KIRR1_RAT
ID KIRR1_RAT Reviewed; 789 AA.
AC Q6X936; F1M7V1; Q80W67;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 134.
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; Synonyms=Kirrel, Neph1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Kawachi H., Koike H., Han G.D., Shimizu F.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-786, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=12865409; DOI=10.1172/jci200318242;
RA Liu G., Kaw B., Kurfis J., Rahmanuddin S., Kanwar Y.S., Chugh S.S.;
RT "Neph1 and nephrin interaction in the slit diaphragm is an important
RT determinant of glomerular permeability.";
RL J. Clin. Invest. 112:209-221(2003).
RN [4]
RP PHOSPHORYLATION AT TYR-637 AND TYR-638 BY FYN, AND INTERACTION WITH GRB2.
RX PubMed=18258597; DOI=10.1074/jbc.m707247200;
RA Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T.,
RA Hattori S.;
RT "Neph1, a component of the kidney slit diaphragm, is tyrosine-
RT phosphorylated by the Src family tyrosine kinase and modulates
RT intracellular signaling by binding to Grb2.";
RL J. Biol. Chem. 283:9177-9186(2008).
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 (By
CC similarity). It is a signaling protein that needs the presence of TEC
CC kinases to fully trans-activate the transcription factor AP-1 (By
CC similarity). {ECO:0000250|UniProtKB:Q96J84}.
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) (By similarity). Interacts when tyrosine-
CC phosphorylated with GRB2. {ECO:0000250, ECO:0000269|PubMed:18258597}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=Predominantly located at podocyte
CC slit diaphragm. {ECO:0000269|PubMed:12865409}.
CC -!- PTM: Phosphorylation probably regulates the interaction with NPHS2 (By
CC similarity). Phosphorylated at Tyr-637 and Tyr-638 by FYN, leading to
CC GRB2 binding. {ECO:0000250, ECO:0000269|PubMed:18258597}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AY249056; AAP78673.1; -; mRNA.
DR EMBL; AABR06018737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06018738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY271309; AAP12626.1; -; mRNA.
DR RefSeq; NP_997489.1; NM_207606.1.
DR RefSeq; XP_006232739.1; XM_006232677.3.
DR AlphaFoldDB; Q6X936; -.
DR SMR; Q6X936; -.
DR CORUM; Q6X936; -.
DR IntAct; Q6X936; 1.
DR MINT; Q6X936; -.
DR STRING; 10116.ENSRNOP00000033900; -.
DR GlyGen; Q6X936; 5 sites.
DR iPTMnet; Q6X936; -.
DR PhosphoSitePlus; Q6X936; -.
DR PaxDb; Q6X936; -.
DR PRIDE; Q6X936; -.
DR Ensembl; ENSRNOT00000031743; ENSRNOP00000033900; ENSRNOG00000016408.
DR GeneID; 310695; -.
DR KEGG; rno:310695; -.
DR UCSC; RGD:727883; rat.
DR CTD; 55243; -.
DR RGD; 727883; Kirrel1.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000155795; -.
DR InParanoid; Q6X936; -.
DR OMA; TIIWYRD; -.
DR OrthoDB; 269917at2759; -.
DR TreeFam; TF327139; -.
DR Reactome; R-RNO-373753; Nephrin family interactions.
DR PRO; PR:Q6X936; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000016408; Expressed in ovary and 19 other tissues.
DR ExpressionAtlas; Q6X936; baseline and differential.
DR Genevisible; Q6X936; RN.
DR GO; GO:0031253; C:cell projection membrane; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0045217; P:cell-cell junction maintenance; ISO:RGD.
DR GO; GO:0003094; P:glomerular filtration; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0097017; P:renal protein absorption; ISO:RGD.
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 Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT CHAIN 48..789
FT /note="Kin of IRRE-like protein 1"
FT /id="PRO_0000015095"
FT TOPO_DOM 48..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..147
FT /note="Ig-like C2-type 1"
FT DOMAIN 152..248
FT /note="Ig-like C2-type 2"
FT DOMAIN 255..335
FT /note="Ig-like C2-type 3"
FT DOMAIN 340..419
FT /note="Ig-like C2-type 4"
FT DOMAIN 424..520
FT /note="Ig-like C2-type 5"
FT REGION 687..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 437..439
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96J84"
FT MOD_RES 637
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000269|PubMed:18258597"
FT MOD_RES 638
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000269|PubMed:18258597"
FT MOD_RES 654
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96J84"
FT MOD_RES 657
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96J84"
FT MOD_RES 756
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96J84"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 175..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 361..403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 445..504
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 322..323
FT /note="YN -> DS (in Ref. 1; AAP78673)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="L -> V (in Ref. 1; AAP78673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 789 AA; 87241 MW; D463901B08FB34BB CRC64;
MTLENRSTCL MTCQSSLLPK KPRFLSQKMW APHLVVAYLI FVTLALALPG TQTRFSQEPA
DQTVVAGHRA VLPCVLLNYS GIVQWTKDGL ALGMGQGLKA WPRYRVVGSA DAGQYNLEIT
DAELSDDASY ECQATEAALR SRRAKLTVLI PPEDTRIDGG PVILLQAGTP YNLTCRAFNA
KPAATIIWFR DGTQQEGAVT STELLKDGKR ETTISQLLIQ PTDLDIGRVF TCRSMNEAIP
NGKETSIELD VHHPPTVTLS IEPQTVLEGE RVIFTCQATA NPEILGYRWA KGGFLIEDAH
ESRYETNVDY SFFTEPVSCE VYNKVGSTNV STLVNVHFAP RIVVYPKPTT TDIGSDVTLT
CVWVGNPPLT LTWTKKDSNM VLSNSNQLLL KSVTQADAGT YTCRAIVPRI GVAEREVPLY
VNGPPIISSE AVQFAVRGDG GKVECFIGST PPPDRIAWAW KENFLEVGTL ERYTVERTNS
GSGVLSTLTI NNVMEADFQT HYNCTAWNSF GPGTAIIQLE EREVLPVGII AGATIGAGIL
LVFSFAALVF FLYRRRKGSR KDVTLRKLDI KVETVNREPL TMHSDREDDT TSISTATRVM
KAIYSSFKDD VDLKQDLHCD TIETREEYEM KDPTNGYYNV RAHEDRPSSR AVLYADYRAP
GPTRFDGRPS SRLSHSSGYA QLNTYSRAPA SDYGTEPTPS GPSAPGGTDT TSQLSYENYE
KFNSHPFPGA AGYPTYRLGY PQAPPSGLER TPYEAYDPIG KYATATRFSY TSQHSDYGQR
FQQRMQTHV
