PPB_GADMO
ID PPB_GADMO Reviewed; 477 AA.
AC P83456;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Alkaline phosphatase;
DE Short=AP;
DE EC=3.1.3.1;
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, DISULFIDE BOND, GLYCOSYLATION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Small intestine {ECO:0000269|PubMed:12941638};
RX PubMed=12941638; DOI=10.1016/s1096-4959(03)00167-2;
RA Asgeirsson B., Nielsen B.N., Hoejrup P.;
RT "Amino acid sequence of the cold-active alkaline phosphatase from Atlantic
RT cod (Gadus morhua).";
RL Comp. Biochem. Physiol. 136B:45-60(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10042,
CC ECO:0000269|PubMed:12941638};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermolabile.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12941638}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12941638};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12941638}.
CC -!- MASS SPECTROMETRY: Mass=61000; Mass_error=1100; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12941638};
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
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DR AlphaFoldDB; P83456; -.
DR SMR; P83456; -.
DR STRING; 8049.ENSGMOP00000020512; -.
DR iPTMnet; P83456; -.
DR Proteomes; UP000694546; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..477
FT /note="Alkaline phosphatase"
FT /id="PRO_0000186166"
FT ACT_SITE 94
FT /note="Phosphoserine intermediate"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12941638"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12941638"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12941638"
FT DISULFID 165..185
FT /evidence="ECO:0000269|PubMed:12941638"
FT UNSURE 8
FT /note="P or K"
FT UNSURE 351
FT /note="T or A"
SQ SEQUENCE 477 AA; 52198 MW; 0637907C62188DF9 CRC64;
AGFPEQEPEP KFWNDWAQKT LDKALSLQTL NKNKAQNLIL FLGDGMGVPT VTAARILKGQ
LRGQPGEEGQ LEMDKFPFVA LSKTYNTNAQ VADSAGTATA YLCGVKANEG TVGVSAAAVR
SQANTTQGNE VTSILRWAKD AGKSIGIVTT TRVNHATPSA AYAHCVDRDW YSDNEMPADA
VEAGCKDIAR QLFENIPDID VIMGGGRKYM YPKNTTDVEY PGQPKHSGTR KDGRNLVKEW
VDRNTEKKGH YVWNKKDLLS LNPTKVDYLL GLFEPADLPY DLERNKETDP SLSEMVEVAI
KILRRNPNGF YLLVEGGRID HGHHEGKDKQ AIHEAVEMDR AIGRADLMTS TSDTLTVVTA
DHSHLFSFGG YTPRGNEIFG LAAFISDVDQ KPFTAILYGN GPGYKLVNGA RENVSTVDYQ
DNSYLAQAAV PLSSETHGGE DVAVFAKGPM AHLLHGVHEQ NYIPHAMAYA ACIGQNR
