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P97629

- LCAP_RAT

UniProt

P97629 - LCAP_RAT

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Protein
Leucyl-cystinyl aminopeptidase
Gene
Lnpep, Irap, Otase
Organism
Rattus norvegicus (Rat)
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: RGD
  2. angiotensin receptor activity Source: RGD
  3. metallopeptidase activity Source: UniProtKB-KW
  4. peptide hormone binding Source: RGD
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiotensin-activated signaling pathway Source: GOC
  2. neuropeptide catabolic process Source: RGD
  3. peptide catabolic process Source: RGD
  4. positive regulation of blood pressure Source: RGD
  5. regulation of long-term neuronal synaptic plasticity Source: RGD
  6. response to hormone Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199176. Translocation of GLUT4 to the plasma membrane.
REACT_199254. 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):
GP160
Insulin-regulated membrane aminopeptidase
Insulin-responsive aminopeptidase
Short name:
IRAP
Oxytocinase
Short name:
OTase
Placental leucine aminopeptidase
Short name:
P-LAP
Vesicle protein of 165 kDa
Short name:
Vp165
Gene namesi
Name:Lnpep
Synonyms:Irap, Otase
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi621752. Lnpep.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 109109Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei110 – 13122Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini132 – 1025894Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: RGD
  2. cytoplasm Source: RGD
  3. insulin-responsive compartment Source: RGD
  4. integral component of membrane Source: UniProtKB-KW
  5. intracellular membrane-bounded organelle Source: RGD
  6. intracellular organelle Source: RGD
  7. neuronal cell body Source: RGD
  8. perinuclear region of cytoplasm Source: RGD
  9. plasma membrane Source: RGD
  10. vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10251025Leucyl-cystinyl aminopeptidase
PRO_0000095115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei70 – 701Phosphotyrosine By similarity
Modified residuei80 – 801Phosphoserine; by PKC/PRKCZ; in vitro1 Publication
Modified residuei91 – 911Phosphoserine; by PKC/PRKCZ; in vitro1 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...) Reviewed prediction
Glycosylationi525 – 5251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi578 – 5781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi664 – 6641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi682 – 6821N-linked (GlcNAc...) Reviewed prediction
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

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP97629.
PRIDEiP97629.

PTM databases

PhosphoSiteiP97629.

Expressioni

Tissue specificityi

Highly expressed in heart, brain, spleen, lung, kidney and white adipose tissue. Detected at lower levels in skeletal muscle and liver.

Gene expression databases

GenevestigatoriP97629.

Interactioni

Subunit structurei

Homodimer. Binds tankyrases 1 and 2 By similarity.

Protein-protein interaction databases

IntActiP97629. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP97629.

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.
InParanoidiP97629.
KOiK01257.
OMAiMEPFTND.
OrthoDBiEOG754HNR.
PhylomeDBiP97629.

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.

