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Protein

Macrophage metalloelastase

Gene

Mmp12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3 (By similarity).By similarity

Catalytic activityi

Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi96 – 961Zinc 2; in inhibited formBy similarity
Metal bindingi128 – 1281Calcium 1By similarity
Metal bindingi162 – 1621Calcium 2By similarity
Metal bindingi172 – 1721Zinc 1By similarity
Metal bindingi174 – 1741Zinc 1By similarity
Metal bindingi179 – 1791Calcium 3By similarity
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi182 – 1821Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi184 – 1841Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi187 – 1871Zinc 1By similarity
Metal bindingi194 – 1941Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi198 – 1981Calcium 2By similarity
Metal bindingi200 – 2001Zinc 1By similarity
Metal bindingi202 – 2021Calcium 3By similarity
Metal bindingi203 – 2031Calcium 1By similarity
Metal bindingi205 – 2051Calcium 1By similarity
Metal bindingi205 – 2051Calcium 3By similarity
Metal bindingi222 – 2221Zinc 2; catalyticBy similarity
Active sitei223 – 2231PROSITE-ProRule annotation
Metal bindingi226 – 2261Zinc 2; catalyticBy similarity
Metal bindingi232 – 2321Zinc 2; catalyticBy similarity
Metal bindingi293 – 2931Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi385 – 3851Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi434 – 4341Calcium 4; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. positive regulation of epithelial cell proliferation involved in wound healing Source: MGI
  2. wound healing, spreading of epidermal cells Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_313067. Collagen degradation.

Protein family/group databases

MEROPSiM10.009.
MoonProtiP34960.

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage metalloelastase (EC:3.4.24.65)
Short name:
MME
Alternative name(s):
Matrix metalloproteinase-12
Short name:
MMP-12
Gene namesi
Name:Mmp12
Synonyms:Mme, Mmel
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:97005. Mmp12.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828CuratedAdd
BLAST
Propeptidei29 – 10981Activation peptide1 PublicationPRO_0000028778Add
BLAST
Chaini110 – 473364Macrophage metalloelastasePRO_0000028779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi85 – 851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi286 ↔ 473By similarity
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP34960.

PTM databases

PhosphoSiteiP34960.

Expressioni

Gene expression databases

BgeeiP34960.
CleanExiMM_MME.
MM_MMP12.
ExpressionAtlasiP34960. baseline and differential.
GenevestigatoriP34960.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliP34960.
SMRiP34960. Positions 40-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati289 – 33244Hemopexin 1Add
BLAST
Repeati333 – 37947Hemopexin 2Add
BLAST
Repeati381 – 42949Hemopexin 3Add
BLAST
Repeati430 – 47344Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi94 – 1018Cysteine switchBy similarity

Domaini

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG323958.
GeneTreeiENSGT00760000118870.
HOVERGENiHBG052484.
InParanoidiP34960.
KOiK01413.
OMAiPKLISTH.
PhylomeDBiP34960.
TreeFamiTF315428.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028718. MMP12.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF32. PTHR10201:SF32. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCTLLKGVC TMKFLMMIVF LQVSACGAAP MNDSEFAEWY LSRFYDYGKD
60 70 80 90 100
RIPMTKTKTN RNFLKEKLQE MQQFFGLEAT GQLDNSTLAI MHIPRCGVPD
110 120 130 140 150
VQHLRAVPQR SRWMKRYLTY RIYNYTPDMK REDVDYIFQK AFQVWSDVTP
160 170 180 190 200
LRFRKLHKDE ADIMILFAFG AHGDFNYFDG KGGTLAHAFY PGPGIQGDAH
210 220 230 240 250
FDEAETWTKS FQGTNLFLVA VHELGHSLGL QHSNNPKSIM YPTYRYLNPS
260 270 280 290 300
TFRLSADDIR NIQSLYGAPV KPPSLTKPSS PPSTFCHQSL SFDAVTTVGE
310 320 330 340 350
KIFFFKDWFF WWKLPGSPAT NITSISSIWP SIPSGIQAAY EIESRNQLFL
360 370 380 390 400
FKDEKYWLIN NLVPEPHYPR SIYSLGFSAS VKKVDAAVFD PLRQKVYFFV
410 420 430 440 450
DKHYWRYDVR QELMDPAYPK LISTHFPGIK PKIDAVLYFK RHYYIFQGAY
460 470
QLEYDPLFRR VTKTLKSTSW FGC
Length:473
Mass (Da):54,971
Last modified:July 10, 2007 - v3
Checksum:iD377250610BA249E
GO

