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P15541

- AMPN_RABIT

UniProt

P15541 - AMPN_RABIT

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Protein
Aminopeptidase N
Gene
ANPEP
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis By similarity.

Catalytic activityi

Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi384 – 3841Zinc; catalytic By similarity
Active sitei385 – 3851Proton acceptor By similarity
Metal bindingi388 – 3881Zinc; catalytic By similarity
Metal bindingi407 – 4071Zinc; catalytic By similarity
Sitei473 – 4731Transition state stabilizer By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Developmental protein, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Short name:
AP-N
Short name:
rbAPN
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name:
AP-M
Microsomal aminopeptidase
CD_antigen: CD13
Gene namesi
Name:ANPEP
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 87Cytoplasmic By similarity
Transmembranei9 – 3224Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini33 – 966934Extracellular By similarity
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 966965Aminopeptidase N
PRO_0000095084Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi125 – 1251N-linked (GlcNAc...) Reviewed prediction
Modified residuei173 – 1731Sulfotyrosine Reviewed prediction
Glycosylationi259 – 2591N-linked (GlcNAc...) Reviewed prediction
Glycosylationi315 – 3151N-linked (GlcNAc...) Reviewed prediction
Modified residuei415 – 4151Sulfotyrosine Reviewed prediction
Modified residuei420 – 4201Sulfotyrosine Reviewed prediction
Glycosylationi552 – 5521N-linked (GlcNAc...) Reviewed prediction
Glycosylationi570 – 5701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi624 – 6241N-linked (GlcNAc...) Reviewed prediction
Glycosylationi734 – 7341N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi760 ↔ 767 By similarity
Disulfide bondi797 ↔ 833 By similarity
Glycosylationi817 – 8171N-linked (GlcNAc...) Reviewed prediction
Modified residuei852 – 8521Phosphotyrosine By similarity
Modified residuei912 – 9121Sulfotyrosine Reviewed prediction

Post-translational modificationi

Sulfated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000015166.

Structurei

3D structure databases

ProteinModelPortaliP15541.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6533Cytosolic Ser/Thr-rich junction
Add
BLAST
Regioni66 – 966901Metalloprotease
Add
BLAST
Regioni348 – 3525Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15541-1 [UniParc]FASTAAdd to Basket

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MAKGFYISKS LGILGILLGV AALCTIVALS VVYRQEKNKN TSQSPSMAPL    50
NPTATSSPAT TLDQNLPWNR YRLPKTLIPD SYNVVLRPYL SPNSQGLYIF 100
TGSSTVRFTC QEATNVIIIH SKKLNYTITQ GHRVVLRGVR GSQPPAIAST 150
ELVELTEYLV VHLQGQLVAG SQYEMDTQFQ GELADDLAGF YRSEYMEGNV 200
RKVVATTQMQ AADARKSFPC FDEPAMKATF NITPIHPRDY TALSNMLPRS 250
STALPEDPNW TVTEFHTTPK MSTYLLAYIV SEFTNIEAQS PNNVQIRIWA 300
RPSAISEGHG QYALNVTGPI LNFFANHYNT PYPLEKSDQI GLPDFNAGAM 350
ENWGLVTYRE SALLFDPLVS SISNKERVVT VVAHELAHQW FGNLVTVDWW 400
NDLWLNEGFA SYVEYLGADY AEPTWNLKDL IVLNELHSVM AVDALASSHP 450
LSSPADEVNT PAQISELFDS ITYSKGASVL RMLSSFLTED LFKEGLASYL 500
HTFAYQNTIY LDLWEHLQQA VNSQSAIQLP ASVRDIMDRW ILQMGFPVVT 550
VNTTNGIISQ HHFLLDPTSN VTRPSDFNYL WIVPVSSMRN GVLEQEFWLE 600
GVEQTQNSLF RVEGDNNWIL ANLNVTGYYQ VNYDEGNWKK LQTQLQTNPS 650
VIPVINRAQI IHDAFNLASA QKVPVTLALD NTLFLIRETE YMPWQAALSS 700
LNYFKLMFDR SEVYGPMKNY LSKQVRPLFE HFKNITNDWT RRPDTLMDQY 750
NEINAISTAC SNGIQECETL VSDLFKQWMD DPSNNPIHPN LRTTVYCNAI 800
ALGGEREWDF AWEQFRNATL VNEADKLRSA LACSNEVWIL NRYLSYTLNP 850
DYIRRQDATS TINSIASNVI GQTLVWDFVQ SNWKKLFEDF GGGSFSFANL 900
IRAVTRRFST EYELQQLEQF RLNNLDTGFG SGTRALEQAL EQTRANIKWV 950
QENKEAVLAW FTANSA 966
Length:966
Mass (Da):109,318
Last modified:January 23, 2007 - v4
Checksum:iED12832072B0DB52
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101S → A AA sequence 1 Publication
Sequence conflicti16 – 161I → F AA sequence 1 Publication
Sequence conflicti210 – 2101Q → QMQ1 Publication
Sequence conflicti226 – 2261M → S in CAA35873. 1 Publication
Sequence conflicti234 – 2341P → L in CAA35873. 1 Publication
Sequence conflicti593 – 5942LE → QQ in CAA35873. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S68687 mRNA. Translation: AAB29534.1.
X51508 mRNA. Translation: CAA35873.1.
PIRiS07099.
RefSeqiNP_001075795.1. NM_001082326.1.
UniGeneiOcu.2069.

Genome annotation databases

GeneIDi100009167.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S68687 mRNA. Translation: AAB29534.1 .
X51508 mRNA. Translation: CAA35873.1 .
PIRi S07099.
RefSeqi NP_001075795.1. NM_001082326.1.
UniGenei Ocu.2069.

3D structure databases

ProteinModelPortali P15541.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000015166.

Protein family/group databases

MEROPSi M01.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009167.

Organism-specific databases

CTDi 290.

Phylogenomic databases

eggNOGi COG0308.
HOGENOMi HOG000106482.
HOVERGENi HBG006616.

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. "Complete sequence of rabbit kidney aminopeptidase N and mRNA localization in rabbit kidney by in situ hybridization."
    Yang X.F., Milhiet P.E., Gaudoux F., Crine P., Boileau G.
    Biochem. Cell Biol. 71:278-287(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "The amino acid sequence of the hydrophobic anchor of rabbit intestinal brush border aminopeptidase N."
    Feracci H., Maroux S., Bonicel J., Desnuelle P.
    Biochim. Biophys. Acta 684:133-136(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 6-19.
  3. "Onset of transcription of the aminopeptidase N (leukemia antigen CD 13) gene at the crypt/villus transition zone during rabbit enterocyte differentiation."
    Noren O., Dabelsteen E., Hoeyer P.E., Olsen J., Sjoestroem H., Hansen G.H.
    FEBS Lett. 259:107-112(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-966.

Entry informationi

Entry nameiAMPN_RABIT
AccessioniPrimary (citable) accession number: P15541
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 119 of the entry and version 4 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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