NINJ1_MOUSE
ID NINJ1_MOUSE Reviewed; 152 AA.
AC O70131;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ninjurin-1 {ECO:0000303|PubMed:24347169};
DE AltName: Full=Nerve injury-induced protein 1 {ECO:0000303|PubMed:9465296};
DE Contains:
DE RecName: Full=Secreted ninjurin-1 {ECO:0000305};
DE AltName: Full=Soluble ninjurin-1 {ECO:0000303|PubMed:32883094};
DE Short=sNinJ1 {ECO:0000303|PubMed:32883094};
GN Name=Ninj1 {ECO:0000303|PubMed:33472215, ECO:0000312|MGI:MGI:1196617};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=9465296; DOI=10.1006/geno.1997.5084;
RA Chadwick B.P., Heath S.K., Williamson J., Obermayr F., Patel L., Sheer D.,
RA Frischauf A.-M.;
RT "The human homologue of the ninjurin gene maps to the candidate region of
RT hereditary sensory neuropathy type I (HSNI).";
RL Genomics 47:58-63(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Moon A.R., Kim J.W., Hong Y.M., Oh G.T., Chang S.Y., Lee K.S., Choe I.S.;
RT "Mus musculus ninjurin genomic DNA.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=19557008; DOI=10.1038/cdd.2009.78;
RA Lee H.J., Ahn B.J., Shin M.W., Jeong J.W., Kim J.H., Kim K.W.;
RT "Ninjurin1 mediates macrophage-induced programmed cell death during early
RT ocular development.";
RL Cell Death Differ. 16:1395-1407(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION (SECRETED NINJURIN-1), SUBCELLULAR LOCATION (SECRETED NINJURIN-1),
RP AND PROTEOLYTIC CLEAVAGE.
RX PubMed=23142597; DOI=10.1016/j.bbrc.2012.10.099;
RA Ahn B.J., Le H., Shin M.W., Bae S.J., Lee E.J., Wee H.J., Cha J.H.,
RA Park J.H., Lee H.S., Lee H.J., Jung H., Park Z.Y., Park S.H., Han B.W.,
RA Seo J.H., Lo E.H., Kim K.W.;
RT "The N-terminal ectodomain of Ninjurin1 liberated by MMP9 has chemotactic
RT activity.";
RL Biochem. Biophys. Res. Commun. 428:438-444(2012).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=23690620; DOI=10.1073/pnas.1221242110;
RA Cho S.J., Rossi A., Jung Y.S., Yan W., Liu G., Zhang J., Zhang M., Chen X.;
RT "Ninjurin1, a target of p53, regulates p53 expression and p53-dependent
RT cell survival, senescence, and radiation-induced mortality.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:9362-9367(2013).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24347169; DOI=10.1074/jbc.m113.498212;
RA Ahn B.J., Le H., Shin M.W., Bae S.J., Lee E.J., Wee H.J., Cha J.H.,
RA Lee H.J., Lee H.S., Kim J.H., Kim C.Y., Seo J.H., Lo E.H., Jeon S.,
RA Lee M.N., Oh G.T., Yin G.N., Ryu J.K., Suh J.K., Kim K.W.;
RT "Ninjurin1 deficiency attenuates susceptibility of experimental autoimmune
RT encephalomyelitis in mice.";
RL J. Biol. Chem. 289:3328-3338(2014).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24917672; DOI=10.1074/jbc.m113.532358;
RA Ahn B.J., Le H., Shin M.W., Bae S.J., Lee E.J., Lee S.Y., Yang J.H.,
RA Wee H.J., Cha J.H., Seo J.H., Lee H.S., Lee H.J., Arai K., Lo E.H.,
RA Jeon S., Oh G.T., Kim W.J., Ryu J.K., Suh J.K., Kim K.W.;
RT "Ninjurin1 enhances the basal motility and transendothelial migration of
RT immune cells by inducing protrusive membrane dynamics.";
RL J. Biol. Chem. 289:21926-21936(2014).
RN [9]
RP FUNCTION.
RX PubMed=24979788; DOI=10.1073/pnas.1403471111;
RA Yin G.N., Choi M.J., Kim W.J., Kwon M.H., Song K.M., Park J.M., Das N.D.,
RA Kwon K.D., Batbold D., Oh G.T., Koh G.Y., Kim K.W., Ryu J.K., Suh J.K.;
RT "Inhibition of Ninjurin 1 restores erectile function through dual
RT angiogenic and neurotrophic effects in the diabetic mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2731-E2740(2014).
RN [10]
RP FUNCTION.
