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ADAM8

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

ADAM8

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
4DD8

Identifiers

Aliases

ADAM8, CD156, CD156a, MS2, ADAM metallopeptidase domain 8

External IDs

OMIM:602267;MGI:107825;HomoloGene:74384;GeneCards:ADAM8;OMA:ADAM8 - orthologs

Gene location (Human)

Chr.	Chromosome 10 (human)^[1]

Band	10q26.3	Start	133,262,420bp^[1]
Band	10q26.3	End	133,276,868bp^[1]

Gene location (Mouse)

Chr.	Chromosome 7 (mouse)^[2]

Band	7\|7 F4	Start	139,558,845bp^[2]
Band	7\|7 F4	End	139,572,475bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

granulocyte

blood

spleen

monocyte

bone marrow cells

pancreatic ductal cell

periodontal fiber

appendix

upper lobe of left lung

right lung

Top expressed in

granulocyte

stroma of bone marrow

decidua

trachea

calvaria

tibiofemoral joint

lumbar spinal ganglion

gastrula

vein

mesenteric lymph nodes

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	metal ion binding protein self-association peptidase activity protein binding metalloendopeptidase activity hydrolase activity cell adhesion molecule binding calcium ion binding serine-type endopeptidase activity metallopeptidase activity zinc ion binding
Cellular component	cytoplasm integral component of membrane alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex membrane tertiary granule integral component of plasma membrane cell surface specific granule dense core granule membrane podosome phagolysosome alpha9-beta1 integrin-ADAM8 complex plasma membrane specific granule membrane tertiary granule membrane ficolin-1-rich granule membrane
Biological process	positive regulation of inflammatory response extracellular matrix disassembly proteolysis positive regulation of cellular extravasation positive regulation of neutrophil extravasation positive regulation of protein processing regulation of cell-cell adhesion positive regulation of protein secretion inflammatory response cellular response to hypoxia positive regulation of T cell migration positive regulation of tumor necrosis factor (ligand) superfamily member 11 production positive regulation of acute inflammatory response cell morphogenesis positive regulation of thymocyte apoptotic process positive regulation of bone resorption negative regulation of neuron apoptotic process positive regulation of fibronectin-dependent thymocyte migration positive regulation of eosinophil migration positive regulation of NF-kappaB transcription factor activity leukocyte migration involved in inflammatory response positive regulation of membrane protein ectodomain proteolysis positive regulation of protein kinase B signaling positive regulation of T cell differentiation in thymus lymphocyte chemotaxis positive regulation of cell adhesion angiogenesis neutrophil degranulation cell-cell adhesion positive regulation of MAP kinase activity positive regulation of innate immune response
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


101


11501

Ensembl


ENSG00000151651


ENSMUSG00000025473

UniProt


P78325


Q05910

RefSeq (mRNA)


NM_001109 NM_001164489 NM_001164490


NM_001291066 NM_007403

RefSeq (protein)


NP_001100 NP_001157961 NP_001157962


NP_001277995 NP_031429

Location (UCSC)

Chr 10: 133.26 – 133.28 Mb

Chr 7: 139.56 – 139.57 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

A Disintegrin and metalloproteinase domain-containing protein 8 is anenzyme that in humans is encoded by theADAM8gene.^[5]^[6]

Function

[edit]

This gene encodes a member of the ADAM (a disintegrin and metalloproteinase domain) family. Members of this family are membrane-anchored proteins structurally related to snake venomdisintegrins, and have been implicated in a variety of biological processes involving cell–cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene may be involved incell adhesion duringneurodegeneration.^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000151651 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000025473 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Yoshiyama K, Higuchi Y, Kataoka M, Matsuura K, Yamamoto S (April 1997). "CD156 (human ADAM8): expression, primary amino acid sequence, and gene location".Genomics.41 (1):56–62.doi:10.1006/geno.1997.4607.PMID 9126482.
^^a ^b"Entrez Gene: ADAM8 ADAM metallopeptidase domain 8".

External links

[edit]

TheMEROPS online database for peptidases and their inhibitors:M12.208
ADAM8 human gene location in theUCSC Genome Browser.
ADAM8 human gene details in theUCSC Genome Browser.
PDBe-KB provides an overview of all the structure information available in the PDB for Human Disintegrin and metalloproteinase domain-containing protein 8 (ADAM8)

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

v t e Proteins:clusters of differentiation (see alsolist of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 -CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 -CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

v t e Proteases:metalloendopeptidases (EC 3.4.24)
ADAM proteins	Alpha secretases ADAM9 ADAM10 ADAM17 ADAM19 ADAM2 ADAM7 ADAM8 ADAM11 ADAM12 ADAM15 ADAM18 ADAM22 ADAM23 ADAM28 ADAM33 ADAMTS1 ADAMTS2 ADAMTS3 ADAMTS4 ADAMTS5 ADAMTS8 ADAMTS9 ADAMTS10 ADAMTS12 ADAMTS13
Matrix metalloproteinases	Collagenases MMP1 MMP8 Gelatinases MMP2 MMP9 MMP3 MMP7 MMP10 MMP11 MMP12 MMP13 MMP14 MMP15 MMP16 MMP17 MMP19 MMP20 MMP21 MMP23A MMP23B MMP24 MMP25 MMP26 MMP27 MMP28
Other	Neprilysin Procollagen peptidase Thermolysin Pregnancy-associated plasma protein A Bone morphogenetic protein 1 Lysostaphin Insulin-degrading enzyme ZMPSTE24

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)