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Q9UIQ6

- LCAP_HUMAN

UniProt

Q9UIQ6 - LCAP_HUMAN

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Protein

Leucyl-cystinyl aminopeptidase

Gene

LNPEP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Release of an N-terminal amino acid, cleaves 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.3 Publications

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.2 Publications

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei154 – 1552Cleavage; to produce pregnancy serum form
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: HGNC
  2. metallopeptidase activity Source: ProtInc
  3. zinc ion binding Source: ProtInc

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent Source: Reactome
  3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  4. cell-cell signaling Source: ProtInc
  5. female pregnancy Source: ProtInc
  6. membrane organization Source: Reactome
  7. protein catabolic process Source: Ensembl
  8. protein polyubiquitination Source: Reactome
  9. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_111168. Endosomal/Vacuolar pathway.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RKQ9UIQ6.

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):
Insulin-regulated membrane aminopeptidase
Insulin-responsive aminopeptidase
Short name:
IRAP
Oxytocinase
Short name:
OTase
Placental leucine aminopeptidase
Short name:
P-LAP
Cleaved into the following chain:
Gene namesi
Name:LNPEP
Synonyms:OTASE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:6656. LNPEP.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Note: In brain only the membrane-bound form is found. The protein resides in intracellular vesicles together with GLUT4 and can then translocate to the cell surface in response to insulin and/or oxytocin. Localization may be determined by dileucine internalization motifs, and/or by interaction with tankyrases.
Chain Leucyl-cystinyl aminopeptidase, pregnancy serum form : Secreted
Note: During pregnancy serum levels are low in the first trimester, rise progressively during the second and third trimester and decrease rapidly after parturition.

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: Reactome
  2. cytosol Source: Reactome
  3. early endosome lumen Source: Reactome
  4. extracellular region Source: UniProtKB-KW
  5. integral component of plasma membrane Source: ProtInc
  6. intracellular Source: HGNC
  7. lysosomal membrane Source: UniProtKB
  8. membrane Source: UniProtKB
  9. perinuclear region of cytoplasm Source: Ensembl
  10. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30418.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10251025Leucyl-cystinyl aminopeptidasePRO_0000095114Add
BLAST
Chaini155 – 1025871Leucyl-cystinyl aminopeptidase, pregnancy serum formPRO_0000292264Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei70 – 701PhosphotyrosineBy similarity
Modified residuei80 – 801PhosphoserineBy similarity
Modified residuei91 – 911PhosphoserineBy similarity
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)1 Publication
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
Glycosylationi448 – 4481N-linked (GlcNAc...)1 Publication
Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi664 – 6641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi682 – 6821N-linked (GlcNAc...)1 Publication
Glycosylationi760 – 7601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi834 – 8341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi850 – 8501N-linked (GlcNAc...)1 Publication
Glycosylationi989 – 9891N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The pregnancy serum form is derived from the membrane-bound form by proteolytic processing.
N-glycosylated.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9UIQ6.
PaxDbiQ9UIQ6.
PeptideAtlasiQ9UIQ6.
PRIDEiQ9UIQ6.

PTM databases

PhosphoSiteiQ9UIQ6.

Miscellaneous databases

PMAP-CutDBQ9UIQ6.

Expressioni

Tissue specificityi

Highly expressed in placenta, heart, kidney and small intestine. Detected at lower levels in neuronal cells in the brain, in skeletal muscle, spleen, liver, testes and colon.3 Publications

Gene expression databases

BgeeiQ9UIQ6.
CleanExiHS_LNPEP.
GenevestigatoriQ9UIQ6.

Organism-specific databases

HPAiHPA043642.

Interactioni

Subunit structurei

Homodimer. Binds tankyrases 1 and 2.

Protein-protein interaction databases

BioGridi110196. 17 interactions.
IntActiQ9UIQ6. 4 interactions.
STRINGi9606.ENSP00000231368.

