Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for F1Q4S1

Entry ID Method Resolution Chain Position Source
AF-F1Q4S1-F1 Predicted AlphaFoldDB

No variants for F1Q4S1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for F1Q4S1

No associated diseases with F1Q4S1

4 regional properties for F1Q4S1

Type Name Position InterPro Accession
ptm P-type ATPase, phosphorylation site 455 - 461 IPR018303
domain P-type ATPase, C-terminal 890 - 1117 IPR032630
domain P-type ATPase, N-terminal 112 - 170 IPR032631
domain P-type ATPase, haloacid dehalogenase domain 435 - 911 IPR044492

Functions

Description
EC Number 7.6.2.1 Linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Golgi apparatus, trans-Golgi network membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
endosome A vacuole to which materials ingested by endocytosis are delivered.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
trans-Golgi network The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATPase-coupled intramembrane lipid transporter activity Catalysis of the movement of lipids from one membrane leaflet to the other, driven by ATP hydrolysis. This includes flippases and floppases.
magnesium ion binding Binding to a magnesium (Mg) ion.

3 GO annotations of biological process

Name Definition
endocytosis A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
phospholipid translocation The movement of a phospholipid molecule from one leaflet of a membrane bilayer to the opposite leaflet.
retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P40527 NEO1 Probable phospholipid-transporting ATPase NEO1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
O43861 ATP9B Probable phospholipid-transporting ATPase IIB Homo sapiens (Human) PR
10 20 30 40 50 60
MADGIPLNPV RKNLRKTAYY DASRPARYQI EDESSNLDEM PLMMSEEAFE NDESDYQTLP
70 80 90 100 110 120
RARVSQRRRG LGWFLCGGWK VLCSSCCECL VHTCRRKKEL KARTVWLGHP EKCEEKYPKN
130 140 150 160 170 180
AIKNQKYNIV TFVPGVLYQQ FKFFLNLYFL VVACSQFVPS LKIGYLYTYW APLGFVLAVT
190 200 210 220 230 240
MVREAVDEVR RCRRDKEMNS QLYSKLTVRG KVQVKSSDIQ VGDLIIVEKN QRIPADMIFL
250 260 270 280 290 300
RTSEKTGSCF IRTDQLDGET DWKLRIGVAC TQRLPALGDL FSISAYVYVQ KPQLDIHSFE
310 320 330 340 350 360
GNFTREDCDP PIHESLSIEN TLWASTVVAS GTVIGVVIYT GKEMRSVMNT SQSKNKVGLL
370 380 390 400 410 420
DLELNRLTKA LFLAQVVLSV VMVALQGFLG PWFRNLFRFV VLFSYIIPIS LRVNLDMGKS
430 440 450 460 470 480
AYGWMIMKDE NIPGTVVRTS TIPEELGRLV YLLTDKTGTL TQNEMVFKRL HLGTVSYGTD
490 500 510 520 530 540
TMDEIQSHII QSYAQVSSAQ SNGSSASSTP SRKPQPPAPK VRKSVSSRIH EAVKAIALCH
550 560 570 580 590 600
NVTPVYESRV NGANAEPEST EADQDFSDDN RTYQASSPDE VALVRWTESV GLTLVNRDLT
610 620 630 640 650 660
SLQLKTPAGQ ILTYYILQIF PFTSESKRMG IIVREEATGD ITFYMKGADV AMASIVQYND
670 680 690 700 710 720
WLEEECGNMA REGLRTLVVA KKSLTEEQYQ DFENRYNQAK LSIHDRNLKV AAVVESLERE
730 740 750 760 770 780
MELLCLTGVE DQLQADVRPT LELLRNAGIK IWMLTGDKLE TATCIAKSSH LVSRNQDIHV
790 800 810 820 830 840
FKPVSNRGEA HLELNAFRRK HDCALVISGD SLEVCLRYYE HEFVELACQC PAVVCCRCSP
850 860 870 880 890 900
TQKAQIVRLL QQHTANRTCA IGDGGNDVSM IQAADCGIGI EGKEGKQASL AADFSITQFK
910 920 930 940 950 960
HIGRLLMVHG RNSYKRSAAL GQFVMHRGMI ISTMQAVFSS IFYFASVPLY QGFLMVGYAT
970 980 990 1000 1010 1020
IYTMFPVFSL VLDQDVKPEM ALLYPELYKD LTKGRSLSFK TFLIWVLISI YQGGILMYGA
1030 1040 1050 1060 1070 1080
LVLFDQEFVH VVAISFTALI LTELLMVALT IRTWHWLMVV AQLISLACYL ASLAFLNEYF
1090 1100 1110 1120
DLSFITTRVF LWKVCVITLV SCLPLYIIKY LKRKFSPPSY SKLSS