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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).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; catalyticPROSITE-ProRule annotation
Active sitei385 – 3851Proton acceptorPROSITE-ProRule annotation
Metal bindingi388 – 3881Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi407 – 4071Zinc; catalyticPROSITE-ProRule annotation
Sitei473 – 4731Transition state stabilizerBy 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

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 – 11RemovedBy similarity
Chaini2 – 966965Aminopeptidase NPRO_0000095084Add
BLAST

Amino acid modifications

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

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.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 87CytoplasmicBy similarity
Topological domaini33 – 966934ExtracellularBy similarityAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei9 – 3224Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6533Cytosolic Ser/Thr-rich junctionAdd
BLAST
Regioni66 – 966901MetalloproteaseAdd
BLAST
Regioni348 – 3525Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP15541.

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

« Hide

        10         20         30         40         50
MAKGFYISKS LGILGILLGV AALCTIVALS VVYRQEKNKN TSQSPSMAPL
60 70 80 90 100
NPTATSSPAT TLDQNLPWNR YRLPKTLIPD SYNVVLRPYL SPNSQGLYIF
110 120 130 140 150
TGSSTVRFTC QEATNVIIIH SKKLNYTITQ GHRVVLRGVR GSQPPAIAST
160 170 180 190 200
ELVELTEYLV VHLQGQLVAG SQYEMDTQFQ GELADDLAGF YRSEYMEGNV
210 220 230 240 250
RKVVATTQMQ AADARKSFPC FDEPAMKATF NITPIHPRDY TALSNMLPRS
260 270 280 290 300
STALPEDPNW TVTEFHTTPK MSTYLLAYIV SEFTNIEAQS PNNVQIRIWA
310 320 330 340 350
RPSAISEGHG QYALNVTGPI LNFFANHYNT PYPLEKSDQI GLPDFNAGAM
360 370 380 390 400
ENWGLVTYRE SALLFDPLVS SISNKERVVT VVAHELAHQW FGNLVTVDWW
410 420 430 440 450
NDLWLNEGFA SYVEYLGADY AEPTWNLKDL IVLNELHSVM AVDALASSHP
460 470 480 490 500
LSSPADEVNT PAQISELFDS ITYSKGASVL RMLSSFLTED LFKEGLASYL
510 520 530 540 550
HTFAYQNTIY LDLWEHLQQA VNSQSAIQLP ASVRDIMDRW ILQMGFPVVT
560 570 580 590 600
VNTTNGIISQ HHFLLDPTSN VTRPSDFNYL WIVPVSSMRN GVLEQEFWLE
610 620 630 640 650
GVEQTQNSLF RVEGDNNWIL ANLNVTGYYQ VNYDEGNWKK LQTQLQTNPS
660 670 680 690 700
VIPVINRAQI IHDAFNLASA QKVPVTLALD NTLFLIRETE YMPWQAALSS
710 720 730 740 750
LNYFKLMFDR SEVYGPMKNY LSKQVRPLFE HFKNITNDWT RRPDTLMDQY
760 770 780 790 800
NEINAISTAC SNGIQECETL VSDLFKQWMD DPSNNPIHPN LRTTVYCNAI
810 820 830 840 850
ALGGEREWDF AWEQFRNATL VNEADKLRSA LACSNEVWIL NRYLSYTLNP
860 870 880 890 900
DYIRRQDATS TINSIASNVI GQTLVWDFVQ SNWKKLFEDF GGGSFSFANL
910 920 930 940 950
IRAVTRRFST EYELQQLEQF RLNNLDTGFG SGTRALEQAL EQTRANIKWV
960
QENKEAVLAW FTANSA
Length:966
Mass (Da):109,318
Last modified:January 23, 2007 - v4
Checksum:iED12832072B0DB52
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101S → A AA sequence (PubMed:6120002)Curated
Sequence conflicti16 – 161I → F AA sequence (PubMed:6120002)Curated
Sequence conflicti210 – 2101Q → QMQ(PubMed:2574692)Curated
Sequence conflicti226 – 2261M → S in CAA35873. (PubMed:2574692)Curated
Sequence conflicti234 – 2341P → L in CAA35873. (PubMed:2574692)Curated
Sequence conflicti593 – 5942LE → QQ in CAA35873. (PubMed:2574692)Curated

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.
InParanoidi P15541.

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: October 29, 2014
This is version 121 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