Structurei

3D structure databases

ProteinModelPortaliQ9UIQ6.
SMRiQ9UIQ6. Positions 161-1025.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 110110CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini132 – 1025894ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei111 – 13121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 1016Tankyrase binding
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.
HOVERGENiHBG108296.
InParanoidiQ9UIQ6.
KOiK01257.
OMAiMEPFTND.
OrthoDBiEOG754HNR.
PhylomeDBiQ9UIQ6.
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]

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

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q9UIQ6-1) [UniParc]FASTAAdd to Basket

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
MEPFTNDRLQ LPRNMIENSM FEEEPDVVDL AKEPCLHPLE PDEVEYEPRG
60 70 80 90 100
SRLLVRGLGE HEMEEDEEDY ESSAKLLGMS FMNRSSGLRN SATGYRQSPD
110 120 130 140 150
GACSVPSART MVVCAFVIVV AVSVIMVIYL LPRCTFTKEG CHKKNQSIGL
160 170 180 190 200
IQPFATNGKL FPWAQIRLPT AVVPLRYELS LHPNLTSMTF RGSVTISVQA
210 220 230 240 250
LQVTWNIILH STGHNISRVT FMSAVSSQEK QAEILEYAYH GQIAIVAPEA
260 270 280 290 300
LLAGHNYTLK IEYSANISSS YYGFYGFSYT DESNEKKYFA ATQFEPLAAR
310 320 330 340 350
SAFPCFDEPA FKATFIIKII RDEQYTALSN MPKKSSVVLD DGLVQDEFSE
360 370 380 390 400
SVKMSTYLVA FIVGEMKNLS QDVNGTLVSI YAVPEKIGQV HYALETTVKL
410 420 430 440 450
LEFFQNYFEI QYPLKKLDLV AIPDFEAGAM ENWGLLTFRE ETLLYDSNTS
460 470 480 490 500
SMADRKLVTK IIAHELAHQW FGNLVTMKWW NDLWLNEGFA TFMEYFSLEK
510 520 530 540 550
IFKELSSYED FLDARFKTMK KDSLNSSHPI SSSVQSSEQI EEMFDSLSYF
560 570 580 590 600
KGSSLLLMLK TYLSEDVFQH AVVLYLHNHS YASIQSDDLW DSFNEVTNQT
610 620 630 640 650
LDVKRMMKTW TLQKGFPLVT VQKKGKELFI QQERFFLNMK PEIQPSDTSY
660 670 680 690 700
LWHIPLSYVT EGRNYSKYQS VSLLDKKSGV INLTEEVLWV KVNINMNGYY
710 720 730 740 750
IVHYADDDWE ALIHQLKINP YVLSDKDRAN LINNIFELAG LGKVPLKRAF
760 770 780 790 800
DLINYLGNEN HTAPITEALF QTDLIYNLLE KLGYMDLASR LVTRVFKLLQ
810 820 830 840 850
NQIQQQTWTD EGTPSMRELR SALLEFACTH NLGNCSTTAM KLFDDWMASN
860 870 880 890 900
GTQSLPTDVM TTVFKVGAKT DKGWSFLLGK YISIGSEAEK NKILEALASS
910 920 930 940 950
EDVRKLYWLM KSSLNGDNFR TQKLSFIIRT VGRHFPGHLL AWDFVKENWN
960 970 980 990 1000
KLVQKFPLGS YTIQNIVAGS TYLFSTKTHL SEVQAFFENQ SEATFRLRCV
1010 1020
QEALEVIQLN IQWMEKNLKS LTWWL
Length:1,025
Mass (Da):117,349
Last modified:April 17, 2007 - v3
Checksum:iF84C0EA9D48DC2C0
GO
Isoform 2 (identifier: Q9UIQ6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.

Show »
Length:1,011
Mass (Da):115,636
Checksum:iFBB54EFECFBA8FD9
GO
Isoform 3 (identifier: Q9UIQ6-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: Missing.

