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Database: UniProt
Entry: A0A1L8FZC3_XENLA
LinkDB: A0A1L8FZC3_XENLA
Original site: A0A1L8FZC3_XENLA 
ID   A0A1L8FZC3_XENLA        Unreviewed;      1130 AA.
AC   A0A1L8FZC3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Extracellular sulfatase Sulf-1 isoform X1 {ECO:0000313|RefSeq:XP_018123564.1, ECO:0000313|RefSeq:XP_041422423.1};
GN   Name=sulf1.L {ECO:0000313|RefSeq:XP_018123564.1,
GN   ECO:0000313|RefSeq:XP_041422423.1,
GN   ECO:0000313|Xenbase:XB-GENE-6488695};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018123564.1};
RN   [1] {ECO:0000313|RefSeq:XP_018123564.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018123564.1,
RC   ECO:0000313|RefSeq:XP_041422423.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018123564.1,
RC   ECO:0000313|RefSeq:XP_041422423.1};
RG   RefSeq;
RL   Submitted (APR-2022) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}.
CC       Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus,
CC       Golgi stack {ECO:0000256|ARBA:ARBA00004348}.
CC   -!- SIMILARITY: Belongs to the sulfatase family.
CC       {ECO:0000256|ARBA:ARBA00008779}.
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DR   RefSeq; XP_018123564.1; XM_018268075.2.
DR   RefSeq; XP_041422423.1; XM_041566489.1.
DR   STRING; 8355.A0A1L8FZC3; -.
DR   PaxDb; 8355-A0A1L8FZC3; -.
DR   GeneID; 108719292; -.
DR   KEGG; xla:108719292; -.
DR   AGR; Xenbase:XB-GENE-6488695; -.
DR   CTD; 108719292; -.
DR   Xenbase; XB-GENE-6488695; sulf1.L.
DR   OMA; ECKRRKW; -.
DR   OrthoDB; 1365192at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 108719292; Expressed in egg cell and 18 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd16147; G6S; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR024609; Extracellular_sulfatase_C.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR43108:SF1; EXTRACELLULAR SULFATASE SULF-1; 1.
DR   PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR   Pfam; PF12548; DUF3740; 2.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 2.
DR   PROSITE; PS00523; SULFATASE_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1130
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041081215"
FT   DOMAIN          43..373
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   DOMAIN          535..694
FT                   /note="Extracellular sulfatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12548"
FT   DOMAIN          697..755
FT                   /note="Extracellular sulfatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12548"
FT   REGION          561..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          658..685
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        561..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..602
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1130 AA;  130174 MW;  FC7D7BE6807134B2 CRC64;
     MKFLGFALVF ILLQMELPVG HGSSLKGSRV RGRIQPDRRN IRPNIILVLT DDQDVELGSL
     QVMNKTRRIM EEGGASFINA FVTTPMCCPS RSSMLTGKYV HNHNIFTNNE NCSSPSWQAI
     HEPRTFAVYL NNTGYRTAFF GKYLNEYNGS YIPPGWREWL GLVKNSRFYN YTMCRNGFKE
     KHGFEYEKDY FTDLITNDSI NYFKLSKKMY PHRPIMMVIS HAAPHGPEDS APQFSEFFPN
     ASQHITPSYN YAPNMDKHWI MQYTGAMLPI HMEFTNVLHR KRLQTLLSVD DSMEKLYNML
     VDIGELENTY LIYTSDHGYH IGQFGLVKGK SMPYDFDIRV PFFVRGPNVE PGSVVPQMVL
     NLDLAPTILD IAGLDTPPDM DGKSVLTLLD IERPGNRLRT NKKNKIWRDT FLVERGKFLR
     KKEEPSKSTP QSNHLPKYER VKELCQQARY QTACEQPGQK WQCIEDMSGK LRIHKCKGSS
     HTISLKKRTR SINSKGYGSK HKECVCGEAD YKPSRSQKKK QRLFMRTPGA KKFNPRFVHT
     RHTRSLSVEF EGEIYDINLD DEEDHQSSQL RSITKRHYIS EEEVGGDEDD DDNGEDEEDE
     EYMTTIPDND ELMLADGVIS ASQSASVRVT HKCYILANDT VHCERELYQS TKAWKDHKAY
     IDKEIEALQD KIKNLREVRG HLKRRKPDEC DCSKPGFYKK EKGVKVQDRL KGRMHPFKDG
     VQDVDNKFQI FKENRKKKKE RKEKKRQKKG EECSLPGLTC FTHDKNHWQT APFWNSGSFC
     ACTSSNNNTY WCLRTINETH NFLFCEFATG FLEYFDMNTD PYQLTNAVHT VERGILNQLH
     IQLMELRSCQ GHKQCNPRPK GLEAGDIYGT DGRANLPNFT EDVDWKGLED LYSVNETLYG
     YRNNYRLSLD DWANYLKDVD RVFALLNGNS KQTRRNETLV TQPDGFSNAS RYEMTSAESE
     EEFSGAAAED REPVTETNFS ALNMSIAVFN NEKKLETVND FPEQTDLNQP LWSNKNTERS
     TAVAPDPYEV EFSGNGLTEM ESKNTFHLQT DIYLSTERQQ DRSLTSGDIF EDQVYLPIDS
     KPVHQMALPA LQLDNSKNLE TTNNMSLLCY SEEISKDNVE GSALSPLLSD
//
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