NINJ1_RAT
ID NINJ1_RAT Reviewed; 152 AA.
AC P70617;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ninjurin-1 {ECO:0000305};
DE AltName: Full=Nerve injury-induced protein 1 {ECO:0000303|PubMed:8780658};
DE Contains:
DE RecName: Full=Secreted ninjurin-1 {ECO:0000305};
GN Name=Ninj1 {ECO:0000312|RGD:3179};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=8780658; DOI=10.1016/s0896-6273(00)80166-x;
RA Araki T., Milbrandt J.;
RT "Ninjurin, a novel adhesion molecule, is induced by nerve injury and
RT promotes axonal growth.";
RL Neuron 17:353-361(1996).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-21 AND SER-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP FUNCTION.
RX PubMed=19595672; DOI=10.1016/j.bbrc.2009.07.019;
RA Ahn B.J., Lee H.J., Shin M.W., Choi J.H., Jeong J.W., Kim K.W.;
RT "Ninjurin1 is expressed in myeloid cells and mediates endothelium adhesion
RT in the brains of EAE rats.";
RL Biochem. Biophys. Res. Commun. 387:321-325(2009).
RN [4]
RP FUNCTION.
RX PubMed=33028854; DOI=10.1038/s41598-020-73340-5;
RA Kim S.W., Lee H.K., Seol S.I., Davaanyam D., Lee H., Lee J.K.;
RT "Ninjurin 1 dodecamer peptide containing the N-terminal adhesion motif (N-
RT NAM) exerts proangiogenic effects in HUVECs and in the postischemic
RT brain.";
RL Sci. Rep. 10:16656-16656(2020).
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 (By similarity). Promotes cell
CC adhesion by mediating homophilic interactions via its extracellular N-
CC terminal adhesion motif (N-NAM) (PubMed:19595672). Involved in the
CC progression of the inflammatory stress by promoting cell-to-cell
CC interactions between immune cells and endothelial cells (By
CC similarity). Involved in leukocyte migration during inflammation by
CC promoting transendothelial migration of macrophages via homotypic
CC binding (By similarity). Promotes the migration of monocytes across the
CC brain endothelium to central nervous system inflammatory lesions (By
CC similarity). Acts as a regulator of Toll-like receptor 4 (TLR4)
CC signaling triggered by lipopolysaccharide (LPS) during systemic
CC inflammation; directly binds LPS (By similarity). Acts as a mediator of
CC both programmed and necrotic cell death (By similarity). 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 (By similarity). Plays
CC a role in nerve regeneration by promoting maturation of Schwann cells
CC (By similarity). Acts as a regulator of angiogenesis (PubMed:33028854).
CC Promotes the formation of new vessels by mediating the interaction
CC between capillary pericyte cells and endothelial cells (By similarity).
CC Promotes osteoclasts development by enhancing the survival of prefusion
CC osteoclasts (By similarity). Also involved in striated muscle growth
CC and differentiation (By similarity). {ECO:0000250|UniProtKB:O70131,
CC ECO:0000250|UniProtKB:Q92982, ECO:0000269|PubMed:19595672,
CC ECO:0000269|PubMed:33028854}.
CC -!- FUNCTION: [Secreted ninjurin-1]: Secreted form generated by cleavage,
CC which has chemotactic activity. Acts as an anti-inflammatory mediator
CC by promoting monocyte recruitment, thereby ameliorating
CC atherosclerosis. {ECO:0000250|UniProtKB:O70131}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250|UniProtKB:O70131}.
CC -!- SUBCELLULAR LOCATION: [Ninjurin-1]: Cell membrane
CC {ECO:0000250|UniProtKB:O70131}; Multi-pass membrane protein
CC {ECO:0000255}. Synaptic cell membrane {ECO:0000250|UniProtKB:O70131};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Secreted ninjurin-1]: Secreted
CC {ECO:0000250|UniProtKB:O70131}.
CC -!- INDUCTION: By nerve injury. {ECO:0000269|PubMed:8780658}.
CC -!- PTM: [Ninjurin-1]: Cleaved by MMP9 protease to generate the Secreted
CC ninjurin-1 form. {ECO:0000250|UniProtKB:O70131}.
CC -!- PTM: [Ninjurin-1]: N-linked glycosylation is required for
CC homooligomerization. {ECO:0000250|UniProtKB:O70131}.
CC -!- SIMILARITY: Belongs to the ninjurin family. {ECO:0000305}.
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DR EMBL; U72660; AAB17559.1; -; mRNA.
DR RefSeq; NP_036999.1; NM_012867.1.
DR AlphaFoldDB; P70617; -.
DR STRING; 10116.ENSRNOP00000022341; -.
DR GlyGen; P70617; 1 site.
DR iPTMnet; P70617; -.
DR PhosphoSitePlus; P70617; -.
DR jPOST; P70617; -.
DR PaxDb; P70617; -.
DR PRIDE; P70617; -.
DR Ensembl; ENSRNOT00000022341; ENSRNOP00000022341; ENSRNOG00000016587.
DR GeneID; 25338; -.
DR KEGG; rno:25338; -.
DR CTD; 4814; -.
DR RGD; 3179; Ninj1.
DR eggNOG; ENOG502S12Z; Eukaryota.
DR GeneTree; ENSGT00940000158892; -.
DR HOGENOM; CLU_093971_2_0_1; -.
DR InParanoid; P70617; -.
DR OMA; LNDESTH; -.
DR OrthoDB; 1560683at2759; -.
DR PhylomeDB; P70617; -.
DR TreeFam; TF323538; -.
DR PRO; PR:P70617; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000016587; Expressed in pancreas and 19 other tissues.
DR Genevisible; P70617; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0031527; C:filopodium membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; ISO:RGD.
DR GO; GO:0098631; F:cell adhesion mediator activity; IDA:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; ISO:RGD.
DR GO; GO:0019835; P:cytolysis; ISS:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0048246; P:macrophage chemotaxis; ISO:RGD.
DR GO; GO:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0070265; P:necrotic cell death; ISS:UniProtKB.
DR GO; GO:1905351; P:pericyte cell migration; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:2001206; P:positive regulation of osteoclast development; ISO:RGD.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR GO; GO:0045765; P:regulation of angiogenesis; ISO:RGD.
DR GO; GO:0090025; P:regulation of monocyte chemotaxis; ISS: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; Cell adhesion; Cell membrane; Cytolysis;
KW Glycoprotein; Inflammatory response; Membrane; Phosphoprotein;
KW Reference proteome; Secreted; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..152
FT /note="Ninjurin-1"
FT /id="PRO_0000159645"
FT CHAIN 1..56
FT /note="Secreted ninjurin-1"
FT /evidence="ECO:0000250|UniProtKB:O70131"
FT /id="PRO_0000452826"
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..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..37
FT /note="N-terminal adhesion motif"
FT /evidence="ECO:0000269|PubMed:33028854"
FT REGION 40..69
FT /note="Required to induce plasma membrane rupture"
FT /evidence="ECO:0000250|UniProtKB:O70131"
FT SITE 56..57
FT /note="Cleavage; by MMP9"
FT /evidence="ECO:0000250|UniProtKB:O70131"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q92982"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 152 AA; 16539 MW; 414B3B9DE1807E80 CRC64;
MDPGTEEYEL NGDLRPGSPG SPDASPPRWG LRNRPINVNH YANKKSAAES MLDIALLMAN
ASQLKAVVEQ GNEFAFFVPL VVLISISLVL QIGVGVLLIF LVKYDLNNPA KHAKLDFLNN
LATGLVFIIV VVNIFITAFG VQKPVMDVAP RQ