RX PubMed=25860173; DOI=10.1165/rcmb.2014-0354oc;
RA Jennewein C., Sowa R., Faber A.C., Dildey M., von Knethen A., Meybohm P.,
RA Scheller B., Droese S., Zacharowski K.;
RT "Contribution of Ninjurin1 to Toll-like receptor 4 signaling and systemic
RT inflammation.";
RL Am. J. Respir. Cell Mol. Biol. 53:656-663(2015).
RN [11]
RP FUNCTION.
RX PubMed=25766274; DOI=10.1253/circj.cj-14-1376;
RA Matsuki M., Kabara M., Saito Y., Shimamura K., Minoshima A., Nishimura M.,
RA Aonuma T., Takehara N., Hasebe N., Kawabe J.;
RT "Ninjurin1 is a novel factor to regulate angiogenesis through the function
RT of pericytes.";
RL Circ. J. 79:1363-1371(2015).
RN [12]
RP FUNCTION.
RX PubMed=26677008; DOI=10.3892/ijo.2015.3296;
RA Shin M.W., Bae S.J., Wee H.J., Lee H.J., Ahn B.J., Le H., Lee E.J.,
RA Kim R.H., Lee H.S., Seo J.H., Park J.H., Kim K.W.;
RT "Ninjurin1 regulates lipopolysaccharide-induced inflammation through direct
RT binding.";
RL Int. J. Oncol. 48:821-828(2016).
RN [13]
RP SUBUNIT, GLYCOSYLATION AT ASN-60, AND MUTAGENESIS OF ASN-60.
RX PubMed=28067406; DOI=10.1002/jcb.25872;
RA Bae S.J., Shin M.W., Kim R.H., Shin D., Son T., Wee H.J., Kim K.W.;
RT "Ninjurin1 assembles into a homomeric protein complex maintained by N-
RT linked glycosylation.";
RL J. Cell. Biochem. 118:2219-2230(2017).
RN [14]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27815839; DOI=10.1007/s12035-016-0207-6;
RA Le H., Ahn B.J., Lee H.S., Shin A., Chae S., Lee S.Y., Shin M.W., Lee E.J.,
RA Cha J.H., Son T., Seo J.H., Wee H.J., Lee H.J., Jang Y., Lo E.H., Jeon S.,
RA Oh G.T., Kim D., Kim K.W.;
RT "Disruption of Ninjurin1 leads to repetitive and anxiety-like behaviors in
RT mice.";
RL Mol. Neurobiol. 54:7353-7368(2017).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29073078; DOI=10.1073/pnas.1711814114;
RA Yang H.J., Zhang J., Yan W., Cho S.J., Lucchesi C., Chen M., Huang E.C.,
RA Scoumanne A., Zhang W., Chen X.;
RT "Ninjurin 1 has two opposing functions in tumorigenesis in a p53-dependent
RT manner.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:11500-11505(2017).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30354207; DOI=10.1161/atvbaha.118.311375;
RA Minoshima A., Kabara M., Matsuki M., Yoshida Y., Kano K., Tomita Y.,
RA Hayasaka T., Horiuchi K., Saito Y., Aonuma T., Nishimura M., Maruyama K.,
RA Nakagawa N., Sawada J., Takehara N., Hasebe N., Kawabe J.I.;
RT "Pericyte-specific ninjurin1 deletion attenuates vessel maturation and
RT blood flow recovery in hind limb ischemia.";
RL Arterioscler. Thromb. Vasc. Biol. 38:2358-2370(2018).
RN [17]
RP FUNCTION.
RX PubMed=30510259; DOI=10.1038/s41598-018-35997-x;
RA Choi S., Woo J.K., Jang Y.S., Kang J.H., Hwang J.I., Seong J.K., Yoon Y.S.,
RA Oh S.H.;
RT "Ninjurin1 plays a crucial role in pulmonary fibrosis by promoting
RT interaction between macrophages and alveolar epithelial cells.";
RL Sci. Rep. 8:17542-17542(2018).
RN [18]
RP FUNCTION.
RX PubMed=31526566; DOI=10.1016/j.bbrc.2019.09.007;
RA Tomita Y., Horiuchi K., Kano K., Tatsukawa T., Matsuo R., Hayasaka T.,
RA Yoshida Y., Kabara M., Yasuda S., Nakajima K., Nakagawa N., Takehara N.,
RA Okizaki A., Hasebe N., Kawabe J.I.;
RT "Ninjurin 1 mediates peripheral nerve regeneration through Schwann cell
RT maturation of NG2-positive cells.";
RL Biochem. Biophys. Res. Commun. 519:462-468(2019).
