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Q9JLI3

- MMEL1_MOUSE

UniProt

Q9JLI3 - MMEL1_MOUSE

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Protein

Membrane metallo-endopeptidase-like 1

Gene

Mmel1

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

Functioni

Metalloprotease involved in sperm function, possibly by modulating the processes of fertilization and early embryonic development. Degrades a broad variety of small peptides with a preference for peptides shorter than 3 kDa containing neutral bulky aliphatic or aromatic amino acid residues. Shares the same substrate specificity with MME and cleaves peptides at the same amide bond.2 Publications

Catalytic activityi

Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.

Cofactori

Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by thiorphan and phosphoramidon.1 Publication

Kineticsi

  1. KM=18 µM for D-Ala(2)-Leu(5)-enkephalin1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei62 – 632CleavageCurated
Binding sitei121 – 1211Substrate carboxylBy similarity
Metal bindingi599 – 5991Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi603 – 6031Zinc; catalyticPROSITE-ProRule annotation
Active sitei606 – 6061PROSITE-ProRule annotation
Metal bindingi662 – 6621Zinc; catalyticPROSITE-ProRule annotation
Active sitei666 – 6661Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM13.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Membrane metallo-endopeptidase-like 1 (EC:3.4.24.11)
Alternative name(s):
NEP2(m)
Neprilysin II
Short name:
NEPII
Neprilysin-2
Short name:
NEP2
Short name:
NL2
Neprilysin-like 1
Short name:
NL-1
Neprilysin-like peptidase
Short name:
NEPLP
Soluble secreted endopeptidase
Cleaved into the following chain:
Alternative name(s):
Neprilysin-2 secreted
Short name:
NEP2(s)
Gene namesi
Name:Mmel1
Synonyms:Nep2, Nl1, Sep
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1351603. Mmel1.

Subcellular locationi

Membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Secreted 1 Publication
Note: A secreted form produced by proteollytic cleavage also exists.

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. extracellular space Source: MGI
  3. Golgi apparatus Source: MGI
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice are viable and develop normally. However, males produce smaller litters, indicating specific male fertility problems.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 632KR → NG: Abolishes formation the soluble form. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 765765Membrane metallo-endopeptidase-like 1PRO_0000248417Add
BLAST
Chaini63 – 765703Membrane metallo-endopeptidase-like 1, soluble formCuratedPRO_0000248418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 80By similarity
Disulfide bondi98 ↔ 750By similarity
Disulfide bondi106 ↔ 710By similarity
Disulfide bondi161 ↔ 425By similarity
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi636 ↔ 762By similarity
Glycosylationi694 – 6941N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9JLI3.
PRIDEiQ9JLI3.

PTM databases

PhosphoSiteiQ9JLI3.

Expressioni

Tissue specificityi

Highly expressed in testis. Also expressed in ovary. Weakly or not expressed in brain, lung, heart, liver, kidney, adrenal gland and intestine.1 Publication

Gene expression databases

BgeeiQ9JLI3.
CleanExiMM_MMEL1.
ExpressionAtlasiQ9JLI3. baseline and differential.
GenevestigatoriQ9JLI3.

Interactioni

Protein-protein interaction databases

IntActiQ9JLI3. 2 interactions.
MINTiMINT-4129130.

Structurei

3D structure databases

ProteinModelPortaliQ9JLI3.
SMRiQ9JLI3. Positions 74-765.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini41 – 765725LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 4021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili523 – 54927Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M13 family.Curated

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3590.
HOGENOMiHOG000245574.
HOVERGENiHBG005554.
InParanoidiQ9JLI3.
KOiK08635.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
InterProiIPR024079. MetalloPept_cat_dom.
IPR029735. MMEL1.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF112. PTHR11733:SF112. 1 hit.
PfamiPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9JLI3-1) [UniParc]FASTAAdd to Basket

