GenomeNet

Database: UniProt
Entry: Q9HB63
LinkDB: Q9HB63
Original site: Q9HB63 
ID   NET4_HUMAN              Reviewed;         628 AA.
AC   Q9HB63; B2RNC2; Q658K9; Q7L3F1; Q7L9D6; Q7Z5B6; Q9BZP1; Q9NT44;
AC   Q9P133;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   13-FEB-2019, entry version 146.
DE   RecName: Full=Netrin-4;
DE   AltName: Full=Beta-netrin;
DE   AltName: Full=Hepar-derived netrin-like protein;
DE   Flags: Precursor;
GN   Name=NTN4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11038171; DOI=10.1083/jcb.151.2.221;
RA   Koch M., Murrell J.R., Hunter D.D., Olson P.F., Jin W., Keene D.R.,
RA   Brunken W.J., Burgeson R.E.;
RT   "A novel member of the netrin family, beta-netrin, shares homology
RT   with the beta chain of laminin. Identification, expression, and
RT   functional characterization.";
RL   J. Cell Biol. 151:221-234(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Niranjan B., Hohenester E., Slade M., Ali S., Kamalati T.,
RA   Buluwela L.;
RT   "Identification of a novel member of the netrin family, which is
RT   induced during in vitro mammary tubule morphogenesis.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Fetal liver;
RA   Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M.,
RA   He F.;
RT   "Hetrin, an alternative splicing form of beta-netrin.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Li H., Zhou G., Shen C., Li M., Xiao W., Zhong G., Zheng G., Yu R.,
RA   Ke R., Zhong J., Huang F., Lin L., Yang S.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 160-628 (ISOFORMS 1/3).
RC   TISSUE=Brain, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-628 (ISOFORMS 1/3).
RC   TISSUE=Stomach;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-628 (ISOFORMS 1/3).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
CC   -!- FUNCTION: May play an important role in neural, kidney and
CC       vascular development. Promotes neurite elongation from olfactory
CC       bulb explants. {ECO:0000269|PubMed:11038171}.
CC   -!- SUBUNIT: May form a homodimer.
CC   -!- INTERACTION:
CC       P26371:KRTAP5-9; NbExp=3; IntAct=EBI-743459, EBI-3958099;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000269|PubMed:11038171}.
CC       Note=Major component.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9HB63-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HB63-2; Sequence=VSP_015746;
CC         Note=No experimental confirmation available.;
CC       Name=3; Synonyms=Hetrin;
CC         IsoId=Q9HB63-3; Sequence=VSP_015745;
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, spleen, mammary gland,
CC       aorta, heart, ovary, prostate and fetal spleen.
CC       {ECO:0000269|PubMed:11038171}.
DR   EMBL; AF278532; AAG30822.1; -; mRNA.
DR   EMBL; AF297711; AAG53651.1; -; mRNA.
DR   EMBL; AF119916; AAF69670.2; -; mRNA.
DR   EMBL; AY330211; AAP92113.1; -; mRNA.
DR   EMBL; AL137540; CAB70800.3; -; mRNA.
DR   EMBL; CH471054; EAW97544.1; -; Genomic_DNA.
DR   EMBL; BC013591; AAH13591.2; -; mRNA.
DR   EMBL; BC136798; AAI36799.1; -; mRNA.
DR   EMBL; BC136799; AAI36800.1; -; mRNA.
DR   EMBL; AL833767; CAH56243.1; -; mRNA.
DR   EMBL; AK024691; BAB14964.1; -; mRNA.
DR   CCDS; CCDS86324.1; -. [Q9HB63-3]
DR   CCDS; CCDS86325.1; -. [Q9HB63-2]
DR   CCDS; CCDS9054.1; -. [Q9HB63-1]
DR   PIR; T46383; T46383.
DR   RefSeq; NP_001316629.1; NM_001329700.1. [Q9HB63-2]
DR   RefSeq; NP_001316630.1; NM_001329701.1. [Q9HB63-3]
DR   RefSeq; NP_001316631.1; NM_001329702.1. [Q9HB63-3]
DR   RefSeq; NP_067052.2; NM_021229.3. [Q9HB63-1]
DR   UniGene; Hs.201034; -.
DR   ProteinModelPortal; Q9HB63; -.
DR   SMR; Q9HB63; -.
DR   BioGrid; 121866; 8.
DR   DIP; DIP-46274N; -.
DR   IntAct; Q9HB63; 19.
DR   MINT; Q9HB63; -.
DR   STRING; 9606.ENSP00000340998; -.
DR   iPTMnet; Q9HB63; -.
DR   PhosphoSitePlus; Q9HB63; -.
DR   BioMuta; NTN4; -.
DR   DMDM; 76789662; -.
DR   MaxQB; Q9HB63; -.
DR   PaxDb; Q9HB63; -.
DR   PeptideAtlas; Q9HB63; -.
DR   PRIDE; Q9HB63; -.
DR   ProteomicsDB; 81495; -.
