UniProt: A0A1S3STS2

Database: UniProt
Entry: A0A1S3STS2_SALSA

LinkDB:  A0A1S3STS2_SALSA 
Original site:  A0A1S3STS2_SALSA

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
All databases (25)   

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ID   A0A1S3STS2_SALSA        Unreviewed;      1129 AA.
AC   A0A1S3STS2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE            EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN   Name=LOC106611735 {ECO:0000313|RefSeq:XP_014067733.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014067733.1};
RN   [1] {ECO:0000313|RefSeq:XP_014067733.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014067733.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC         phospholipidSide 2.; EC=7.6.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00034036,
CC         ECO:0000256|RuleBase:RU362033};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC       ECO:0000256|RuleBase:RU362033}.
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DR   RefSeq; XP_014067733.1; XM_014212258.1.
DR   AlphaFoldDB; A0A1S3STS2; -.
DR   GeneID; 106611735; -.
DR   OrthoDB; 275833at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa09.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
DR   CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006539; P-type_ATPase_IV.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24092:SF38; PHOSPHOLIPID-TRANSPORTING ATPASE IG; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362033};
KW   Magnesium {ECO:0000256|RuleBase:RU362033};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362033};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362033}.
FT   TRANSMEM        64..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        285..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        339..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        972..994
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1006..1028
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   TRANSMEM        1040..1061
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362033"
FT   DOMAIN          38..91
FT                   /note="P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16209"
FT   DOMAIN          858..1104
FT                   /note="P-type ATPase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16212"
SQ   SEQUENCE   1129 AA;  128867 MW;  34EBD35D915E2914 CRC64;
     MLRRRLNRLF GRDERKVDSR TIYVGHRPCP ATEALIPPKF CDNRIVSSKY TVWNFLPKNL
     FEQFRRIANF YFLIIFLVQV IVDTPTSPVT SGLPLFFVIT VTAIKQGYED WLRHKADNEV
     NKYLVTVLED GRRACKESEK IKVGDVVEVV EDETFPCDLI LLQSSREDET CFVTTASLDG
     ESNHKTHYTV PDTERNLESL SATIECEQPQ PDLYKFVGRM HIYRNNQEPA VRSLGPENLL
     LKGATLKNTQ KIYGVAVYSG METKMALNYQ GKSQKRSAVE KSINAFLLVY LCILVSKALV
     CTTLKYVWQS RPGQDEPWYN QKTQKEKDTN LYLKMFTDFL SFMVLFNFII PVSMYVTVEM
     QKFLGSFFIS WDKDFFDPEI QEGALVNTSD LNEELGQVEY VFTDKTGTLT QNNMEFIECC
     IDGFQYKYAD SGTELDSFCV TDGPVSMLQQ KAGREKEELF LRALCLCHTV QVKEATGQGD
     GVEDQVDGVM GLDGETVHPA DIRGFIASSP DEVALVKGAM KYGFKFLGTE SKNMRVMNRN
     NDVETYELLH VLNFDPVRRR MSVLVRTKSG DIMLFCKGAD SSIFPRVRQD EVDRIRMHVE
     RNATEGYRTL CVAYKLLSSE EYDQADTGLR EAKLALQDRE EKLMAVYNQV ETGMSLIGAT
     AVEDRLQEEA AETMEALQGA GMKVWVLTGD KMETAKSTCY ACRLFQRSTE LLELTVRTLV
     DPGRKREERL QELLLDYHKR AVQDAPPIKA GVTRSWSSAN QDYGFIIDGA TLSLVLNSSP
     DSNSSCYKSL FLQICQNCTT VLCCRMAPLQ KAQIVKMVKT SKGSPITLSI GDGANDVSMI
     LEAHVGIGIK GREGRQAVRN SDYAIPKLKH LKKLLLGHGH LYYVRIAHLV QYFFYKNLCF
     ILPQFLYQFF CGYSQQPLYD AAYLTMYNIC FTSMPILANS LLEQHICMEV LMDNAALYRD
     VAKNAMLRWG PFLYWTLLGV YQGLLFFFGV RFLFSNPALQ DNGQVFGNWS FGTIVFTVLV
     FTVTLKLAMD TRHWTWINHF VIWGSLAFYM FFSFFWGGII WPFLRQQRLY FVFANMLSSV
     SAWLIIIMLI LLSLLPEILL LVLREPRGPH SRQIAAVTPL SYKHLIGQE
//

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