Show »
Length:1,006
Mass (Da):115,062
Checksum:iF57E71F1AA3C28E3
GO

Sequence cautioni

The sequence BAD92120.1 differs from that shown. Reason: Frameshift at position 405.
The sequence BAA09436.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661D → V in CAB61646. (PubMed:10759854)Curated
Sequence conflicti66 – 661D → V in CAB94753. (PubMed:10759854)Curated
Sequence conflicti301 – 3011S → L AA sequence (PubMed:8119729)Curated
Sequence conflicti386 – 3861K → N in AAB66672. (PubMed:9177475)Curated
Sequence conflicti386 – 3861K → N in AAB66673. (PubMed:9177475)Curated
Sequence conflicti386 – 3861K → N in CAB61646. (PubMed:10759854)Curated
Sequence conflicti386 – 3861K → N in CAB94753. (PubMed:10759854)Curated
Sequence conflicti892 – 8921K → Q in BAA09436. (PubMed:8550619)Curated
Sequence conflicti944 – 9441F → L in BAA09436. (PubMed:8550619)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861S → P.
Corresponds to variant rs3797799 [ dbSNP | Ensembl ].
VAR_031616
Natural varianti594 – 5941N → I.
Corresponds to variant rs12520455 [ dbSNP | Ensembl ].
VAR_051567
Natural varianti763 – 7631A → T.
Corresponds to variant rs2303138 [ dbSNP | Ensembl ].
VAR_012812
Natural varianti913 – 9131S → T.
Corresponds to variant rs17087233 [ dbSNP | Ensembl ].
VAR_051568
Natural varianti963 – 9631I → V.
Corresponds to variant rs11746232 [ dbSNP | Ensembl ].
VAR_031617

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1919Missing in isoform 3. 1 PublicationVSP_005449Add
BLAST
Alternative sequencei1 – 1414Missing in isoform 2. 2 PublicationsVSP_005448Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50810 mRNA. Translation: BAA09436.1. Different initiation.
U62768 mRNA. Translation: AAB66672.1.
U62769 mRNA. Translation: AAB66673.1.
AJ131023
, AJ131025, AJ131026, AJ131027, AJ131028, AJ131029, AJ131030, AJ131031, AJ131032, AJ131033, AJ131034, AJ131035, AJ131036, AJ131037, AJ131038, AJ131039 Genomic DNA. Translation: CAB61646.1.
AJ131025
, AJ131026, AJ131027, AJ131028, AJ131029, AJ131030, AJ131031, AJ131032, AJ131033, AJ131034, AJ131035, AJ131036, AJ131037, AJ131038, AJ131039 Genomic DNA. Translation: CAB94753.1.
AB208883 mRNA. Translation: BAD92120.1. Frameshift.
CCDSiCCDS4087.1. [Q9UIQ6-1]
CCDS43346.1. [Q9UIQ6-2]
PIRiA59383.
A59384.
RefSeqiNP_005566.2. NM_005575.2. [Q9UIQ6-1]
NP_787116.2. NM_175920.3. [Q9UIQ6-2]
UniGeneiHs.527199.
Hs.656905.

Genome annotation databases

EnsembliENST00000231368; ENSP00000231368; ENSG00000113441. [Q9UIQ6-1]
ENST00000395770; ENSP00000379117; ENSG00000113441. [Q9UIQ6-2]
GeneIDi4012.
KEGGihsa:4012.
UCSCiuc003kmv.1. human. [Q9UIQ6-1]

Polymorphism databases

DMDMi145559489.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50810 mRNA. Translation: BAA09436.1 . Different initiation.
U62768 mRNA. Translation: AAB66672.1 .
U62769 mRNA. Translation: AAB66673.1 .
AJ131023
, AJ131025 , AJ131026 , AJ131027 , AJ131028 , AJ131029 , AJ131030 , AJ131031 , AJ131032 , AJ131033 , AJ131034 , AJ131035 , AJ131036 , AJ131037 , AJ131038 , AJ131039 Genomic DNA. Translation: CAB61646.1 .
AJ131025
, AJ131026 , AJ131027 , AJ131028 , AJ131029 , AJ131030 , AJ131031 , AJ131032 , AJ131033 , AJ131034 , AJ131035 , AJ131036 , AJ131037 , AJ131038 , AJ131039 Genomic DNA. Translation: CAB94753.1 .
AB208883 mRNA. Translation: BAD92120.1 . Frameshift.
CCDSi CCDS4087.1. [Q9UIQ6-1 ]
CCDS43346.1. [Q9UIQ6-2 ]
PIRi A59383.
A59384.
RefSeqi NP_005566.2. NM_005575.2. [Q9UIQ6-1 ]
NP_787116.2. NM_175920.3. [Q9UIQ6-2 ]
UniGenei Hs.527199.
Hs.656905.

3D structure databases

ProteinModelPortali Q9UIQ6.
SMRi Q9UIQ6. Positions 161-1025.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110196. 17 interactions.
IntActi Q9UIQ6. 4 interactions.
STRINGi 9606.ENSP00000231368.

Chemistry

BindingDBi Q9UIQ6.
ChEMBLi CHEMBL2693.

