NINJ1_HUMAN
ID NINJ1_HUMAN Reviewed; 152 AA.
AC Q92982; Q6GU89; Q8WUV5; Q9BT07;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
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};
DE AltName: Full=Soluble ninjurin-1 {ECO:0000303|PubMed:32883094};
GN Name=NINJ1 {ECO:0000312|HGNC:HGNC:7824};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP VARIANT ASP-110.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ASP-110.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-110.
RC TISSUE=Lung, and Skin;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=9261151; DOI=10.1074/jbc.272.34.21373;
RA Araki T., Zimonjic D.B., Popescu N.C., Milbrandt J.;
RT "Mechanism of homophilic binding mediated by ninjurin, a novel widely
RT expressed adhesion molecule.";
RL J. Biol. Chem. 272:21373-21380(1997).
RN [8]
RP FUNCTION.
RX PubMed=22162058; DOI=10.1002/ana.22519;
RA Ifergan I., Kebir H., Terouz S., Alvarez J.I., Lecuyer M.A., Gendron S.,
RA Bourbonniere L., Dunay I.R., Bouthillier A., Moumdjian R., Fontana A.,
RA Haqqani A., Klopstein A., Prinz M., Lopez-Vales R., Birchler T., Prat A.;
RT "Role of Ninjurin-1 in the migration of myeloid cells to central nervous
RT system inflammatory lesions.";
RL Ann. Neurol. 70:751-763(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
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 [11]
RP FUNCTION (SECRETED NINJURIN-1), 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 [12]
RP FUNCTION.
RX PubMed=32147432; DOI=10.1016/j.lfs.2020.117518;
RA Toma L., Sanda G.M., Raileanu M., Stancu C.S., Niculescu L.S., Sima A.V.;
RT "Ninjurin-1 upregulated by TNFalpha receptor 1 stimulates monocyte adhesion
RT to human TNFalpha-activated endothelial cells; benefic effects of
RT amlodipine.";
RL Life Sci. 249:117518-117518(2020).
RN [13]
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).
RN [14]
RP FUNCTION, AND SUBUNIT.
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:8780658,
CC PubMed:9261151, PubMed:33472215). Promotes cell adhesion by mediating
CC homophilic interactions via its extracellular N-terminal adhesion motif
CC (N-NAM) (PubMed:33028854). Involved in the progression of the
CC inflammatory stress by promoting cell-to-cell interactions between
CC immune cells and endothelial cells (PubMed:22162058, PubMed:26677008,
CC PubMed:32147432). Involved in leukocyte migration during inflammation
CC by 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
CC (PubMed:22162058). Acts as a regulator of Toll-like receptor 4 (TLR4)
CC signaling triggered by lipopolysaccharide (LPS) during systemic
CC inflammation; directly binds LPS (PubMed:26677008). Acts as a mediator
CC of both programmed and necrotic cell death (PubMed:33472215). Plays a
CC key role in the induction of plasma membrane rupture during programmed
CC and 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:8780658, PubMed:9261151). Acts as a regulator of
CC angiogenesis (PubMed:33028854). Promotes the formation of new vessels
CC by mediating the interaction between capillary pericyte cells and
CC endothelial cells (By similarity). Promotes osteoclasts development by
CC enhancing the survival of prefusion osteoclasts (By similarity). Also
CC involved in striated muscle growth and differentiation (By similarity).
CC {ECO:0000250|UniProtKB:O70131, ECO:0000269|PubMed:22162058,
CC ECO:0000269|PubMed:26677008, ECO:0000269|PubMed:32147432,
CC ECO:0000269|PubMed:33028854, ECO:0000269|PubMed:33472215,
CC ECO:0000269|PubMed:8780658, ECO:0000269|PubMed:9261151}.
CC -!- FUNCTION: [Secreted ninjurin-1]: Secreted form generated by cleavage,
CC which has chemotactic activity (By similarity). Acts as an anti-
CC inflammatory mediator by promoting monocyte recruitment, thereby
CC ameliorating atherosclerosis (PubMed:32883094).
CC {ECO:0000250|UniProtKB:O70131, ECO:0000269|PubMed:32883094}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000269|PubMed:9261151}.
CC -!- INTERACTION:
CC Q92982; Q13520: AQP6; NbExp=3; IntAct=EBI-2802124, EBI-13059134;
CC Q92982; Q8TD46-4: CD200R1; NbExp=3; IntAct=EBI-2802124, EBI-12824513;
CC Q92982; P40198: CEACAM3; NbExp=3; IntAct=EBI-2802124, EBI-12851752;
CC Q92982; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2802124, EBI-6942903;
CC Q92982; P00387: CYB5R3; NbExp=3; IntAct=EBI-2802124, EBI-1046040;
CC Q92982; Q15125: EBP; NbExp=3; IntAct=EBI-2802124, EBI-3915253;
CC Q92982; P12314: FCGR1A; NbExp=3; IntAct=EBI-2802124, EBI-2869867;
CC Q92982; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-2802124, EBI-12142257;
CC Q92982; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-2802124, EBI-712073;
CC Q92982; Q8TED1: GPX8; NbExp=3; IntAct=EBI-2802124, EBI-11721746;
CC Q92982; Q6A162: KRT40; NbExp=3; IntAct=EBI-2802124, EBI-10171697;
CC Q92982; Q9H400: LIME1; NbExp=3; IntAct=EBI-2802124, EBI-2830566;
CC Q92982; P15941-11: MUC1; NbExp=3; IntAct=EBI-2802124, EBI-17263240;
CC Q92982; P15151: PVR; NbExp=3; IntAct=EBI-2802124, EBI-3919694;
CC Q92982; Q16585: SGCB; NbExp=3; IntAct=EBI-2802124, EBI-5663627;
CC Q92982; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-2802124, EBI-6268651;
CC Q92982; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-2802124, EBI-12947623;
CC Q92982; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2802124, EBI-8638294;
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:0000305|PubMed:32883094}.