Also known as: Beta

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVERAGWCRK KSPGFVEYGL MVLLLLLLGA IVTLGVFYSI GKQLPLLTSL
60 70 80 90 100
LHFSWDERTV VKRALRDSSL KSDICTTPSC VIAAARILEN MDQSRNPCEN
110 120 130 140 150
FYQYACGGWL RHHVIPETNS RYSVFDILRD ELEVILKGVL EDSTSQHRPA
160 170 180 190 200
VEKAKTLYRS CMNQSVIEKR DSEPLLSVLK MVGGWPVAMD KWNETMGLKW
210 220 230 240 250
ELERQLAVLN SQFNRRVLID LFIWNDDQNS SRHVIYIDQP TLGMPSREYY
260 270 280 290 300
FQEDNNHKVR KAYLEFMTSV ATMLRKDQNL SKESAMVREE MAEVLELETH
310 320 330 340 350
LANATVPQEK RHDVTALYHR MDLMELQERF GLKGFNWTLF IQNVLSSVEV
360 370 380 390 400
ELFPDEEVVV YGIPYLENLE DIIDSYSART MQNYLVWRLV LDRIGSLSQR
410 420 430 440 450
FKEARVDYRK ALYGTTVEEV RWRECVSYVN SNMESAVGSL YIKRAFSKDS
460 470 480 490 500
KSTVRELIEK IRSVFVDNLD ELNWMDEESK KKAQEKAMNI REQIGYPDYI
510 520 530 540 550
LEDNNKHLDE EYSSLTFYED LYFENGLQNL KNNAQRSLKK LREKVDQNLW
560 570 580 590 600
IIGAAVVNAF YSPNRNQIVF PAGILQPPFF SKDQPQSLNF GGIGMVIGHE
610 620 630 640 650
ITHGFDDNGR NFDKNGNMLD WWSNFSARHF QQQSQCMIYQ YGNFSWELAD
660 670 680 690 700
NQNVNGFSTL GENIADNGGV RQAYKAYLRW LADGGKDQRL PGLNLTYAQL
710 720 730 740 750
FFINYAQVWC GSYRPEFAVQ SIKTDVHSPL KYRVLGSLQN LPGFSEAFHC
760
PRGSPMHPMK RCRIW
Length:765
Mass (Da):88,700
Last modified:October 1, 2000 - v1
Checksum:iD3662F1CE5B957F7
GO
Isoform 2 (identifier: Q9JLI3-2) [UniParc]FASTAAdd to Basket

Also known as: Alpha, Delta

The sequence of this isoform differs from the canonical sequence as follows:
     41-63: Missing.

Show »
Length:742
Mass (Da):85,994
Checksum:i4A44EAD211B2499F
GO
Isoform 3 (identifier: Q9JLI3-3) [UniParc]FASTAAdd to Basket

Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     41-63: Missing.
     330-330: F → FGLKDRVSLCSPGCPGTHSVDQAGLELGNPPASDSRVL

Show »
Length:779
Mass (Da):89,710
Checksum:i5E48CA530828584B
GO

Sequence cautioni

The sequence BAE32538.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891M → L in AAF13152. (PubMed:10542292)Curated
Sequence conflicti189 – 1891M → L in AAF13153. (PubMed:10542292)Curated
Sequence conflicti264 – 2641L → P in AAF13152. (PubMed:10542292)Curated
Sequence conflicti264 – 2641L → P in AAF13153. (PubMed:10542292)Curated
Sequence conflicti659 – 6591T → S in AAF13152. (PubMed:10542292)Curated
Sequence conflicti659 – 6591T → S in AAF13153. (PubMed:10542292)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei41 – 6323Missing in isoform 2 and isoform 3. 2 PublicationsVSP_020290Add
BLAST
Alternative sequencei330 – 3301F → FGLKDRVSLCSPGCPGTHSV DQAGLELGNPPASDSRVL in isoform 3. CuratedVSP_020291

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF157105 mRNA. Translation: AAF13152.1.
AF157106 mRNA. Translation: AAF13153.1.
AF176569 mRNA. Translation: AAF69247.1.
AF302075 mRNA. Translation: AAG18446.1.
AF302076 mRNA. Translation: AAG18447.1.
AF302077 mRNA. Translation: AAG18448.1.
AK154366 mRNA. Translation: BAE32538.1. Different initiation.
RefSeqiNP_038811.2. NM_013783.2.
UniGeneiMm.116944.

