GenomeNet

Database: UniProt
Entry: Q5RB89
LinkDB: Q5RB89
Original site: Q5RB89 
ID   NET4_PONAB              Reviewed;         628 AA.
AC   Q5RB89; Q5R9V5;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=Netrin-4;
DE   Flags: Precursor;
GN   Name=NTN4;
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=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play an important role in neural, kidney and
CC       vascular development. {ECO:0000250}.
CC   -!- SUBUNIT: May form a homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
DR   EMBL; CR858764; CAH90971.1; -; mRNA.
DR   EMBL; CR859277; CAH91455.1; -; mRNA.
DR   RefSeq; NP_001125560.1; NM_001132088.1.
DR   UniGene; Pab.19164; -.
DR   UniGene; Pab.8196; -.
DR   ProteinModelPortal; Q5RB89; -.
DR   SMR; Q5RB89; -.
DR   STRING; 9601.ENSPPYP00000005528; -.
DR   GeneID; 100172474; -.
DR   KEGG; pon:100172474; -.
DR   CTD; 59277; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   eggNOG; ENOG410XPEG; LUCA.
DR   HOVERGEN; HBG082019; -.
DR   InParanoid; Q5RB89; -.
DR   KO; K06845; -.
DR   OrthoDB; 236390at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   CDD; cd03578; NTR_netrin-4_like; 1.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   InterPro; IPR035811; Netrin-4_NTR.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR018933; Netrin_module_non-TIMP.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   Pfam; PF00053; Laminin_EGF; 3.
DR   Pfam; PF00055; Laminin_N; 1.
DR   Pfam; PF01759; NTR; 1.
DR   SMART; SM00643; C345C; 1.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF50242; SSF50242; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 2.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   PROSITE; PS50189; NTR; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    628       Netrin-4.
FT                                /FTId=PRO_0000042118.
FT   DOMAIN       30    261       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      262    331       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      332    394       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      395    448       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      506    627       NTR. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00295}.
FT   CARBOHYD     56     56       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    163    163       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    353    353       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    483    483       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    262    271       {ECO:0000250}.
FT   DISULFID    264    293       {ECO:0000250}.
FT   DISULFID    295    304       {ECO:0000250}.
FT   DISULFID    307    329       {ECO:0000250}.
FT   DISULFID    332    341       {ECO:0000250}.
FT   DISULFID    334    359       {ECO:0000250}.
FT   DISULFID    362    371       {ECO:0000250}.
FT   DISULFID    374    392       {ECO:0000250}.
FT   DISULFID    395    413       {ECO:0000250}.
FT   DISULFID    397    420       {ECO:0000250}.
FT   DISULFID    422    431       {ECO:0000250}.
FT   DISULFID    434    446       {ECO:0000250}.
FT   DISULFID    506    576       {ECO:0000250}.
FT   DISULFID    520    627       {ECO:0000250}.
FT   CONFLICT    475    475       F -> V (in Ref. 1; CAH91455).
FT                                {ECO:0000305}.
SQ   SEQUENCE   628 AA;  69972 MW;  D22F95E61E473A7E CRC64;
     MGSCARLLLL WGCTVVAAGL SGVAGVSSRC EKACNPRMGN LALGRKLWAD TTCGQNATEL
     YCFYSENTDL TCRQPKCDKC NAAHPHLAHL PSAMADSSFR FPRTWWQSAE DVHREKIQLD
     LEAEFYFTHL IMMFKSPRPA AMVLDRSQDF GKTWKPYKYF ATNCSATFGL EDDVVKKGAI
     CTSKYSSPFP CTGGEVIFKA LSPPYDTENP YSAKVQEQLK ITNLRVQLLK RQSCPCQRND
     LNDEPQHFTH YAIYDFIVKG SCFCNGHADQ CIPVHGFRPV KAPGTFHMVH GKCMCKHNTA
     GSHCQHCAPL YNDQPWEAAD GKTGAPNECR TCKCNGHADT CHFDVNVWEA SGNRSGGVCD
     DCQHNTEGQH CQRCKPGFYR DLRRPFSAPD ACKPCSCHPV GSAVLPANSV TFCDPSNGDC
     PCKPGVAGRH CDRCMVGYWG FGDYGCRPCD CAGSCDPITG DCISSHTDID WHHEFPDFRP
     VHNKSEAAWE WEDAQGFSAL LHSGKCECKE QTLGNAKAFC GMKYSYVLKI KILSAHDKGT
     HVEVNVKIKK VLKSTKLKIF RGKRTLYPES WTDRGCTCPI LNPGLEYLVA GHEDVRTGKL
     IVNMKSFVQH WKPSLGRKVM DILKRECK
//
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