RN [19]
RP FUNCTION.
RX PubMed=30700695; DOI=10.1038/s12276-018-0201-3;
RA Bae S.J., Shin M.W., Son T., Lee H.S., Chae J.S., Jeon S., Oh G.T.,
RA Kim K.W.;
RT "Ninjurin1 positively regulates osteoclast development by enhancing the
RT survival of prefusion osteoclasts.";
RL Exp. Mol. Med. 51:1-16(2019).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31091274; DOI=10.1371/journal.pone.0216987;
RA Kny M., Csalyi K.D., Klaeske K., Busch K., Meyer A.M., Merks A.M., Darm K.,
RA Dworatzek E., Fliegner D., Baczko I., Regitz-Zagrosek V., Butter C.,
RA Luft F.C., Panakova D., Fielitz J.;
RT "Ninjurin1 regulates striated muscle growth and differentiation.";
RL PLoS ONE 14:e0216987-e0216987(2019).
RN [21]
RP FUNCTION (SECRETED NINJURIN-1), SUBCELLULAR LOCATION (SECRETED NINJURIN-1),
RP AND PROTEOLYTIC CLEAVAGE.
RX PubMed=32883094; DOI=10.1161/circulationaha.120.046907;
RA Jeon S., Kim T.K., Jeong S.J., Jung I.H., Kim N., Lee M.N., Sonn S.K.,
RA Seo S., Jin J., Kweon H.Y., Kim S., Shim D., Park Y.M., Lee S.H., Kim K.W.,
RA Cybulsky M.I., Shim H., Roh T.Y., Park W.Y., Lee H.O., Choi J.H.,
RA Park S.H., Oh G.T.;
RT "Anti-inflammatory actions of soluble ninjurin-1 ameliorate
RT atherosclerosis.";
RL Circulation 142:1736-1751(2020).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 43-ASN--SER-46.
RX PubMed=33472215; DOI=10.1038/s41586-021-03218-7;
RA Kayagaki N., Kornfeld O.S., Lee B.L., Stowe I.B., O'Rourke K., Li Q.,
RA Sandoval W., Yan D., Kang J., Xu M., Zhang J., Lee W.P., McKenzie B.S.,
RA Ulas G., Payandeh J., Roose-Girma M., Modrusan Z., Reja R., Sagolla M.,
RA Webster J.D., Cho V., Andrews T.D., Morris L.X., Miosge L.A., Goodnow C.C.,
RA Bertram E.M., Dixit V.M.;
RT "NINJ1 mediates plasma membrane rupture during lytic cell death.";
RL Nature 591:131-136(2021).
CC -!- FUNCTION: [Ninjurin-1]: Homophilic transmembrane adhesion molecule
CC involved in various processes such as inflammation, cell death, axonal
CC growth, cell chemotaxis and angiogenesis (PubMed:19557008,
CC PubMed:24347169, PubMed:24917672, PubMed:31526566, PubMed:33472215).
CC Promotes cell adhesion by mediating homophilic interactions via its
CC extracellular N-terminal adhesion motif (N-NAM) (PubMed:24917672,
CC PubMed:30510259). Involved in the progression of the inflammatory
CC stress by promoting cell-to-cell interactions between immune cells and
CC endothelial cells (PubMed:24917672, PubMed:30510259). Involved in
CC leukocyte migration during inflammation by promoting transendothelial
CC migration of macrophages via homotypic binding (PubMed:24917672).
CC Promotes the migration of monocytes across the brain endothelium to
CC central nervous system inflammatory lesions (By similarity). Acts as a
CC regulator of Toll-like receptor 4 (TLR4) signaling triggered by
CC lipopolysaccharide (LPS) during systemic inflammation; directly binds
CC LPS (PubMed:25860173). Acts as a mediator of both programmed and
CC necrotic cell death (PubMed:19557008, PubMed:33472215). Plays a key
CC role in the induction of plasma membrane rupture during programmed and
CC necrotic cell death: oligomerizes in response to death stimuli to
CC mediate plasma membrane rupture (cytolysis), leading to release
CC intracellular molecules named damage-associated molecular patterns
CC (DAMPs) that propagate the inflammatory response (PubMed:33472215).
