GenomeNet

Database: UniProt
Entry: Q5RBP1
LinkDB: Q5RBP1
Original site: Q5RBP1 
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   10-APR-2019, entry version 70.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
CC       a role in the development and function of various tissues,
CC       regulating cell adhesion, spreading and survival through the
CC       binding of several 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}.
DR   EMBL; CR858597; CAH90819.1; -; mRNA.
DR   RefSeq; NP_001125467.1; NM_001131995.1.
DR   UniGene; Pab.11540; -.
DR   ProteinModelPortal; Q5RBP1; -.
DR   SMR; Q5RBP1; -.
DR   STRING; 9601.ENSPPYP00000016729; -.
DR   GeneID; 100172375; -.
DR   KEGG; pon:100172375; -.
DR   CTD; 255743; -.
DR   eggNOG; ENOG410KD9N; Eukaryota.
DR   eggNOG; ENOG411039V; LUCA.
DR   HOVERGEN; HBG108200; -.
DR   InParanoid; Q5RBP1; -.
DR   KO; K06824; -.
DR   OrthoDB; 766075at2759; -.
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   GO; GO:0007275; P:multicellular organism development; 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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000998; MAM_dom.
DR   Pfam; PF07645; EGF_CA; 3.
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; Complete proteome; Developmental protein;
KW   Differentiation; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    565       Nephronectin.
FT                                /FTId=PRO_0000295686.
FT   DOMAIN       52     87       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       89    128       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      132    168       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      169    213       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      214    254       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      420    563       MAM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   MOTIF       382    384       Integrin interaction.
FT   COMPBIAS    296    365       Pro-rich.
FT   DISULFID     56     69       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     60     75       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     77     86       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     93    104       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    100    113       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    115    127       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    173    186       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    180    195       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    197    212       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    218    231       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    225    240       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    242    253       {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
//
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