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Protein

Leucyl-cystinyl aminopeptidase

Gene

Lnpep

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

Functioni

Release of an N-terminal amino acid, cleave before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain (By similarity).By similarity

Catalytic activityi

Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half-cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei295 – 2951SubstrateBy similarity
Metal bindingi464 – 4641Zinc; catalyticPROSITE-ProRule annotation
Active sitei465 – 4651Proton acceptorPROSITE-ProRule annotation
Metal bindingi468 – 4681Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi487 – 4871Zinc; catalyticPROSITE-ProRule annotation
Sitei549 – 5491Transition state stabilizerBy similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: MGI
  2. metallopeptidase activity Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein catabolic process Source: MGI
  2. SMAD protein signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_342269. Endosomal/Vacuolar pathway.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiM01.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucyl-cystinyl aminopeptidase (EC:3.4.11.3)
Short name:
Cystinyl aminopeptidase
Alternative name(s):
Oxytocinase
Short name:
OTase
Gene namesi
Name:Lnpep
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2387123. Lnpep.

Subcellular locationi

  1. Cell membrane By similarity; Single-pass type II membrane protein By similarity
  2. Endomembrane system By similarity; Single-pass type II membrane protein By similarity

  3. Note: Localized mainly in intracellular vesicles together with GLUT4. Relocalizes to the plasma membrane in response to insulin. The dileucine internalization motif and/or the interaction with tankyrases may be involved in intracellular sequestration (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 109109CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei110 – 13122Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini132 – 1025894ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: Reactome
  2. endomembrane system Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. intracellular Source: MGI
  5. lysosomal membrane Source: MGI
  6. membrane Source: MGI
  7. perinuclear region of cytoplasm Source: MGI
  8. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10251025Leucyl-cystinyl aminopeptidasePRO_0000278198Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei70 – 701Phosphotyrosine1 Publication
Modified residuei80 – 801Phosphoserine1 Publication
Modified residuei91 – 911Phosphoserine1 Publication
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi447 – 4471N-linked (GlcNAc...)1 Publication
Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi664 – 6641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi682 – 6821N-linked (GlcNAc...)1 Publication
Glycosylationi695 – 6951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi758 – 7581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi834 – 8341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi850 – 8501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi989 – 9891N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8C129.
PaxDbiQ8C129.
PRIDEiQ8C129.

PTM databases

PhosphoSiteiQ8C129.

Expressioni

Gene expression databases

BgeeiQ8C129.
CleanExiMM_LNPEP.
ExpressionAtlasiQ8C129. baseline and differential.
GenevestigatoriQ8C129.

Interactioni

Subunit structurei

Homodimer. Binds tankyrases 1 and 2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi232146. 2 interactions.
IntActiQ8C129. 1 interaction.
MINTiMINT-4113930.

Structurei

3D structure databases

ProteinModelPortaliQ8C129.
SMRiQ8C129. Positions 161-1025.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 1016Tankyrase bindingBy similarity
Regioni428 – 4325Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi53 – 542Dileucine internalization motifSequence Analysis
Motifi76 – 772Dileucine internalization motifSequence Analysis

