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Q8C129 (LCAP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucyl-cystinyl aminopeptidase

Short name=Cystinyl aminopeptidase
EC=3.4.11.3
Alternative name(s):
Oxytocinase
Short name=OTase
Gene names
Name:Lnpep
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer. Binds tankyrases 1 and 2 By similarity.

Subcellular location

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.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10251025Leucyl-cystinyl aminopeptidase
PRO_0000278198

Regions

Topological domain1 – 109109Cytoplasmic Potential
Transmembrane110 – 13122Helical; Signal-anchor for type II membrane protein; Potential
Topological domain132 – 1025894Extracellular Potential
Region96 – 1016Tankyrase binding By similarity
Region428 – 4325Substrate binding By similarity
Motif53 – 542Dileucine internalization motif Potential
Motif76 – 772Dileucine internalization motif Potential

Sites

Active site4651Proton acceptor By similarity
Metal binding4641Zinc; catalytic By similarity
Metal binding4681Zinc; catalytic By similarity
Metal binding4871Zinc; catalytic By similarity
Binding site2951Substrate By similarity
Site5491Transition state stabilizer By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue701Phosphotyrosine Ref.3
Modified residue801Phosphoserine Ref.3
Modified residue911Phosphoserine Ref.3
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Ref.4
Glycosylation5251N-linked (GlcNAc...) Potential
Glycosylation5781N-linked (GlcNAc...) Potential
Glycosylation6641N-linked (GlcNAc...) Potential
Glycosylation6821N-linked (GlcNAc...) Ref.4
Glycosylation6951N-linked (GlcNAc...) Potential
Glycosylation7581N-linked (GlcNAc...) Potential
Glycosylation8341N-linked (GlcNAc...) Potential
Glycosylation8501N-linked (GlcNAc...) Potential
Glycosylation9891N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8C129 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: AD6F98196EBA683B

FASTA1,025117,304
        10         20         30         40         50         60 
MESFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG SRLLVRGLGE 

        70         80         90        100        110        120 
HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SAAGYRQSPD GTCSLPSART LVICVFVIVV 

       130        140        150        160        170        180 
AVSVIMVIYL LPRCTFTKEG CHKTNQSAEL IQPVATNGKV FPWAQIRLPT AIIPLCYELS 

       190        200        210        220        230        240 
LHPNLTSMTF RGSVTISLQA LQDTRDIILH STGHNISRVT FMSAVSSQEK QVEILEYPYH 

       250        260        270        280        290        300 
EQIAVVAPEP LLTGHNYTLK IEYSANISNS YYGFYGITYT DKSNEKKYFA ATQFEPLAAR 

       310        320        330        340        350        360 
SAFPCFDEPA FKATFIIKIT RNEHHTALSN MPKKSSVPAE EGLIQDEFSE SVKMSTYLVA 

       370        380        390        400        410        420 
FIVGEMRNLS QDVNGTLVSV YAVPEKIGQV HHALDTTIKL LEFYQTYFEI QYPLKKLDLV 

       430        440        450        460        470        480 
AIPDFEAGAM ENWGLLTFRE ETLLYDNATS SVADRKLVTK IIAHELAHQW FGNLVTMQWW 

       490        500        510        520        530        540 
NDLWLNEGFA TFMEYFSVEK IFKELNSYED FLDARFKTMR KDSLNSSHPI SSSVQSSEQI 

       550        560        570        580        590        600 
EEMFDSLSYF KGASLLLMLK SYLSEDVFRH AVILYLHNHS YAAIQSDDLW DSFNEVTDKT 

       610        620        630        640        650        660 
LDVKKMMKTW TLQKGFPLVT VQRKGTELLL QQERFFLRMQ PESQPSDTSH LWHIPISYVT 

       670        680        690        700        710        720 
DGRNYSEYRS VSLLDKKSDV INLTEQVQWV KVNSNMTGYY IVHYAHDDWT ALINQLKRNP 

       730        740        750        760        770        780 
YVLSDKDRAN LINNIFELAG LGKVPLRMAF DLIDYLKNET HTAPITEALF QTNLIYNLLE 

       790        800        810        820        830        840 
KLGHMDLSSR LVARVHKLLQ NQIQQQTWTD EGTPSMRELR SALLEFACAH SLENCTTMAT 

       850        860        870        880        890        900 
NLFDSWMASN GTQSLPTDVM VTVFKVGART EKGWLFLFSM YSSMGSEAEK NKILEALASS 

       910        920        930        940        950        960 
EDVHKLYWLM KSSLDGDIIR TQKLSLIIRT VGRHFPGHLL AWDFVKENWN KLVHKFHLGS 

       970        980        990       1000       1010       1020 
YTIQSIVAGS THLFSTKTHL SEVQAFFENQ SEATLKLRCV QEALEVIQLN IQWMVRNLKT 


LSQWL 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK029094 mRNA. Translation: BAC26293.1.
BC120925 mRNA. Translation: AAI20926.1.
BC120926 mRNA. Translation: AAI20927.1.
CCDSCCDS37457.1.
RefSeqNP_766415.1. NM_172827.3.
UniGeneMm.328807.
Mm.393452.

3D structure databases

ProteinModelPortalQ8C129.
SMRQ8C129. Positions 161-1025.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid232146. 2 interactions.
IntActQ8C129. 1 interaction.
MINTMINT-4113930.

Protein family/group databases

MEROPSM01.011.

PTM databases

PhosphoSiteQ8C129.

Proteomic databases

MaxQBQ8C129.
PaxDbQ8C129.
PRIDEQ8C129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041047; ENSMUSP00000036998; ENSMUSG00000023845.
GeneID240028.
KEGGmmu:240028.
UCSCuc008apj.1. mouse.

Organism-specific databases

CTD4012.
MGIMGI:2387123. Lnpep.

Phylogenomic databases

eggNOGCOG0308.
GeneTreeENSGT00740000115181.
HOGENOMHOG000106482.
HOVERGENHBG108296.
InParanoidQ8C129.
KOK01257.
OMAMEPFTND.
OrthoDBEOG754HNR.
PhylomeDBQ8C129.
TreeFamTF300395.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_209837. Membrane Trafficking.

Gene expression databases

ArrayExpressQ8C129.
BgeeQ8C129.
CleanExMM_LNPEP.
GenevestigatorQ8C129.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio384369.
PROQ8C129.
SOURCESearch...

Entry information

Entry nameLCAP_MOUSE
AccessionPrimary (citable) accession number: Q8C129
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot