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   25-MAY-2022, entry version 71.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 vascular
CC       development. {ECO:0000250}.
CC   -!- SUBUNIT: May form a homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
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DR   EMBL; CR858764; CAH90971.1; -; mRNA.
DR   EMBL; CR859277; CAH91455.1; -; mRNA.
DR   RefSeq; NP_001125560.1; NM_001132088.1.
DR   AlphaFoldDB; Q5RB89; -.
DR   SMR; Q5RB89; -.
DR   STRING; 9601.ENSPPYP00000005528; -.
DR   GeneID; 100172474; -.
DR   KEGG; pon:100172474; -.
DR   CTD; 59277; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   InParanoid; Q5RB89; -.
DR   OrthoDB; 236390at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   CDD; cd00055; EGF_Lam; 3.
DR   CDD; cd03578; NTR_netrin-4_like; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
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   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..628
FT                   /note="Netrin-4"
FT                   /id="PRO_0000042118"
FT   DOMAIN          30..261
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          262..331
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          332..394
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          395..448
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          506..627
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        262..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        264..293
FT                   /evidence="ECO:0000250"
FT   DISULFID        295..304
FT                   /evidence="ECO:0000250"
FT   DISULFID        307..329
FT                   /evidence="ECO:0000250"
FT   DISULFID        332..341
FT                   /evidence="ECO:0000250"
FT   DISULFID        334..359
FT                   /evidence="ECO:0000250"
FT   DISULFID        362..371
FT                   /evidence="ECO:0000250"
FT   DISULFID        374..392
FT                   /evidence="ECO:0000250"
FT   DISULFID        395..413
FT                   /evidence="ECO:0000250"
FT   DISULFID        397..420
FT                   /evidence="ECO:0000250"
FT   DISULFID        422..431
FT                   /evidence="ECO:0000250"
FT   DISULFID        434..446
FT                   /evidence="ECO:0000250"
FT   DISULFID        506..576
FT                   /evidence="ECO:0000250"
FT   DISULFID        520..627
FT                   /evidence="ECO:0000250"
FT   CONFLICT        475
FT                   /note="F -> V (in Ref. 1; CAH91455)"
FT                   /evidence="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