CC Plays a role in nerve regeneration by promoting maturation of Schwann
CC cells (PubMed:31526566). Acts as a regulator of angiogenesis
CC (PubMed:25766274, PubMed:30354207). Promotes the formation of new
CC vessels by mediating the interaction between capillary pericyte cells
CC and endothelial cells (PubMed:25766274, PubMed:30354207). Also mediates
CC vascular functions in penile tissue as well as vascular formation
CC (PubMed:24979788). Promotes osteoclasts development by enhancing the
CC survival of prefusion osteoclasts (PubMed:30700695). Also involved in
CC striated muscle growth and differentiation (PubMed:31091274). Also
CC involved in cell senescence in a p53/TP53 manner, possibly by acting as
CC an indirect regulator of p53/TP53 mRNA translation (PubMed:23690620,
CC PubMed:29073078). {ECO:0000250|UniProtKB:Q92982,
CC ECO:0000269|PubMed:19557008, ECO:0000269|PubMed:23690620,
CC ECO:0000269|PubMed:24347169, ECO:0000269|PubMed:24917672,
CC ECO:0000269|PubMed:24979788, ECO:0000269|PubMed:25766274,
CC ECO:0000269|PubMed:25860173, ECO:0000269|PubMed:29073078,
CC ECO:0000269|PubMed:30354207, ECO:0000269|PubMed:30510259,
CC ECO:0000269|PubMed:30700695, ECO:0000269|PubMed:31091274,
CC ECO:0000269|PubMed:31526566, ECO:0000269|PubMed:33472215}.
CC -!- FUNCTION: [Secreted ninjurin-1]: Secreted form generated by cleavage,
CC which has chemotactic activity (PubMed:23142597). Acts as an anti-
CC inflammatory mediator by promoting monocyte recruitment, thereby
CC ameliorating atherosclerosis (PubMed:32883094).
CC {ECO:0000269|PubMed:23142597, ECO:0000269|PubMed:32883094}.
CC -!- SUBUNIT: [Ninjurin-1]: Homooligomer. {ECO:0000269|PubMed:33472215}.
CC -!- SUBCELLULAR LOCATION: [Ninjurin-1]: Cell membrane
CC {ECO:0000269|PubMed:24917672, ECO:0000269|PubMed:27815839,
CC ECO:0000269|PubMed:31091274, ECO:0000269|PubMed:33472215}; Multi-pass
CC membrane protein {ECO:0000255}. Synaptic cell membrane
CC {ECO:0000269|PubMed:27815839}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Secreted ninjurin-1]: Secreted
CC {ECO:0000269|PubMed:23142597, ECO:0000269|PubMed:32883094}.
CC -!- INDUCTION: By nerve injury (PubMed:9465296). Expression is activated by
CC p53/TP53 (PubMed:23690620). {ECO:0000269|PubMed:23690620,
CC ECO:0000269|PubMed:9465296}.
CC -!- PTM: [Ninjurin-1]: Cleaved by MMP9 protease to generate the Secreted
CC ninjurin-1 form. {ECO:0000269|PubMed:23142597,
CC ECO:0000269|PubMed:32883094}.
CC -!- PTM: [Ninjurin-1]: N-linked glycosylation is required for
CC homooligomerization. {ECO:0000269|PubMed:28067406}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in most cases
CC (PubMed:24347169, PubMed:27815839). Some mice have dome-shaped heads
CC and die within 2 months after birth (PubMed:27815839). Mice show
CC abnormal behavior, reminiscent of obsessive-compulsive disorder: mice
CC exhibit compulsive grooming-induced hair loss and self-made lesions as
CC well as increased anxiety-like behaviors (PubMed:27815839). Mice are
CC prone to systemic chronic inflammation in the skin, liver, kidney and
CC pancreas (PubMed:29073078). During inflammation, reduced motility of
CC bone marrow-derived macrophages and protrusive membrane dynamics are
CC observed (PubMed:24917672). Mice also display attenuated susceptibility
CC to experimental autoimmune encephalomyelitis, an animal model of
CC multiple sclerosis: attenuated susceptibility is caused by reduced
CC leukocyte infiltration and decreased adherence of leukocytes on retinal
CC vessels (PubMed:27815839). Abolished ability to mediate plasma membrane
CC rupture downstream cell death, without affecting GSDMD pore formation
CC (PubMed:33472215). Conditional deletion in pericytes impairs vessel
CC maturation and blood flow recovery in hind limb ischemia
CC (PubMed:30354207). {ECO:0000269|PubMed:24347169,
CC ECO:0000269|PubMed:24917672, ECO:0000269|PubMed:27815839,
CC ECO:0000269|PubMed:29073078, ECO:0000269|PubMed:30354207,
CC ECO:0000269|PubMed:33472215}.
CC -!- SIMILARITY: Belongs to the ninjurin family. {ECO:0000305}.
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DR EMBL; U91513; AAC14594.1; -; mRNA.
