ASP2_NECAM
ID ASP2_NECAM Reviewed; 425 AA.
AC Q9N9H4;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Aspartic protease 2 {ECO:0000303|PubMed:12552433};
DE Short=Na-APR-2 {ECO:0000303|PubMed:12552433};
DE EC=3.4.23.- {ECO:0000269|PubMed:12552433};
DE AltName: Full=Necepsin I {ECO:0000303|Ref.1};
DE AltName: Full=Pepsin-like aspartic protease 2 {ECO:0000303|PubMed:12552433};
DE Flags: Precursor;
GN Name=apr-2 {ECO:0000303|PubMed:12552433};
GN Synonyms=ncpI {ECO:0000303|Ref.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Bunostominae; Necator.
OX NCBI_TaxID=51031 {ECO:0000312|EMBL:CAC00542.1};
RN [1] {ECO:0000312|EMBL:CAC00542.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Girdwood K., Brown A.P., Pritchard D.I., Berry C.;
RT "An aspartic proteinase from the Human Hookworm Necator
RT americanus:identification of new structural classes of aspartic proteinases
RT in nematodes.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND PROTEOLYTIC CLEAVAGE.
RX PubMed=12552433; DOI=10.1086/367708;
RA Williamson A.L., Brindley P.J., Abbenante G., Datu B.J., Prociv P.,
RA Berry C., Girdwood K., Pritchard D.I., Fairlie D.P., Hotez P.J., Zhan B.,
RA Loukas A.;
RT "Hookworm aspartic protease, Na-APR-2, cleaves human hemoglobin and serum
RT proteins in a host-specific fashion.";
RL J. Infect. Dis. 187:484-494(2003).
CC -!- FUNCTION: Aspartic protease which cleaves several human serum proteins
CC including hemoglobin, fibrinogen and albumin. Appears to cleave
CC preferentially between P1 (Ala, Leu, Val, Phe and Gly) and P1' (Ala and
CC Leu) residues. {ECO:0000269|PubMed:12552433}.
CC -!- ACTIVITY REGULATION: Inhibited by pepstatin A.
CC {ECO:0000269|PubMed:12552433}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:12552433};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12552433}.
CC Note=Secreted into the gut lumen. {ECO:0000269|PubMed:12552433}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, amphidal glands and
CC excretory gland (at protein level). {ECO:0000269|PubMed:12552433}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the L4 larval stage and in adults.
CC Not expressed at the L3 infective larval stage.
CC {ECO:0000269|PubMed:12552433}.
CC -!- PTM: Cleaved into a mature form. {ECO:0000269|PubMed:12552433}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255,
CC ECO:0000255|PROSITE-ProRule:PRU01103, ECO:0000255|RuleBase:RU000454}.
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DR EMBL; AJ245458; CAC00542.1; -; mRNA.
DR AlphaFoldDB; Q9N9H4; -.
DR SMR; Q9N9H4; -.
DR MEROPS; A01.A75; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..425
FT /note="Aspartic protease 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5004330323"
FT DOMAIN 72..421
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 103..145
FT /evidence="ECO:0000250|UniProtKB:P0DJD7"
FT DISULFID 351..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 425 AA; 47650 MW; BEC8F83489306DF4 CRC64;
MRSILVLVAL IGCIAAGVYK IPLKRITPPM IKMLRAGTWE TYVEGMRKRQ LQLLKEHKVH
IQDVLGYANM EYLGEITIGT PQQKFLVVLD TGSSNLWVPD DSCYKEKRPD RCLVSNCDAG
LVCQVFCPDP KCCEHTREFK QVNACKDKHR FDQKNSNTYV KTNKTWAIAY GTGDARGFFG
RDTVRLGAEG KDQLVINDTW FGQAEHIAEF FSNTFLDGIL GLAFQELSEG GVAPPIIRAI
DLGLLDQPIF TVYFENVGDK EGVYGGVFTW GGLDPDHCED EVTYEQLTEA TYWQFRLKGV
SSKNFSSTAG WEAISDTGTS LNGAPRGILR SIARQYNGQY VASQGLYVVD CSKNVTVDVT
IGDRNYTMTA KNLVLEIQAD ICIMAFFEMD MFIGPAWILG DPFIREYCNI HDIEKKRIGF
AAVKH