Protein family/group databases

MEROPSi M01.011.

PTM databases

PhosphoSitei Q9UIQ6.

Polymorphism databases

DMDMi 145559489.

Proteomic databases

MaxQBi Q9UIQ6.
PaxDbi Q9UIQ6.
PeptideAtlasi Q9UIQ6.
PRIDEi Q9UIQ6.

Protocols and materials databases

DNASUi 4012.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000231368 ; ENSP00000231368 ; ENSG00000113441 . [Q9UIQ6-1 ]
ENST00000395770 ; ENSP00000379117 ; ENSG00000113441 . [Q9UIQ6-2 ]
GeneIDi 4012.
KEGGi hsa:4012.
UCSCi uc003kmv.1. human. [Q9UIQ6-1 ]

Organism-specific databases

CTDi 4012.
GeneCardsi GC05P096272.
H-InvDB HIX0005054.
HGNCi HGNC:6656. LNPEP.
HPAi HPA043642.
MIMi 151300. gene.
neXtProti NX_Q9UIQ6.
PharmGKBi PA30418.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0308.
GeneTreei ENSGT00760000119082.
HOVERGENi HBG108296.
InParanoidi Q9UIQ6.
KOi K01257.
OMAi MEPFTND.
OrthoDBi EOG754HNR.
PhylomeDBi Q9UIQ6.
TreeFami TF300395.

Enzyme and pathway databases

Reactomei REACT_111168. Endosomal/Vacuolar pathway.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RK Q9UIQ6.

Miscellaneous databases

GeneWikii Cystinyl_aminopeptidase.
GenomeRNAii 4012.
NextBioi 15736.
PMAP-CutDB Q9UIQ6.
PROi Q9UIQ6.
SOURCEi Search...

Gene expression databases

Bgeei Q9UIQ6.
CleanExi HS_LNPEP.
Genevestigatori Q9UIQ6.

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

« Hide 'large scale' publications
  1. "Human placental leucine aminopeptidase/oxytocinase. A new member of type II membrane-spanning zinc metallopeptidase family."
    Rogi T., Tsujimoto M., Nakazato H., Mizutani S., Tomoda Y.
    J. Biol. Chem. 271:56-61(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 160-168; 319-332; 615-624; 635-647; 798-814 AND 870-880, TISSUE SPECIFICITY.
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Placenta.
  3. "Structure of the human oxytocinase/insulin-regulated aminopeptidase gene and localization to chromosome 5q21."
    Rasmussen T.E., Pedraza-Diaz S., Hardre R., Laustsen P.G., Carrion A.G., Kristensen T.
    Eur. J. Biochem. 267:2297-2306(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3).
  4. "Expression of placental leucine aminopeptidase/oxytocinase in neuronal cells and its action on neuronal peptides."
    Matsumoto H., Nagasaka T., Hattori A., Rogi T., Tsuruoka N., Mizutani S., Tsujimoto M.
    Eur. J. Biochem. 268:3259-3266(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 206-1025.
    Tissue: Brain.
  6. "Pool sequencing of natural HLA-DR, DQ, and DP ligands reveals detailed peptide motifs, constraints of processing, and general rules."
    Falk K., Roetzschke O., Stevanovic S., Jung G., Rammensee H.G.
    Immunogenetics 39:230-242(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 285-301 AND 710-724.
  7. "Identification of human placental leucine aminopeptidase as oxytocinase."
    Tsujimoto M., Mizutani S., Adachi H., Kimura M., Nakazato H., Tomoda Y.
    Arch. Biochem. Biophys. 292:388-392(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  8. "Evidence that the angiotensin IV (AT(4)) receptor is the enzyme insulin-regulated aminopeptidase."
    Albiston A.L., McDowall S.G., Matsacos D., Sim P., Clune E., Mustafa T., Lee J., Mendelsohn F.A., Simpson R.J., Connolly L.M., Chai S.Y.
    J. Biol. Chem. 276:48623-48626(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-184; ASN-448; ASN-682 AND ASN-850.
    Tissue: Leukemic T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLCAP_HUMAN
AccessioniPrimary (citable) accession number: Q9UIQ6
Secondary accession number(s): O00769
, Q15145, Q59H76, Q9TNQ2, Q9TNQ3, Q9UIQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: April 17, 2007
Last modified: October 29, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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