DR EMBL; AF219626; AAG32161.1; -; Genomic_DNA.
DR CCDS; CCDS26497.1; -.
DR RefSeq; NP_038638.1; NM_013610.2.
DR AlphaFoldDB; O70131; -.
DR STRING; 10090.ENSMUSP00000036740; -.
DR GlyGen; O70131; 1 site.
DR PhosphoSitePlus; O70131; -.
DR jPOST; O70131; -.
DR PaxDb; O70131; -.
DR PRIDE; O70131; -.
DR ProteomicsDB; 293556; -.
DR Antibodypedia; 28361; 179 antibodies from 27 providers.
DR DNASU; 18081; -.
DR Ensembl; ENSMUST00000049022; ENSMUSP00000036740; ENSMUSG00000037966.
DR GeneID; 18081; -.
DR KEGG; mmu:18081; -.
DR UCSC; uc007qiw.1; mouse.
DR CTD; 4814; -.
DR MGI; MGI:1196617; Ninj1.
DR VEuPathDB; HostDB:ENSMUSG00000037966; -.
DR eggNOG; ENOG502S12Z; Eukaryota.
DR GeneTree; ENSGT00940000158892; -.
DR HOGENOM; CLU_093971_2_0_1; -.
DR InParanoid; O70131; -.
DR OMA; LNDESTH; -.
DR OrthoDB; 1560683at2759; -.
DR PhylomeDB; O70131; -.
DR TreeFam; TF323538; -.
DR BioGRID-ORCS; 18081; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ninj1; mouse.
DR PRO; PR:O70131; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O70131; protein.
DR Bgee; ENSMUSG00000037966; Expressed in stroma of bone marrow and 260 other tissues.
DR ExpressionAtlas; O70131; baseline and differential.
DR Genevisible; O70131; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0097060; C:synaptic membrane; IDA:UniProtKB.
DR GO; GO:0098631; F:cell adhesion mediator activity; IDA:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IMP:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IDA:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; IDA:UniProtKB.
DR GO; GO:0048246; P:macrophage chemotaxis; IDA:UniProtKB.
DR GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0070265; P:necrotic cell death; IDA:UniProtKB.
DR GO; GO:1905351; P:pericyte cell migration; IMP:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:2001206; P:positive regulation of osteoclast development; IMP:UniProtKB.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IDA:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0090025; P:regulation of monocyte chemotaxis; IMP:UniProtKB.
DR GO; GO:0042246; P:tissue regeneration; IEA:InterPro.
DR InterPro; IPR007007; Ninjurin.
DR InterPro; IPR015639; Ninjurin1.
DR PANTHER; PTHR12316; PTHR12316; 1.
DR PANTHER; PTHR12316:SF19; PTHR12316:SF19; 1.
DR Pfam; PF04923; Ninjurin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Angiogenesis; Behavior; Cell adhesion; Cell membrane;
KW Cytolysis; Glycoprotein; Inflammatory response; Membrane; Phosphoprotein;
KW Reference proteome; Secreted; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..152
FT /note="Ninjurin-1"
FT /id="PRO_0000159644"
FT CHAIN 1..56
FT /note="Secreted ninjurin-1"
FT /evidence="ECO:0000305|PubMed:23142597"
FT /id="PRO_0000452825"
FT TOPO_DOM 1..79
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..37
FT /note="N-terminal adhesion motif"
FT /evidence="ECO:0000250|UniProtKB:Q92982"
FT REGION 40..69
FT /note="Required to induce plasma membrane rupture"
FT /evidence="ECO:0000269|PubMed:33472215"
FT SITE 56..57
FT /note="Cleavage; by MMP9"
FT /evidence="ECO:0000269|PubMed:23142597"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q92982"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70617"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70617"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28067406"
FT MUTAGEN 43..46
FT /note="NKKS->AAAA: Abolished ability to induce plasma
FT membrane rupture in response to death stimuli."
FT /evidence="ECO:0000269|PubMed:33472215"
FT MUTAGEN 60
FT /note="N->A,Q: Impaired N-glycosylation and reduced
FT homooligomerization."
FT /evidence="ECO:0000269|PubMed:28067406"
SQ SEQUENCE 152 AA; 16555 MW; E261CB447BC0A2E6 CRC64;
MESGTEEYEL NGDLRPGSPG SPDALPPRWG LRNRPINVNH YANKKSAAES MLDIALLMAN
ASQLKAVVEQ GNDFAFFVPL VVLISISLVL QIGVGVLLIF LVKYDLNNPA KHAKLDFLNN
LATGLVFIIV VVNIFITAFG VQKPVMDVAP RQ