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG108296.
InParanoidiQ8C129.
KOiK01257.
OMAiTEEVQWI.
OrthoDBiEOG754HNR.
PhylomeDBiQ8C129.
TreeFamiTF300395.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C129-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG
60 70 80 90 100
SRLLVRGLGE HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SAAGYRQSPD
110 120 130 140 150
GTCSLPSART LVICVFVIVV AVSVIMVIYL LPRCTFTKEG CHKTNQSAEL
160 170 180 190 200
IQPVATNGKV FPWAQIRLPT AIIPLCYELS LHPNLTSMTF RGSVTISLQA
210 220 230 240 250
LQDTRDIILH STGHNISRVT FMSAVSSQEK QVEILEYPYH EQIAVVAPEP
260 270 280 290 300
LLTGHNYTLK IEYSANISNS YYGFYGITYT DKSNEKKYFA ATQFEPLAAR
310 320 330 340 350
SAFPCFDEPA FKATFIIKIT RNEHHTALSN MPKKSSVPAE EGLIQDEFSE
360 370 380 390 400
SVKMSTYLVA FIVGEMRNLS QDVNGTLVSV YAVPEKIGQV HHALDTTIKL
410 420 430 440 450
LEFYQTYFEI QYPLKKLDLV AIPDFEAGAM ENWGLLTFRE ETLLYDNATS
460 470 480 490 500
SVADRKLVTK IIAHELAHQW FGNLVTMQWW NDLWLNEGFA TFMEYFSVEK
510 520 530 540 550
IFKELNSYED FLDARFKTMR KDSLNSSHPI SSSVQSSEQI EEMFDSLSYF
560 570 580 590 600
KGASLLLMLK SYLSEDVFRH AVILYLHNHS YAAIQSDDLW DSFNEVTDKT
610 620 630 640 650
LDVKKMMKTW TLQKGFPLVT VQRKGTELLL QQERFFLRMQ PESQPSDTSH
660 670 680 690 700
LWHIPISYVT DGRNYSEYRS VSLLDKKSDV INLTEQVQWV KVNSNMTGYY
710 720 730 740 750
IVHYAHDDWT ALINQLKRNP YVLSDKDRAN LINNIFELAG LGKVPLRMAF
760 770 780 790 800
DLIDYLKNET HTAPITEALF QTNLIYNLLE KLGHMDLSSR LVARVHKLLQ
810 820 830 840 850
NQIQQQTWTD EGTPSMRELR SALLEFACAH SLENCTTMAT NLFDSWMASN
860 870 880 890 900
GTQSLPTDVM VTVFKVGART EKGWLFLFSM YSSMGSEAEK NKILEALASS
910 920 930 940 950
EDVHKLYWLM KSSLDGDIIR TQKLSLIIRT VGRHFPGHLL AWDFVKENWN
960 970 980 990 1000
KLVHKFHLGS YTIQSIVAGS THLFSTKTHL SEVQAFFENQ SEATLKLRCV
1010 1020
QEALEVIQLN IQWMVRNLKT LSQWL
Length:1,025
Mass (Da):117,304
Last modified:March 1, 2003 - v1
Checksum:iAD6F98196EBA683B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029094 mRNA. Translation: BAC26293.1.
BC120925 mRNA. Translation: AAI20926.1.
BC120926 mRNA. Translation: AAI20927.1.
CCDSiCCDS37457.1.
RefSeqiNP_766415.1. NM_172827.3.
UniGeneiMm.328807.
Mm.393452.

Genome annotation databases

EnsembliENSMUST00000041047; ENSMUSP00000036998; ENSMUSG00000023845.
GeneIDi240028.
KEGGimmu:240028.
UCSCiuc008apj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029094 mRNA. Translation: BAC26293.1.
BC120925 mRNA. Translation: AAI20926.1.
BC120926 mRNA. Translation: AAI20927.1.
CCDSiCCDS37457.1.
RefSeqiNP_766415.1. NM_172827.3.
UniGeneiMm.328807.
Mm.393452.

3D structure databases

ProteinModelPortaliQ8C129.
SMRiQ8C129. Positions 161-1025.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232146. 2 interactions.
IntActiQ8C129. 1 interaction.
MINTiMINT-4113930.

Protein family/group databases

MEROPSiM01.011.

PTM databases

PhosphoSiteiQ8C129.

Proteomic databases

MaxQBiQ8C129.
PaxDbiQ8C129.
PRIDEiQ8C129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041047; ENSMUSP00000036998; ENSMUSG00000023845.
GeneIDi240028.
KEGGimmu:240028.
UCSCiuc008apj.1. mouse.

Organism-specific databases

CTDi4012.
MGIiMGI:2387123. Lnpep.

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG108296.
InParanoidiQ8C129.
KOiK01257.
OMAiTEEVQWI.
OrthoDBiEOG754HNR.
PhylomeDBiQ8C129.
TreeFamiTF300395.

Enzyme and pathway databases

ReactomeiREACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_342269. Endosomal/Vacuolar pathway.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi384369.
PROiQ8C129.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C129.
CleanExiMM_LNPEP.
ExpressionAtlasiQ8C129. baseline and differential.
GenevestigatoriQ8C129.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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: C57BL/6J.
    Tissue: Skin.
  2. "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].
  3. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-70; SER-80 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-447 AND ASN-682.

Entry informationi

Entry nameiLCAP_MOUSE
AccessioniPrimary (citable) accession number: Q8C129
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: March 1, 2003
Last modified: April 1, 2015
This is version 103 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

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.