P97629-1 [UniParc]FASTAAdd to Basket

« Hide

METFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG     50
SRLLVRGLGE HEMDEDEEDY ESSAKLLGMS FMNRSSGLRN SATGYRQSPD 100
GTCSVPSART LVICVFVIVV AVSVIMVIYL LPRCTFTKEG CHKTNQSAEL 150
IQPIATNGKV FPWAQIRLPT AIIPQRYELS LHPNLTSMTF RGSVTISLQA 200
LQDTRDIILH STGHNISSVT FMSAVSSQEK QVEILEYPYH EQIAVVAPES 250
LLTGHNYTLK IEYSANISNS YYGFYGITYT DKSNEKKNFA ATQFEPLAAR 300
SAFPCFDEPA FKATFIIKIT RDEHHTALSN MPKKSSVPTE EGLIQDEFSE 350
SVKMSTYLVA FIVGEMRNLS QDVNGTLVSV YAVPEKIDQV YHALDTTVKL 400
LEFYQNYFEI QYPLKKLDLV AIPDFEAGAM ENWGLLTFRE ETLLYDNATS 450
SVADRKLVTK IIAHELAHQW FGNLVTMQWW NDLWLNEGFA TFMEYFSVEK 500
IFKELNSYED FLDARFKTMR KDSLNSSHPI SSSVQSSEQI EEMFDSLSYF 550
KGASLLLMLK SYLSEDVFQH AIILYLHNHS YAAIQSDDLW DSFNEVTGKT 600
LDVKKMMKTW TLQKGFPLVT VQRKGTELLL QQERFFPSMQ PEIQDSDTSH 650
LWHIPISYVT DGRNYSEYRS VSLLDKKSDV INLTEQVQWV KVNTNMTGYY 700
IVHYAHDGWA ALINQLKRNP YVLSDKDRAN LINNIFELAG LGKVPLQMAF 750
DLIDYLRNET HTAPITEALF QTDLIYNLLE KLGHMDLSSR LVTRVHKLLQ 800
NQIQQQTWTD EGTPSMRELR SALLEFACAH SLENCTTMAT KLFDGWMASN 850
GTQSLPTDVM TTVFKVGART EKGWLFLFSM YSSMGSEAEK DKILEALASS 900
ADAHKLYWLM KSSLDGDIIR TQKLSLIIRT VGRQFPGHLL AWDFVKENWN 950
KLVHKFHLGS YTIQSIVAGS THLFSTKTHL SEVQEFFENQ SEATLQLRCV 1000
QEAFEVIELN IQWMARNLKT LTLWL 1025
Length:1,025
Mass (Da):117,201
Last modified:May 1, 1997 - v1
Checksum:i8AD3BA3A446FB5EF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti909 – 9168LMKSSLDG → YGTTQRAW in AAB38021. 1 Publication
Sequence conflicti916 – 1025110Missing in AAB38021. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U76997 mRNA. Translation: AAB19066.1.
U32990 mRNA. Translation: AAB38021.1.
PIRiI55441.
RefSeqiNP_001106874.1. NM_001113403.1.
NP_598258.1. NM_133574.1.
XP_003748754.1. XM_003748706.2.
UniGeneiRn.10614.

Genome annotation databases

EnsembliENSRNOT00000017718; ENSRNOP00000017718; ENSRNOG00000047387.
GeneIDi100912445.
171105.
KEGGirno:100912445.
rno:171105.
UCSCiRGD:621752. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U76997 mRNA. Translation: AAB19066.1 .
U32990 mRNA. Translation: AAB38021.1 .
PIRi I55441.
RefSeqi NP_001106874.1. NM_001113403.1.
NP_598258.1. NM_133574.1.
XP_003748754.1. XM_003748706.2.
UniGenei Rn.10614.

3D structure databases

ProteinModelPortali P97629.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P97629. 1 interaction.

Chemistry

BindingDBi P97629.
ChEMBLi CHEMBL3712.

Protein family/group databases

MEROPSi M01.011.

PTM databases

PhosphoSitei P97629.

Proteomic databases

PaxDbi P97629.
PRIDEi P97629.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000017718 ; ENSRNOP00000017718 ; ENSRNOG00000047387 .
GeneIDi 100912445.
171105.
KEGGi rno:100912445.
rno:171105.
UCSCi RGD:621752. rat.

Organism-specific databases

CTDi 4012.
RGDi 621752. Lnpep.

Phylogenomic databases

eggNOGi COG0308.
GeneTreei ENSGT00740000115181.
HOGENOMi HOG000106482.
HOVERGENi HBG108296.
InParanoidi P97629.
KOi K01257.
OMAi MEPFTND.
OrthoDBi EOG754HNR.
PhylomeDBi P97629.

Enzyme and pathway databases

Reactomei REACT_199176. Translocation of GLUT4 to the plasma membrane.
REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

NextBioi 621794.
PROi P97629.

Gene expression databases

Genevestigatori P97629.

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. "Cloning and characterization of a novel insulin-regulated membrane aminopeptidase from Glut4 vesicles."
    Keller S.R., Scott H.M., Mastick C.C., Aebersold R., Lienhard G.E.
    J. Biol. Chem. 270:23612-23618(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: Sprague-Dawley.
    Tissue: Adipocyte.
  2. "Characterization of a major protein in GLUT4 vesicles. Concentration in the vesicles and insulin-stimulated translocation to the plasma membrane."
    Mastick C.C., Aebersold R., Lienhard G.E.
    J. Biol. Chem. 269:6089-6092(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 168-176; 387-399; 731-740 AND 893-905.
  3. "Protein kinase C-zeta phosphorylates insulin-responsive aminopeptidase in vitro at Ser-80 and Ser-91."
    Ryu J., Hah J.S., Park J.S.S., Lee W., Rampal A.L., Jung C.Y.
    Arch. Biochem. Biophys. 403:71-82(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-80 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiLCAP_RAT
AccessioniPrimary (citable) accession number: P97629
Secondary accession number(s): Q11009
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 120 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, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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