NPNT_PONAB
ID NPNT_PONAB Reviewed; 565 AA.
AC Q5RBP1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Nephronectin;
DE Flags: Precursor;
GN Name=NPNT;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functional ligand of integrin alpha-8/beta-1 in kidney
CC development. Regulates the expression of GDNF with integrin alpha-
CC 8/beta-1 which is essential for kidney development. May also play a
CC role in the development and function of various tissues, regulating
CC cell adhesion, spreading and survival through the binding of several
CC integrins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer and homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Note=Trapped on the cell surface or in the
CC extracellular matrix. {ECO:0000250}.
CC -!- DOMAIN: The MAM domain is required for localization at the cell
CC surface. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nephronectin family. {ECO:0000305}.
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DR EMBL; CR858597; CAH90819.1; -; mRNA.
DR RefSeq; NP_001125467.1; NM_001131995.1.
DR AlphaFoldDB; Q5RBP1; -.
DR SMR; Q5RBP1; -.
DR STRING; 9601.ENSPPYP00000016729; -.
DR GeneID; 100172375; -.
DR KEGG; pon:100172375; -.
DR CTD; 255743; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; Q5RBP1; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR CDD; cd06263; MAM; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50060; MAM_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Developmental protein; Differentiation;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..565
FT /note="Nephronectin"
FT /id="PRO_0000295686"
FT DOMAIN 52..87
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 89..128
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 132..168
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 169..213
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 214..254
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 420..563
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 301..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 382..384
FT /note="Integrin interaction"
FT COMPBIAS 315..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 56..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 60..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 93..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 100..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 115..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 173..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 180..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 197..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 218..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 225..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 242..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 565 AA; 62060 MW; A4E52C361685334A CRC64;
MDFLLALVLV SSLYLQAAAE FDGRWPRQIV SSIGLCRYGG RIDCCWGWAR QSWGQCQPVC
QPRCKHGECI GPNKCKCHPG YAGKTCNQDL NECGLKPRPC KHRCMNTYGS YKCYCLNGYM
LMPDGSCSSA LTCSMANCQY GCDVVKGQIR CQCPSPGLQL APDGRTCVDV DECATGRASC
PRFRQCVNTF GSYICKCHKG FNLMYIGGKY QCHDIDECSL GQYQCSSFAR CYNIHGSYKC
KCKEGYQGDG LTCVYIPKVM IEPSGPIHVP KGNGTILKGD RGHNNWIPDV GSTWWPPKTP
YIPPIITNRP TSKPTTRPTP KPTPIPTPPP PPPLPTELRT PLPPTTPERP TPRLTSIAPA
AGTPPGGITV DNRVQTDPQK LRGDVFIPRQ PSNDLFEIFE IERGVSADDE AKDDPGILVH
SCNFDHGLCG WIREKDNDLH WEPIRDPAGG QYLTVSAAKA PGGKAARLVL PLGRLMHSGD
LCLSFRHKVT GLHSGTLQVF VRKHGAHGAA LWGRNGGHGW RQTQITLRGA DIKSVIFKGE
KRRGHTGEIG LDDVSLKKGH CSEER