Genome annotation databases

GeneIDi27390.
KEGGimmu:27390.
UCSCiuc008wcg.1. mouse. [Q9JLI3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF157105 mRNA. Translation: AAF13152.1 .
AF157106 mRNA. Translation: AAF13153.1 .
AF176569 mRNA. Translation: AAF69247.1 .
AF302075 mRNA. Translation: AAG18446.1 .
AF302076 mRNA. Translation: AAG18447.1 .
AF302077 mRNA. Translation: AAG18448.1 .
AK154366 mRNA. Translation: BAE32538.1 . Different initiation.
RefSeqi NP_038811.2. NM_013783.2.
UniGenei Mm.116944.

3D structure databases

ProteinModelPortali Q9JLI3.
SMRi Q9JLI3. Positions 74-765.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9JLI3. 2 interactions.
MINTi MINT-4129130.

Protein family/group databases

MEROPSi M13.008.

PTM databases

PhosphoSitei Q9JLI3.

Proteomic databases

PaxDbi Q9JLI3.
PRIDEi Q9JLI3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 27390.
KEGGi mmu:27390.
UCSCi uc008wcg.1. mouse. [Q9JLI3-1 ]

Organism-specific databases

CTDi 79258.
MGIi MGI:1351603. Mmel1.

Phylogenomic databases

eggNOGi COG3590.
HOGENOMi HOG000245574.
HOVERGENi HBG005554.
InParanoidi Q9JLI3.
KOi K08635.

Miscellaneous databases

NextBioi 305354.
PROi Q9JLI3.
SOURCEi Search...

Gene expression databases

Bgeei Q9JLI3.
CleanExi MM_MMEL1.
ExpressionAtlasi Q9JLI3. baseline and differential.
Genevestigatori Q9JLI3.

Family and domain databases

Gene3Di 3.40.390.10. 2 hits.
InterProi IPR024079. MetalloPept_cat_dom.
IPR029735. MMEL1.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view ]
PANTHERi PTHR11733. PTHR11733. 1 hit.
PTHR11733:SF112. PTHR11733:SF112. 1 hit.
Pfami PF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view ]
PRINTSi PR00786. NEPRILYSIN.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular identification and characterization of novel membrane-bound metalloprotease, the soluble secreted form of which hydrolyzes a variety of vasoactive peptides."
    Ikeda K., Emoto N., Raharjo S.B., Nurhantari Y., Saiki K., Yokoyama M., Matsuo M.
    J. Biol. Chem. 274:32469-32477(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Molecular cloning and biochemical characterization of a new mouse testis soluble zinc-metallopeptidase of the neprilysin family."
    Ghaddar G., Ruchon A.F., Carpentier M., Marcinkiewicz M., Seidah N.G., Crine P., DesGroseillers L., Boileau G.
    Biochem. J. 347:419-429(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF 62-LYS-ARG-63.
    Tissue: Testis.
  3. "Neprilysin degrades both amyloid beta peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases."
    Shirotani K., Tsubuki S., Iwata N., Takaki Y., Harigaya W., Maruyama K., Kiryu-Seo S., Kiyama H., Iwata H., Tomita T., Iwatsubo T., Saido T.C.
    J. Biol. Chem. 276:21895-21901(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ENZYME REGULATION.
  4. "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] OF 64-765.
    Strain: NOD.
  5. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiMMEL1_MOUSE
AccessioniPrimary (citable) accession number: Q9JLI3
Secondary accession number(s): Q3U495
, Q9ERK2, Q9ERK3, Q9QZV6, Q9QZV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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