Sequence cautioni

The sequence AAA39526.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC40889.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651K → E in AAH19135 (PubMed:15489334).Curated
Sequence conflicti65 – 651K → E in CAJ18584 (Ref. 4) Curated
Sequence conflicti78 – 781E → V in BAE30809 (PubMed:16141072).Curated
Sequence conflicti78 – 781E → V in BAE30260 (PubMed:16141072).Curated
Sequence conflicti78 – 781E → V in BAE30039 (PubMed:16141072).Curated
Sequence conflicti78 – 781E → V in BAE29689 (PubMed:16141072).Curated
Sequence conflicti80 – 801T → N in BAE33415 (PubMed:16141072).Curated
Sequence conflicti87 – 871T → A in BAE42486 (PubMed:16141072).Curated
Sequence conflicti172 – 1721H → N in BAE42198 (PubMed:16141072).Curated
Sequence conflicti188 – 1881A → V in AAA39526 (PubMed:1537850).Curated
Sequence conflicti199 – 1991A → T in BAC40836 (PubMed:16141072).Curated
Sequence conflicti241 – 2411Y → D in AAH19135 (PubMed:15489334).Curated
Sequence conflicti241 – 2411Y → D in CAJ18584 (Ref. 4) Curated
Sequence conflicti247 – 2471L → F in BAE33072 (PubMed:16141072).Curated
Sequence conflicti250 – 2501S → N in AAH19135 (PubMed:15489334).Curated
Sequence conflicti250 – 2501S → N in CAJ18584 (Ref. 4) Curated
Sequence conflicti268 – 2681A → P in BAC40846 (PubMed:16141072).Curated
Sequence conflicti272 – 2721P → T in AAH19135 (PubMed:15489334).Curated
Sequence conflicti272 – 2721P → T in CAJ18584 (Ref. 4) Curated
Sequence conflicti303 – 3031F → L in AAA39526 (PubMed:1537850).Curated
Sequence conflicti303 – 3031F → Y in BAC40889 (PubMed:16141072).Curated
Sequence conflicti303 – 3031F → Y in BAC40913 (PubMed:16141072).Curated
Sequence conflicti319 – 3191A → D in BAE33415 (PubMed:16141072).Curated
Sequence conflicti323 – 3231T → I in AAH19135 (PubMed:15489334).Curated
Sequence conflicti323 – 3231T → I in CAJ18584 (Ref. 4) Curated
Sequence conflicti328 – 3281I → T in BAE41743 (PubMed:16141072).Curated
Sequence conflicti335 – 3351G → A in AAA39526 (PubMed:1537850).Curated
Sequence conflicti403 – 4031H → Q in AAH19135 (PubMed:15489334).Curated
Sequence conflicti403 – 4031H → Q in CAJ18584 (Ref. 4) Curated
Sequence conflicti432 – 4321K → R in BAC40836 (PubMed:16141072).Curated
Sequence conflicti467 – 4671S → G in BAE42201 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M82831 mRNA. Translation: AAA39526.1. Different initiation.
AK089309 mRNA. Translation: BAC40836.1.
AK089335 mRNA. Translation: BAC40846.1.
AK089452 mRNA. Translation: BAC40889.1. Different initiation.
AK089523 mRNA. Translation: BAC40913.1.
AK090051 mRNA. Translation: BAC41067.1.
AK150596 mRNA. Translation: BAE29689.1.
AK151021 mRNA. Translation: BAE30039.1.
AK151273 mRNA. Translation: BAE30260.1.
AK151933 mRNA. Translation: BAE30809.1.
AK155139 mRNA. Translation: BAE33072.1.
AK155743 mRNA. Translation: BAE33411.1.
AK155747 mRNA. Translation: BAE33414.1.
AK155748 mRNA. Translation: BAE33415.1.
AK155865 mRNA. Translation: BAE33469.1.
AK170360 mRNA. Translation: BAE41743.1.
AK170364 mRNA. Translation: BAE41746.1.
AK170798 mRNA. Translation: BAE42035.1.
AK170804 mRNA. Translation: BAE42039.1.
AK170976 mRNA. Translation: BAE42154.1.
AK171006 mRNA. Translation: BAE42177.1.
AK171032 mRNA. Translation: BAE42198.1.
AK171036 mRNA. Translation: BAE42201.1.
AK171176 mRNA. Translation: BAE42294.1.
AK171428 mRNA. Translation: BAE42446.1.
AK171447 mRNA. Translation: BAE42457.1.
AK171448 mRNA. Translation: BAE42458.1.
AK171449 mRNA. Translation: BAE42459.1.
AK171450 mRNA. Translation: BAE42460.1.
AK171466 mRNA. Translation: BAE42472.1.
AK171468 mRNA. Translation: BAE42474.1.
AK171470 mRNA. Translation: BAE42476.1.
AK171472 mRNA. Translation: BAE42478.1.
AK171485 mRNA. Translation: BAE42486.1.
AK171518 mRNA. Translation: BAE42502.1.
AK171542 mRNA. Translation: BAE42516.1.
AK171570 mRNA. Translation: BAE42531.1.
BC019135 mRNA. Translation: AAH19135.2.
CT010377 mRNA. Translation: CAJ18584.1.
CCDSiCCDS22804.1.
PIRiA42401.
RefSeqiNP_032631.3. NM_008605.3.
UniGeneiMm.2055.