DR   ProteomicsDB; 81496; -. [Q9HB63-2]
DR   ProteomicsDB; 81497; -. [Q9HB63-3]
DR   Ensembl; ENST00000343702; ENSP00000340998; ENSG00000074527. [Q9HB63-1]
DR   Ensembl; ENST00000344911; ENSP00000339436; ENSG00000074527. [Q9HB63-3]
DR   Ensembl; ENST00000538383; ENSP00000444432; ENSG00000074527. [Q9HB63-3]
DR   Ensembl; ENST00000553059; ENSP00000447292; ENSG00000074527. [Q9HB63-2]
DR   GeneID; 59277; -.
DR   KEGG; hsa:59277; -.
DR   UCSC; uc001tei.3; human. [Q9HB63-1]
DR   CTD; 59277; -.
DR   DisGeNET; 59277; -.
DR   EuPathDB; HostDB:ENSG00000074527.11; -.
DR   GeneCards; NTN4; -.
DR   HGNC; HGNC:13658; NTN4.
DR   HPA; HPA049832; -.
DR   MIM; 610401; gene.
DR   neXtProt; NX_Q9HB63; -.
DR   OpenTargets; ENSG00000074527; -.
DR   PharmGKB; PA31815; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   eggNOG; ENOG410XPEG; LUCA.
DR   GeneTree; ENSGT00940000156615; -.
DR   HOVERGEN; HBG082019; -.
DR   InParanoid; Q9HB63; -.
DR   KO; K06845; -.
DR   OMA; KPQHFTH; -.
DR   OrthoDB; 236390at2759; -.
DR   PhylomeDB; Q9HB63; -.
DR   TreeFam; TF352481; -.
DR   Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-HSA-373752; Netrin-1 signaling.
DR   SIGNOR; Q9HB63; -.
DR   ChiTaRS; NTN4; human.
DR   GenomeRNAi; 59277; -.
DR   PRO; PR:Q9HB63; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000074527; Expressed in 194 organ(s), highest expression level in layer of synovial tissue.
DR   ExpressionAtlas; Q9HB63; baseline and differential.
DR   Genevisible; Q9HB63; HS.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043237; F:laminin-1 binding; IEA:Ensembl.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0016322; P:neuron remodeling; IEA:Ensembl.
DR   GO; GO:0060668; P:regulation of branching involved in salivary gland morphogenesis by extracellular matrix-epithelial cell signaling; IEA:Ensembl.
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   1: Evidence at protein level;
KW   Alternative splicing; Basement membrane; Complete proteome;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Polymorphism; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    628       Netrin-4.
FT                                /FTId=PRO_0000042116.
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   VAR_SEQ       1     37       Missing (in isoform 3).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_015745.
FT   VAR_SEQ     504    526       Missing (in isoform 2).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_015746.
FT   VARIANT     205    205       Y -> H (in dbSNP:rs17288108).
FT                                /FTId=VAR_023548.
FT   CONFLICT     68     68       T -> K (in Ref. 1; AAG30822).
FT                                {ECO:0000305}.
FT   CONFLICT    161    161       A -> G (in Ref. 3; AAF69670).
FT                                {ECO:0000305}.
FT   CONFLICT    222    222       T -> I (in Ref. 4; AAP92113).
FT                                {ECO:0000305}.
FT   CONFLICT    331    331       T -> A (in Ref. 1 and 4). {ECO:0000305}.
FT   CONFLICT    462    462       C -> R (in Ref. 4; AAP92113).
FT                                {ECO:0000305}.
FT   CONFLICT    472    472       Y -> C (in Ref. 1; AAG30822).
FT                                {ECO:0000305}.
FT   CONFLICT    472    472       Y -> H (in Ref. 4; AAP92113).
FT                                {ECO:0000305}.
FT   CONFLICT    545    545       N -> S (in Ref. 4; AAP92113).
FT                                {ECO:0000305}.
SQ   SEQUENCE   628 AA;  70071 MW;  275613B63A39B267 CRC64;
     MGSCARLLLL WGCTVVAAGL SGVAGVSSRC EKACNPRMGN LALGRKLWAD TTCGQNATEL
     YCFYSENTDL TCRQPKCDKC NAAYPHLAHL PSAMADSSFR FPRTWWQSAE DVHREKIQLD
     LEAEFYFTHL IVMFKSPRPA AMVLDRSQDF GKTWKPYKYF ATNCSATFGL EDDVVKKGAI
     CTSKYSSPFP CTGGEVIFKA LSPPYDTENP YSAKVQEQLK ITNLRVQLLK RQSCPCQRND
     LNEEPQHFTH YAIYDFIVKG SCFCNGHADQ CIPVHGFRPV KAPGTFHMVH GKCMCKHNTA
     GSHCQHCAPL YNDRPWEAAD GKTGAPNECR TCKCNGHADT CHFDVNVWEA SGNRSGGVCD
     DCQHNTEGQY CQRCKPGFYR DLRRPFSAPD ACKPCSCHPV GSAVLPANSV TFCDPSNGDC
     PCKPGVAGRR CDRCMVGYWG FGDYGCRPCD CAGSCDPITG DCISSHTDID WYHEVPDFRP
     VHNKSEPAWE WEDAQGFSAL LHSGKCECKE QTLGNAKAFC GMKYSYVLKI KILSAHDKGT
     HVEVNVKIKK VLKSTKLKIF RGKRTLYPES WTDRGCTCPI LNPGLEYLVA GHEDIRTGKL
     IVNMKSFVQH WKPSLGRKVM DILKRECK
//
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