96J84-1]
DR GeneID; 55243; -.
DR KEGG; hsa:55243; -.
DR MANE-Select; ENST00000359209.11; ENSP00000352138.6; NM_018240.7; NP_060710.3.
DR UCSC; uc001frn.6; human. [Q96J84-1]
DR CTD; 55243; -.
DR DisGeNET; 55243; -.
DR GeneCards; KIRREL1; -.
DR HGNC; HGNC:15734; KIRREL1.
DR HPA; ENSG00000183853; Low tissue specificity.
DR MalaCards; KIRREL1; -.
DR MIM; 607428; gene.
DR MIM; 619201; phenotype.
DR neXtProt; NX_Q96J84; -.
DR OpenTargets; ENSG00000183853; -.
DR PharmGKB; PA30126; -.
DR VEuPathDB; HostDB:ENSG00000183853; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155795; -.
DR InParanoid; Q96J84; -.
DR OMA; TIIWYRD; -.
DR OrthoDB; 269917at2759; -.
DR PhylomeDB; Q96J84; -.
DR TreeFam; TF327139; -.
DR PathwayCommons; Q96J84; -.
DR Reactome; R-HSA-373753; Nephrin family interactions.
DR SignaLink; Q96J84; -.
DR SIGNOR; Q96J84; -.
DR BioGRID-ORCS; 55243; 35 hits in 1083 CRISPR screens.
DR ChiTaRS; KIRREL; human.
DR GeneWiki; KIRREL; -.
DR GenomeRNAi; 55243; -.
DR Pharos; Q96J84; Tbio.
DR PRO; PR:Q96J84; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96J84; protein.
DR Bgee; ENSG00000183853; Expressed in stromal cell of endometrium and 134 other tissues.
DR ExpressionAtlas; Q96J84; baseline and differential.
DR Genevisible; Q96J84; HS.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; IPI:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0045217; P:cell-cell junction maintenance; IMP:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0097017; P:renal protein absorption; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..757
FT /note="Kin of IRRE-like protein 1"
FT /id="PRO_0000015093"
FT TOPO_DOM 17..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..115
FT /note="Ig-like C2-type 1"
FT DOMAIN 120..216
FT /note="Ig-like C2-type 2"
FT DOMAIN 223..299
FT /note="Ig-like C2-type 3"
FT DOMAIN 308..387
FT /note="Ig-like C2-type 4"
FT DOMAIN 392..488
FT /note="Ig-like C2-type 5"
FT REGION 649..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 405..407
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 605
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q6X936"
FT MOD_RES 606
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q6X936"
FT MOD_RES 622
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 625
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 724
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 143..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 244..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 329..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 413..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 118..221
FT /note="IPPEDTRIDGGPVILLQAGTPHNLTCRAFNAKPAATIIWFRDGTQQEGAVAS
FT TELLKDGKRETTVSQLLINPTDLDIGRVFTCRSMNEAIPSGKETSIELDVHH -> N
FT (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_011732"
FT VAR_SEQ 348
FT /note="M -> MGPRPPGSPPEAALSAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011733"
FT VARIANT 78
FT /note="A -> T (in dbSNP:rs35927201)"
FT /id="VAR_059428"
FT VARIANT 440
FT /note="R -> C (in NPHS23; decreased localization to cell
FT membrane due to intracellular retention; affects integrity
FT of podocyte cell-cell junctions and leads to altered
FT cellular permeability)"
FT /evidence="ECO:0000269|PubMed:31472902"
FT /id="VAR_085245"
FT VARIANT 573
FT /note="S -> L (in NPHS23; unknown pathological
FT significance; affects integrity of podocyte cell-cell
FT junctions and leads to altered cellular permeability)"
FT /evidence="ECO:0000269|PubMed:31472902"
FT /id="VAR_085246"
FT CONFLICT 591..605
FT /note="DTREEYEMKDPTNGY -> ERPRIRGRLNTSYSD (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 83536 MW; B937421970447FC2 CRC64;
MLSLLVWILT LSDTFSQGTQ TRFSQEPADQ TVVAGQRAVL PCVLLNYSGI VQWTKDGLAL
GMGQGLKAWP RYRVVGSADA GQYNLEITDA ELSDDASYEC QATEAALRSR RAKLTVLIPP
EDTRIDGGPV ILLQAGTPHN LTCRAFNAKP AATIIWFRDG TQQEGAVAST ELLKDGKRET
TVSQLLINPT DLDIGRVFTC RSMNEAIPSG KETSIELDVH HPPTVTLSIE PQTVQEGERV
VFTCQATANP EILGYRWAKG GFLIEDAHES RYETNVDYSF FTEPVSCEVH NKVGSTNVST
LVNVHFAPRI VVDPKPTTTD IGSDVTLTCV WVGNPPLTLT WTKKDSNMVL SNSNQLLLKS
VTQADAGTYT CRAIVPRIGV AEREVPLYVN GPPIISSEAV QYAVRGDGGK VECFIGSTPP
PDRIAWAWKE NFLEVGTLER YTVERTNSGS GVLSTLTINN VMEADFQTHY NCTAWNSFGP
GTAIIQLEER EVLPVGIIAG ATIGASILLI FFFIALVFFL YRRRKGSRKD VTLRKLDIKV
ETVNREPLTM HSDREDDTAS VSTATRVMKA IYSSFKDDVD LKQDLRCDTI DTREEYEMKD
PTNGYYNVRA HEDRPSSRAV LYADYRAPGP ARFDGRPSSR LSHSSGYAQL NTYSRGPASD
YGPEPTPPGP AAPAGTDTTS QLSYENYEKF NSHPFPGAAG YPTYRLGYPQ APPSGLERTP
YEAYDPIGKY ATATRFSYTS QHSDYGQRFQ QRMQTHV