CC -!- TISSUE SPECIFICITY: Widely expressed in both adult and embryonic
CC tissues, primarily those of epithelial origin.
CC {ECO:0000269|PubMed:8780658}.
CC -!- INDUCTION: By nerve injury both in dorsal root ganglion neurons and in
CC Schwann cells. {ECO:0000269|PubMed:8780658}.
CC -!- PTM: [Ninjurin-1]: Cleaved by MMP9 protease to generate the Secreted
CC ninjurin-1 form. {ECO:0000305|PubMed:32883094}.
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; U72661; AAB17560.1; -; mRNA.
DR EMBL; U91512; AAC14593.1; -; mRNA.
DR EMBL; AF029251; AAC39574.1; -; Genomic_DNA.
DR EMBL; BT007164; AAP35828.1; -; mRNA.
DR EMBL; AL451065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62856.1; -; Genomic_DNA.
DR EMBL; BC000298; AAH00298.1; -; mRNA.
DR EMBL; BC004440; AAH04440.1; -; mRNA.
DR EMBL; BC019336; AAH19336.2; -; mRNA.
DR EMBL; BC048212; AAH48212.1; -; mRNA.
DR CCDS; CCDS6703.1; -.
DR RefSeq; NP_004139.2; NM_004148.3.
DR AlphaFoldDB; Q92982; -.
DR BMRB; Q92982; -.
DR SMR; Q92982; -.
DR BioGRID; 110879; 22.
DR CORUM; Q92982; -.
DR IntAct; Q92982; 34.
DR STRING; 9606.ENSP00000364595; -.
DR GlyGen; Q92982; 1 site.
DR iPTMnet; Q92982; -.
DR PhosphoSitePlus; Q92982; -.
DR BioMuta; NINJ1; -.
DR DMDM; 317373398; -.
DR EPD; Q92982; -.
DR jPOST; Q92982; -.
DR MassIVE; Q92982; -.
DR MaxQB; Q92982; -.
DR PaxDb; Q92982; -.
DR PeptideAtlas; Q92982; -.
DR PRIDE; Q92982; -.
DR ProteomicsDB; 75642; -.
DR Antibodypedia; 28361; 179 antibodies from 27 providers.
DR DNASU; 4814; -.
DR Ensembl; ENST00000375446.5; ENSP00000364595.4; ENSG00000131669.10.
DR GeneID; 4814; -.
DR KEGG; hsa:4814; -.
DR MANE-Select; ENST00000375446.5; ENSP00000364595.4; NM_004148.4; NP_004139.2.
DR UCSC; uc004atg.4; human.
DR CTD; 4814; -.
DR DisGeNET; 4814; -.
DR GeneCards; NINJ1; -.
DR HGNC; HGNC:7824; NINJ1.
DR HPA; ENSG00000131669; Tissue enhanced (bone).
DR MIM; 602062; gene.
DR neXtProt; NX_Q92982; -.
DR OpenTargets; ENSG00000131669; -.
DR PharmGKB; PA31631; -.
DR VEuPathDB; HostDB:ENSG00000131669; -.
DR eggNOG; ENOG502S12Z; Eukaryota.
DR GeneTree; ENSGT00940000158892; -.
DR HOGENOM; CLU_093971_2_0_1; -.
DR InParanoid; Q92982; -.
DR OMA; LNDESTH; -.
DR OrthoDB; 1560683at2759; -.
DR PhylomeDB; Q92982; -.
DR TreeFam; TF323538; -.
DR PathwayCommons; Q92982; -.
DR SignaLink; Q92982; -.
DR BioGRID-ORCS; 4814; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; NINJ1; human.
DR GeneWiki; NINJ1; -.
DR GenomeRNAi; 4814; -.
DR Pharos; Q92982; Tbio.
DR PRO; PR:Q92982; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q92982; protein.
DR Bgee; ENSG00000131669; Expressed in right adrenal gland cortex and 158 other tissues.
DR Genevisible; Q92982; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097060; C:synaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098631; F:cell adhesion mediator activity; IDA:UniProtKB.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IDA:UniProtKB.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; IDA:UniProtKB.
DR GO; GO:0042692; P:muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0070265; P:necrotic cell death; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA: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; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0090025; P:regulation of monocyte chemotaxis; IDA: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_0000159643"
FT CHAIN 1..56
FT /note="Secreted ninjurin-1"
FT /evidence="ECO:0000250|UniProtKB:O70131"
FT /id="PRO_0000452824"
FT TOPO_DOM 1..80
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..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..26
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:0007744|PubMed:22814378"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70617"
FT MOD_RES 25
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 VARIANT 110
FT /note="A -> D (in dbSNP:rs2275848)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8780658, ECO:0000269|PubMed:9465296"
FT /id="VAR_025549"
SQ SEQUENCE 152 AA; 16345 MW; FEACA99450187855 CRC64;
MDSGTEEYEL NGGLPPGTPG SPDASPARWG WRHGPINVNH YASKKSAAES MLDIALLMAN
ASQLKAVVEQ GPSFAFYVPL VVLISISLVL QIGVGVLLIF LVKYDLNNPA KHAKLDFLNN
LATGLVFIIV VVNIFITAFG VQKPLMDMAP QQ
