PODO_MOUSE
ID PODO_MOUSE Reviewed; 385 AA.
AC Q91X05; Q8BWE6; Q91Z95;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Podocin;
GN Name=Nphs2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=11733557; DOI=10.1172/jci200112849;
RA Schwarz K., Simons M., Reiser J., Saleem M.A., Faul C., Kriz W., Shaw A.S.,
RA Holzman L.B., Mundel P.;
RT "Podocin, a raft-associated component of the glomerular slit diaphragm,
RT interacts with CD2AP and nephrin.";
RL J. Clin. Invest. 108:1621-1629(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11562357; DOI=10.1074/jbc.c100452200;
RA Huber T.B., Kottgen M., Schilling B., Walz G., Benzing T.;
RT "Interaction with podocin facilitates nephrin signaling.";
RL J. Biol. Chem. 276:41543-41546(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-377.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP INTERACTION WITH KIRRL1.
RC STRAIN=Swiss Webster; TISSUE=Brain;
RX PubMed=12424224; DOI=10.1096/fj.02-0242fje;
RA Sellin L., Huber T.B., Gerke P., Quack I., Pavenstaedt H., Walz G.;
RT "NEPH1 defines a novel family of podocin interacting proteins.";
RL FASEB J. 17:115-117(2003).
RN [6]
RP INTERACTION WITH DDN.
RX PubMed=17537921; DOI=10.1073/pnas.0700917104;
RA Asanuma K., Campbell K.N., Kim K., Faul C., Mundel P.;
RT "Nuclear relocation of the nephrin and CD2AP-binding protein dendrin
RT promotes apoptosis of podocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10134-10139(2007).
CC -!- FUNCTION: Plays a role in the regulation of glomerular permeability,
CC acting probably as a linker between the plasma membrane and the
CC cytoskeleton. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with nephrin/NPHS1, KIRRL1 and CD2AP. Interacts with
CC DDN. {ECO:0000269|PubMed:12424224, ECO:0000269|PubMed:17537921}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
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DR EMBL; AJ302048; CAC44636.1; -; mRNA.
DR EMBL; AY050309; AAL06146.1; -; mRNA.
DR EMBL; BC067401; AAH67401.1; -; mRNA.
DR EMBL; AK052746; BAC35128.1; -; mRNA.
DR CCDS; CCDS15391.1; -.
DR RefSeq; NP_569723.1; NM_130456.4.
DR AlphaFoldDB; Q91X05; -.
DR SMR; Q91X05; -.
DR BioGRID; 228352; 64.
DR DIP; DIP-61266N; -.
DR IntAct; Q91X05; 7.
DR STRING; 10090.ENSMUSP00000027896; -.
DR iPTMnet; Q91X05; -.
DR PhosphoSitePlus; Q91X05; -.
DR jPOST; Q91X05; -.
DR PaxDb; Q91X05; -.
DR PRIDE; Q91X05; -.
DR ProteomicsDB; 289716; -.
DR Antibodypedia; 34420; 133 antibodies from 31 providers.
DR DNASU; 170484; -.
DR Ensembl; ENSMUST00000027896; ENSMUSP00000027896; ENSMUSG00000026602.
DR GeneID; 170484; -.
DR KEGG; mmu:170484; -.
DR UCSC; uc007dch.1; mouse.
DR CTD; 7827; -.
DR MGI; MGI:2157018; Nphs2.
DR VEuPathDB; HostDB:ENSMUSG00000026602; -.
DR eggNOG; KOG2621; Eukaryota.
DR GeneTree; ENSGT01030000234614; -.
DR InParanoid; Q91X05; -.
DR OMA; SVTCVWG; -.
DR OrthoDB; 1062075at2759; -.
DR PhylomeDB; Q91X05; -.
DR TreeFam; TF105750; -.
DR Reactome; R-MMU-373753; Nephrin family interactions.
DR BioGRID-ORCS; 170484; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Nphs2; mouse.
DR PRO; PR:Q91X05; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91X05; protein.
DR Bgee; ENSMUSG00000026602; Expressed in renal glomerulus and 39 other tissues.
DR ExpressionAtlas; Q91X05; baseline and differential.
DR Genevisible; Q91X05; MM.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0036057; C:slit diaphragm; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0072249; P:metanephric podocyte development; IEA:Ensembl.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR043202; Band-7_stomatin-like.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR PANTHER; PTHR10264; PTHR10264; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..385
FT /note="Podocin"
FT /id="PRO_0000094036"
FT TOPO_DOM 1..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..385
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 103
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 3..4
FT /note="SR -> FF (in Ref. 1; CAC44636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42337 MW; 02B07F21FB98A0BC CRC64;
MDSRARSSSR EAHGRSSRSS SRDDKKAKAG RGSRGRARPD AGAERQSTGR TATRGEPRAP
AATATVVDVD EVRGPGEEGT EVVALLESER PEEGIKPSGL GACEWLLVLA SLIFIIMTFP
FSIWFCIKVV QEYERVIIFR LGHLLPGRAK GPGLFFFLPC LDTYHKVDLR LQTLEIPFHE
VVTKDMFIME IDAVCYYRME NASLLLSSLA HVSKAIQFLV QTTMKRLLAH RSLTEILLER
KSIAQDVKVA LDAVTCIWGI KVERTEIKDV RLPAGLQHSL AVEAEAQRQA KVRVIAAEGE
KAASESLRMA AEILSGTPAA VQLRYLHTLQ SLSTEKPATV VLPLPFDMLS LLSSPGNRAQ
GSINYPSSSK PVEPLNPKKK DSPML
