NINJ1_DANRE
ID NINJ1_DANRE Reviewed; 146 AA.
AC A0A0R4IDX9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Ninjurin-1 {ECO:0000303|PubMed:31091274};
DE AltName: Full=Nerve injury-induced protein 1 {ECO:0000250|UniProtKB:O70131};
GN Name=ninj1 {ECO:0000303|PubMed:31091274,
GN ECO:0000312|ZFIN:ZDB-GENE-141216-96};
GN ORFNames=si:ch1073-278o19.1 {ECO:0000312|ZFIN:ZDB-GENE-141216-96};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Homophilic transmembrane adhesion molecule involved in
CC various processes such as inflammation, cell death, axonal growth, cell
CC chemotaxis and angiogenesis (By similarity). Promotes cell adhesion by
CC mediating homophilic interactions via its extracellular N-terminal
CC region (By similarity). Involved in the progression of the inflammatory
CC stress by promoting cell-to-cell interactions between immune cells and
CC endothelial cells (By similarity). Acts as a mediator of both
CC programmed and necrotic cell death (By similarity). Plays a key role in
CC the induction of plasma membrane rupture during programmed and necrotic
CC cell death: oligomerizes in response to death stimuli to mediate plasma
CC membrane rupture (cytolysis), leading to release intracellular
CC molecules named damage-associated molecular patterns (DAMPs) that
CC propagate the inflammatory response (By similarity). Acts as a
CC regulator of angiogenesis (By similarity). Promotes the formation of
CC new vessels by mediating the interaction between capillary pericyte
CC cells and endothelial cells (By similarity). Also involved in striated
CC muscle growth and differentiation (PubMed:31091274).
CC {ECO:0000250|UniProtKB:O70131, ECO:0000269|PubMed:31091274}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250|UniProtKB:O70131}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O70131};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein results in
CC impaired heart and skeletal muscle development.
CC {ECO:0000269|PubMed:31091274}.
CC -!- SIMILARITY: Belongs to the ninjurin family. {ECO:0000305}.
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DR EMBL; CU914619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001919024.1; XM_001918989.4.
DR AlphaFoldDB; A0A0R4IDX9; -.
DR STRING; 7955.ENSDARP00000099454; -.
DR PaxDb; A0A0R4IDX9; -.
DR Ensembl; ENSDART00000172074; ENSDARP00000130916; ENSDARG00000103663.
DR GeneID; 100150223; -.
DR KEGG; dre:100150223; -.
DR CTD; 4814; -.
DR ZFIN; ZDB-GENE-141216-96; ninj1.
DR eggNOG; ENOG502S12Z; Eukaryota.
DR GeneTree; ENSGT00940000158892; -.
DR OMA; LNDESTH; -.
DR OrthoDB; 1560683at2759; -.
DR PhylomeDB; A0A0R4IDX9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098631; F:cell adhesion mediator activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0019835; P:cytolysis; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0042692; P:muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0070265; P:necrotic cell death; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
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:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:ZFIN.
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 3: Inferred from homology;
KW Angiogenesis; Cell adhesion; Cell membrane; Cytolysis; Glycoprotein;
KW Inflammatory response; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..146
FT /note="Ninjurin-1"
FT /id="PRO_0000452827"
FT TOPO_DOM 1..77
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..146
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..66
FT /note="Required to induce plasma membrane rupture"
FT /evidence="ECO:0000250|UniProtKB:O70131"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 146 AA; 16131 MW; F1B6AB6B9E11DB27 CRC64;
MASEAMELNG GVNRRDDPGA RPQQGRMSRN TPLNMNHYAN KKSAAESMLD IALLMANASQ
LKTVLELGPS FSFYIPLITL ISISLTLQII VGILLIFIVK WNLNDSSKHY ILNLLENIVT
ALVFIVVVVN VFITAFGVQR PDDKTS
