ID A0A2K5YY55_MANLE Unreviewed; 1040 AA.
AC A0A2K5YY55;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=NPHS1 adhesion molecule, nephrin {ECO:0000313|Ensembl:ENSMLEP00000020481.1};
GN Name=NPHS1 {ECO:0000313|Ensembl:ENSMLEP00000020481.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000020481.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000020481.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC {ECO:0000256|ARBA:ARBA00008637}.
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DR AlphaFoldDB; A0A2K5YY55; -.
DR STRING; 9568.ENSMLEP00000020481; -.
DR Ensembl; ENSMLET00000043979.1; ENSMLEP00000020481.1; ENSMLEG00000034437.1.
DR GeneTree; ENSGT00940000159510; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0017022; F:myosin binding; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0032836; P:glomerular basement membrane development; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0072015; P:podocyte development; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0036060; P:slit diaphragm assembly; IEA:Ensembl.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 8.
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 InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR11640:SF164; MAM DOMAIN-CONTAINING GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR PROTEIN 1; 1.
DR PANTHER; PTHR11640; NEPHRIN; 1.
DR Pfam; PF08205; C2-set_2; 3.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; Immunoglobulin; 8.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1040
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014434643"
FT DOMAIN 27..130
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 242..333
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 340..434
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 440..540
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 639..719
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 736..837
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 900..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 113040 MW; C928DBF47A62E0AD CRC64;
MALGTMLKAP LLLLGLLTEG LAQLAIPASV PRGFWALPEN LTVVEGASVE LRCGVSTPGS
AVQWAKDGLL LGPDPRIPGF PRYRLEGDPA RGEFHLHIEA CDLSDDAEYE CQVGRSEMGP
ELVSPRVILS VLVPPKLLYL TPEAGTVVTW VAGQEYVVSC LSGDAKPAPD ITILLSGQTI
SDISANMNEG SQQKLFTVEA TARVTPQSSD NGQLLVCEAS SPALEAPIKA SFTVNVLFPP
GPPVIEWPGL DEGHVRAGQS LELPCVAQGG NPLATLQWLK NSQPASTAWG TEHTQAVARS
VLVMTVRPED HGARLSCEAH NSVSAGTQER SIMLQVTFSP SAITILGSAS QVENKNVTLS
CVSKSSRPRV LLRWWLGWRQ LLPTEETIMD GLHGGYISMS NLTLLARRED NGLTLTCEAF
SEAFTKETFK KSLTLNVKYP AQKLWIEGAP EGQKLRAGTR VRLVCLAIGG NPEPSLTWYK
DSRTVTESRL PQEPRRMQLG NVEKSGSTFS RELVLVTGPS DNQAKFTCKA GQLSASTQLA
VQYRPEFLGE QVLVVTAVEQ GEALLPVSVS ANPAPEAFNW TFRGYRLSPA GGPRHRILSS
GALHLWNVTR ADDGLYQLHC QNSEGTAEAL LRLDVHYAPT IRALQDPTEV NVGSVDIVCT
VDANPILPGM FSWERLGEDE EDQSLDDMEK ISKGPTGRLR IHQAKLAQAG AYQCIVDNGV
APPARGLVRL VVRFAPQVEH PTPLTKVAAA GDSTSSATLH CRARGVPNIV FTWTKNGVPL
DLQDPRYTEH TYHQGGVHSS LLTIANVSAA QDYALFTCTA TNPLGSDQTN IQLVSISLDQ
PSGEPEDQLP TEPPAGPSGL PLLPVLLGLG GLLLLSNASC VGGVLWQRRL RRLAECVSGK
TEAESEDRVR NEYEESQWTG EQDTRSSTVS TTEAEPYYRS LRDFSPQLPP TQEEVSYSRG
FTGEDEDMAF PGHLYDEVER TYPRSGAWGP LYDEVQMSPW DLRWPEDAYQ DPRGIYDRVA
GDLDTLEPDS LPFELRGHLV
//
