ID H3B3E8_LATCH Unreviewed; 984 AA.
AC H3B3E8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Alkaline phosphatase {ECO:0000256|ARBA:ARBA00012647, ECO:0000256|RuleBase:RU003947};
DE EC=3.1.3.1 {ECO:0000256|ARBA:ARBA00012647, ECO:0000256|RuleBase:RU003947};
GN Name=LOC102354239 {ECO:0000313|Ensembl:ENSLACP00000016419.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000016419.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000016419.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|RuleBase:RU003947};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601952-2};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000256|PIRSR:PIRSR601952-2};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005984, ECO:0000256|RuleBase:RU003946}.
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DR EMBL; AFYH01083675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01083676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01083677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01083678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01083679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01083680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3B3E8; -.
DR STRING; 7897.ENSLACP00000016419; -.
DR Ensembl; ENSLACT00000016533.1; ENSLACP00000016419.1; ENSLACG00000014466.2.
DR eggNOG; KOG4126; Eukaryota.
DR GeneTree; ENSGT00950000183063; -.
DR InParanoid; H3B3E8; -.
DR OMA; YDHEATE; -.
DR TreeFam; TF323513; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; ALKALINE PHOSPHATASE; 1.
DR PANTHER; PTHR11596:SF30; INTESTINAL-TYPE ALKALINE PHOSPHATASE; 1.
DR Pfam; PF00245; Alk_phosphatase; 2.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 2.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 2.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|RuleBase:RU003947};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR601952-2};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601952-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601952-2}.
FT REGION 712..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 591
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-1"
FT BINDING 541
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 652
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 654
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 817
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 822
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 826
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 863
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 864
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
FT BINDING 938
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601952-2"
SQ SEQUENCE 984 AA; 108708 MW; 42A52A91A00EF59B CRC64;
DAEKKPQFWY DKAKLSLETA LNLKSLNYQA KNLILFLGDG MGVSTVTAAR IYKGQRNGKL
GEEEIMAMDT FPYVALSKTY CVDRQVPDSA ATGTAYLCGV KTNYRVLGLS GSAVSSQCNT
TYGHEVYSVL HRAKQAGKSV GIVTTTRVQH ASPAAAYAHI VNRNWYADSS MPKDAIQDGC
KDIAYQLVHN TDFDSTLTLQ VILGGGRMYM TPMGTPDPEY PWDQKQNGIR NDGVNLIQTW
LDARKVNKNA HYVWNKTDFD AVDVKSTFYL MGLFEPKDMK YELNRNITLD PSIVEMMEKA
IGILSKNPKG FFLFVEGGRI DHGHHDSKAK MALTETVLFE QAIQRAGELT SDIDTLSVVT
ADHSHVFSFG GKTYRGNNIF GEAGSVAPKN ADDNLPYTSI LYGNGPGFNI QNGTRPNITM
TDIENKDYTQ QAAVPLDSET HAGEDVAIYA KGPMAYLFHG VQEQTYIAHA MAYAACIERE
KRMLHHIREK SPVSPITVPR NAVQEIKPSF WNLKAKSSLE EALKLKQRHH RAKNLILFLG
DGMGVPTVTA ARILKGQLLS HFGEETVLTM DTFPYLALSK TYNVDHQVPD SAGTATAYLC
GVKGNYGTIG LNAAAIRSNC TSSIGNHVTS ILKRAKDTGK SVGIVTTTRV QHASPAGNYA
HVAERNWYSD ASMPTDALKD GCKDIAYQLL HNTDINTRKL QVILGGGRKY MTPEGTKDPE
YPEHPKENGT RKDGIDLIQN WLNSKKVFKG AKYVWNKEQF DAVDVSTTNY LMGLFEPADM
KYELNRNNSM DPSIVDMTEK AIRILSENPK GFYLFVEGGR IDHGHHSSKA KKALIEAVMF
DHAIQRAGEL TSEEETLTVV TADHSHTFTF GGYTERGNSI FGLAPAKAND RKHYTSILYG
NGPGFAMQNG TRPAVNETIS DDNEYKQQAA VPLDSETHGG EDVVIFSKGP MAHLFHGVQE
QNYIPHVMAY AACIEPYSDC SFEA
//