Genome annotation databases

EnsembliENSMUST00000005950; ENSMUSP00000005950; ENSMUSG00000049723.
GeneIDi17381.
KEGGimmu:17381.
UCSCiuc009och.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M82831 mRNA. Translation: AAA39526.1. Different initiation.
AK089309 mRNA. Translation: BAC40836.1.
AK089335 mRNA. Translation: BAC40846.1.
AK089452 mRNA. Translation: BAC40889.1. Different initiation.
AK089523 mRNA. Translation: BAC40913.1.
AK090051 mRNA. Translation: BAC41067.1.
AK150596 mRNA. Translation: BAE29689.1.
AK151021 mRNA. Translation: BAE30039.1.
AK151273 mRNA. Translation: BAE30260.1.
AK151933 mRNA. Translation: BAE30809.1.
AK155139 mRNA. Translation: BAE33072.1.
AK155743 mRNA. Translation: BAE33411.1.
AK155747 mRNA. Translation: BAE33414.1.
AK155748 mRNA. Translation: BAE33415.1.
AK155865 mRNA. Translation: BAE33469.1.
AK170360 mRNA. Translation: BAE41743.1.
AK170364 mRNA. Translation: BAE41746.1.
AK170798 mRNA. Translation: BAE42035.1.
AK170804 mRNA. Translation: BAE42039.1.
AK170976 mRNA. Translation: BAE42154.1.
AK171006 mRNA. Translation: BAE42177.1.
AK171032 mRNA. Translation: BAE42198.1.
AK171036 mRNA. Translation: BAE42201.1.
AK171176 mRNA. Translation: BAE42294.1.
AK171428 mRNA. Translation: BAE42446.1.
AK171447 mRNA. Translation: BAE42457.1.
AK171448 mRNA. Translation: BAE42458.1.
AK171449 mRNA. Translation: BAE42459.1.
AK171450 mRNA. Translation: BAE42460.1.
AK171466 mRNA. Translation: BAE42472.1.
AK171468 mRNA. Translation: BAE42474.1.
AK171470 mRNA. Translation: BAE42476.1.
AK171472 mRNA. Translation: BAE42478.1.
AK171485 mRNA. Translation: BAE42486.1.
AK171518 mRNA. Translation: BAE42502.1.
AK171542 mRNA. Translation: BAE42516.1.
AK171570 mRNA. Translation: BAE42531.1.
BC019135 mRNA. Translation: AAH19135.2.
CT010377 mRNA. Translation: CAJ18584.1.
CCDSiCCDS22804.1.
PIRiA42401.
RefSeqiNP_032631.3. NM_008605.3.
UniGeneiMm.2055.

3D structure databases

ProteinModelPortaliP34960.
SMRiP34960. Positions 40-473.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP34960.
ChEMBLiCHEMBL2594.

Protein family/group databases

MEROPSiM10.009.
MoonProtiP34960.

PTM databases

PhosphoSiteiP34960.

Proteomic databases

PRIDEiP34960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005950; ENSMUSP00000005950; ENSMUSG00000049723.
GeneIDi17381.
KEGGimmu:17381.
UCSCiuc009och.1. mouse.

Organism-specific databases

CTDi4321.
MGIiMGI:97005. Mmp12.

Phylogenomic databases

eggNOGiNOG323958.
GeneTreeiENSGT00760000118870.
HOVERGENiHBG052484.
InParanoidiP34960.
KOiK01413.
OMAiPKLISTH.
PhylomeDBiP34960.
TreeFamiTF315428.

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_313067. Collagen degradation.

Miscellaneous databases

NextBioi291984.
PROiP34960.
SOURCEiSearch...

Gene expression databases

BgeeiP34960.
CleanExiMM_MME.
MM_MMP12.
ExpressionAtlasiP34960. baseline and differential.
GenevestigatoriP34960.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028718. MMP12.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF32. PTHR10201:SF32. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase."
    Shapiro S.D., Griffin G.L., Gilbert D.J., Jenkins N.A., Copeland N.G., Welgus H.G., Senior R.M., Ley T.J.
    J. Biol. Chem. 267:4664-4671(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 110-136.
    Tissue: Macrophage.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c, C57BL/6J and NOD.
    Tissue: B-cell, Dendritic cell and Macrophage.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-473.

Entry informationi

Entry nameiMMP12_MOUSE
AccessioniPrimary (citable) accession number: P34960
Secondary accession number(s): Q3TB28
, Q3TBV6, Q3TBV9, Q3TD61, Q3U1S8, Q3U1S9, Q3U2R8, Q3UBC5, Q4FJM7, Q8BJ92, Q8BJB3, Q8BJB6, Q8BJB8, Q8BJB9, Q8VED6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 10, 2007
Last modified: April 1, 2015
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.