NPHN_HUMAN » Nephrin

NPHN_HUMAN » Nephrin
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
NPHN_HUMAN » Nephrin » Renal glomerulus-specific cell adhesion receptor;
Hydrophobic Thickness 30.4 ± 2.7 Å
Tilt Angle 16 ± 0°
ΔGtransfer -19.4 kcal/mol
ΔGfold -7.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, Reactome
Topology Out
TM Segments 1059-1078 (1059-1079)
Pathways

Cell-Cell communication (Reactome)

PDB none
OPM none
Complexes none
Interactions

CALX, Complex: NPHN:CALX

KIRR1, Complex: NPHN:KIRR1, PubMed

Domains

AA: 37-127, PDBID: 4OFI, Subunit D, Seq Identity:36%, Immunoglobulin V-set domain

AA: 138-228, PDBID: 4OF8, Subunit B, Seq Identity:22%, CD80-like C2-set immunoglobulin domain

AA: 243-328, PDBID: 3BP5, Subunit B, Seq Identity:36%, CD80-like C2-set immunoglobulin domain

AA: 344-428, PDBID: 3CJJ, Subunit A, Seq Identity:24%, CD80-like C2-set immunoglobulin domain

AA: 444-538, PDBID: 4OFY, Subunit F, Seq Identity:22%, CD80-like C2-set immunoglobulin domain

AA: 548-634, PDBID: 3CJJ, Subunit A, Seq Identity:26%, CD80-like C2-set immunoglobulin domain

AA: 739-820, PDBID: 2EO9, Subunit A, Seq Identity:28%, Immunoglobulin domain

AA: 838-924, PDBID: 2OM5, Subunit A, Seq Identity:35%, Immunoglobulin domain

AA: 942-1025, PDBID: 2EKJ, Subunit A, Seq Identity:36%, Fibronectin type III domain

UniProt annotation for NPHN_HUMAN » Nephrin
FUNCTION: Seems to play a role in the development or function of the kidney glomerular filtration barrier. Regulates glomerular vascular permeability. May anchor the podocyte slit diaphragm to the actin cytoskeleton. Plays a role in skeletal muscle formation through regulation of myoblast fusion (By similarity).

SUBUNIT: Interacts with CD2AP (via C-terminal domain). Interacts with MAGI1 (via PDZ 2 and 3 domains) forming a tripartite complex with IGSF5/JAM4. Interacts with DDN; the interaction is direct. Self-associates (via the Ig-like domains). Also interacts (via the Ig-like domains) with KIRREL/NEPH1 and KIRREL2; the interaction with KIRREL is dependent on KIRREL glycosylation. Forms a complex with ACTN4, CASK, IQGAP1, MAGI2, SPTAN1 and SPTBN1 (By similarity). Interacts with NPHS2.

TISSUE SPECIFICITY: Specifically expressed in podocytes of kidney glomeruli.

DEVELOPMENTAL STAGE: In 23-week-old embryo found in epithelial podocytes of the periphery of mature and developing glomeruli.

DISEASE: Nephrotic syndrome 1 (NPHS1) OMIM: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. mutations affecting the gene represented in this entry.

UniProt features for NPHN_HUMAN » Nephrin
SIGNAL 1 22 Potential.
CHAIN 23 1241 Nephrin.
DOMAIN 27 130 Ig-like C2-type 1.
DOMAIN 143 234 Ig-like C2-type 2.
DOMAIN 242 333 Ig-like C2-type 3.
DOMAIN 340 434 Ig-like C2-type 4.
DOMAIN 440 540 Ig-like C2-type 5.
DOMAIN 544 635 Ig-like C2-type 6.
DOMAIN 740 832 Ig-like C2-type 7.
DOMAIN 838 939 Ig-like C2-type 8.
DOMAIN 941 1035 Fibronectin type-III.
REGION 1160 1241 Binds to NPHS2.
DISULFID 53 111 Potential.
DISULFID 160 217 Potential.
DISULFID 265 317 Potential.
DISULFID 361 417 Potential.
DISULFID 465 528 Potential.
DISULFID 567 623 Potential.
DISULFID 761 816 Potential.
DISULFID 863 920 Potential.
Amino Acid Sequence for NPHN_HUMAN » Nephrin
MALGTTLRAS LLLLGLLTEG LAQLAIPASV PRGFWALPEN LTVVEGASVE LRCGVSTPGS AVQWAKDGLL LGPDPRIPGF PRYRLEGDPA RGEFHLHIEA CDLSDDAEYE CQVGRSEMGP ELVSPRVILS ILVPPKLLLL TPEAGTMVTW VAGQEYVVNC VSGDAKPAPD ITILLSGQTI SDISANVNEG SQQKLFTVEA TARVTPRSSD NRQLLVCEAS SPALEAPIKA SFTVNVLFPP GPPVIEWPGL DEGHVRAGQS LELPCVARGG NPLATLQWLK NGQPVSTAWG TEHTQAVARS VLVMTVRPED HGAQLSCEAH NSVSAGTQEH GITLQVTFPP SAIIILGSAS QTENKNVTLS CVSKSSRPRV LLRWWLGWRQ LLPMEETVMD GLHGGHISMS NLTFLARRED NGLTLTCEAF SEAFTKETFK KSLILNVKYP AQKLWIEGPP EGQKLRAGTR VRLVCLAIGG NPEPSLMWYK DSRTVTESRL PQESRRVHLG SVEKSGSTFS RELVLVTGPS DNQAKFTCKA GQLSASTQLA VQFPPTNVTI LANASALRPG DALNLTCVSV SSNPPVNLSW DKEGERLEGV AAPPRRAPFK GSAAARSVLL QVSSRDHGQR VTCRAHSAEL RETVSSFYRL NVLYRPEFLG EQVLVVTAVE QGEALLPVSV SANPAPEAFN WTFRGYRLSP AGGPRHRILS SGALHLWNVT RADDGLYQLH CQNSEGTAEA RLRLDVHYAP TIRALQDPTE VNVGGSVDIV CTVDANPILP GMFNWERLGE DEEDQSLDDM EKISRGPTGR LRIHHAKLAQ AGAYQCIVDN GVAPPARRLL RLVVRFAPQV EHPTPLTKVA AAGDSTSSAT LHCRARGVPN IVFTWTKNGV PLDLQDPRYT EHTYHQGGVH SSLLTIANVS AAQDYALFTC TATNALGSDQ TNIQLVSISR PDPPSGLKVV SLTPHSVGLE WKPGFDGGLP QRFCIRYEAL GTPGFHYVDV VPPQATTFTL TGLQPSTRYR VWLLASNALG DSGLADKGTQ LPITTPGLHQ PSGEPEDQLP TEPPSGPSGL PLLPVLFALG GLLLLSNASC VGGVLWQRRL RRLAEGISEK TEAGSEEDRV RNEYEESQWT GERDTQSSTV STTEAEPYYR SLRDFSPQLP PTQEEVSYSR GFTGEDEDMA FPGHLYDEVE RTYPPSGAWG PLYDEVQMGP WDLHWPEDTY QDPRGIYDQV AGDLDTLEPD SLPFELRGHL V