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Q8C129

- LCAP_MOUSE

UniProt

Q8C129 - LCAP_MOUSE

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Protein

Leucyl-cystinyl aminopeptidase

Gene
Lnpep
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei295 – 2951Substrate By similarity
Metal bindingi464 – 4641Zinc; catalytic By similarity
Active sitei465 – 4651Proton acceptor By similarity
Metal bindingi468 – 4681Zinc; catalytic By similarity
Metal bindingi487 – 4871Zinc; catalytic By similarity
Sitei549 – 5491Transition state stabilizer By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199112. Endosomal/Vacuolar pathway.
REACT_199115. 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: Chromosome 17

Organism-specific databases

MGIiMGI:2387123. Lnpep.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 109109Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei110 – 13122Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini132 – 1025894Extracellular Reviewed predictionAdd
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. lysosomal membrane Source: Ensembl
  5. membrane Source: MGI
  6. perinuclear region of cytoplasm Source: MGI
  7. 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-acetylmethionine By similarity
Modified residuei70 – 701Phosphotyrosine1 Publication
Modified residuei80 – 801Phosphoserine1 Publication
Modified residuei91 – 911Phosphoserine1 Publication
Glycosylationi145 – 1451N-linked (GlcNAc...) Reviewed prediction
Glycosylationi184 – 1841N-linked (GlcNAc...) Reviewed prediction
Glycosylationi215 – 2151N-linked (GlcNAc...) Reviewed prediction
Glycosylationi256 – 2561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi266 – 2661N-linked (GlcNAc...) Reviewed prediction
Glycosylationi368 – 3681N-linked (GlcNAc...) Reviewed prediction
Glycosylationi374 – 3741N-linked (GlcNAc...) Reviewed prediction
Glycosylationi447 – 4471N-linked (GlcNAc...)1 Publication
Glycosylationi525 – 5251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi578 – 5781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi664 – 6641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi682 – 6821N-linked (GlcNAc...)1 Publication
Glycosylationi695 – 6951N-linked (GlcNAc...) Reviewed prediction
Glycosylationi758 – 7581N-linked (GlcNAc...) Reviewed prediction
Glycosylationi834 – 8341N-linked (GlcNAc...) Reviewed prediction
Glycosylationi850 – 8501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi989 – 9891N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8C129.
PaxDbiQ8C129.
PRIDEiQ8C129.

PTM databases

PhosphoSiteiQ8C129.

Expressioni

Gene expression databases

ArrayExpressiQ8C129.
BgeeiQ8C129.
CleanExiMM_LNPEP.
GenevestigatoriQ8C129.

Interactioni

Subunit structurei

Homodimer. Binds tankyrases 1 and 2 By similarity.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ8C129.
SMRiQ8C129. Positions 161-1025.

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi53 – 542Dileucine internalization motif Reviewed prediction
Motifi76 – 772Dileucine internalization motif Reviewed prediction

Sequence similaritiesi

Belongs to the peptidase M1 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00740000115181.
HOGENOMiHOG000106482.
HOVERGENiHBG108296.
InParanoidiQ8C129.
KOiK01257.
OMAiMEPFTND.
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

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MESFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG     50
SRLLVRGLGE HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SAAGYRQSPD 100
GTCSLPSART LVICVFVIVV AVSVIMVIYL LPRCTFTKEG CHKTNQSAEL 150
IQPVATNGKV FPWAQIRLPT AIIPLCYELS LHPNLTSMTF RGSVTISLQA 200
LQDTRDIILH STGHNISRVT FMSAVSSQEK QVEILEYPYH EQIAVVAPEP 250
LLTGHNYTLK IEYSANISNS YYGFYGITYT DKSNEKKYFA ATQFEPLAAR 300
SAFPCFDEPA FKATFIIKIT RNEHHTALSN MPKKSSVPAE EGLIQDEFSE 350
SVKMSTYLVA FIVGEMRNLS QDVNGTLVSV YAVPEKIGQV HHALDTTIKL 400
LEFYQTYFEI QYPLKKLDLV AIPDFEAGAM ENWGLLTFRE ETLLYDNATS 450
SVADRKLVTK IIAHELAHQW FGNLVTMQWW NDLWLNEGFA TFMEYFSVEK 500
IFKELNSYED FLDARFKTMR KDSLNSSHPI SSSVQSSEQI EEMFDSLSYF 550
KGASLLLMLK SYLSEDVFRH AVILYLHNHS YAAIQSDDLW DSFNEVTDKT 600
LDVKKMMKTW TLQKGFPLVT VQRKGTELLL QQERFFLRMQ PESQPSDTSH 650
LWHIPISYVT DGRNYSEYRS VSLLDKKSDV INLTEQVQWV KVNSNMTGYY 700
IVHYAHDDWT ALINQLKRNP YVLSDKDRAN LINNIFELAG LGKVPLRMAF 750
DLIDYLKNET HTAPITEALF QTNLIYNLLE KLGHMDLSSR LVARVHKLLQ 800
NQIQQQTWTD EGTPSMRELR SALLEFACAH SLENCTTMAT NLFDSWMASN 850
GTQSLPTDVM VTVFKVGART EKGWLFLFSM YSSMGSEAEK NKILEALASS 900
EDVHKLYWLM KSSLDGDIIR TQKLSLIIRT VGRHFPGHLL AWDFVKENWN 950
KLVHKFHLGS YTIQSIVAGS THLFSTKTHL SEVQAFFENQ SEATLKLRCV 1000
QEALEVIQLN IQWMVRNLKT LSQWL 1025
Length:1,025
Mass (Da):117,304
Last modified:March 1, 2003 - v1
Checksum:iAD6F98196EBA683B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK029094 mRNA. Translation: BAC26293.1 .
BC120925 mRNA. Translation: AAI20926.1 .
BC120926 mRNA. Translation: AAI20927.1 .
CCDSi CCDS37457.1.
RefSeqi NP_766415.1. NM_172827.3.
UniGenei Mm.328807.
Mm.393452.

3D structure databases

ProteinModelPortali Q8C129.
SMRi Q8C129. Positions 161-1025.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 232146. 2 interactions.
IntActi Q8C129. 1 interaction.
MINTi MINT-4113930.

Protein family/group databases

MEROPSi M01.011.

PTM databases

PhosphoSitei Q8C129.

Proteomic databases

MaxQBi Q8C129.
PaxDbi Q8C129.
PRIDEi Q8C129.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000041047 ; ENSMUSP00000036998 ; ENSMUSG00000023845 .
GeneIDi 240028.
KEGGi mmu:240028.
UCSCi uc008apj.1. mouse.

Organism-specific databases

CTDi 4012.
MGIi MGI:2387123. Lnpep.

Phylogenomic databases

eggNOGi COG0308.
GeneTreei ENSGT00740000115181.
HOGENOMi HOG000106482.
HOVERGENi HBG108296.
InParanoidi Q8C129.
KOi K01257.
OMAi MEPFTND.
OrthoDBi EOG754HNR.
PhylomeDBi Q8C129.
TreeFami TF300395.

Enzyme and pathway databases

Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_199112. Endosomal/Vacuolar pathway.
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi 384369.
PROi Q8C129.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8C129.
Bgeei Q8C129.
CleanExi MM_LNPEP.
Genevestigatori Q8C129.

Family and domain databases

InterProi IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
Pfami PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 96 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

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