P28876

PR
Gene name
pma2 (SPCC1020.01c, SPCC1393.01)
Protein name
Plasma membrane ATPase 2
Names
Proton pump 2
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPCC1020.01c
EC number
7.1.2.1: Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

29-172 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P28876

Entry ID Method Resolution Chain Position Source
AF-P28876-F1 Predicted AlphaFoldDB

No variants for P28876

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P28876

No associated diseases with P28876

3 regional properties for P28876

Type Name Position InterPro Accession
domain Cation-transporting P-type ATPase, N-terminal 156 - 226 IPR004014
ptm P-type ATPase, phosphorylation site 464 - 470 IPR018303
domain P-type ATPase, haloacid dehalogenase domain 444 - 770 IPR044492

Functions

Description
EC Number 7.1.2.1 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Cell 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
cell division site The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
cell tip The region at the end of the longest axis of a cylindrical or elongated cell.
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.

5 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.
metal ion binding Binding to a metal ion.
P-type ion transporter activity Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of ions across a membrane. The reaction is characterized by the transient formation of a high-energy aspartyl-phosphoryl-enzyme intermediate.
P-type proton-exporting transporter activity Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out). These transporters use a phosphorylative mechanism, which have a phosphorylated intermediate state during the ion transport cycle.

4 GO annotations of biological process

Name Definition
ion transmembrane transport A process in which an ion is transported across a membrane.
proton export across plasma membrane The directed movement of hydrogen ions (protons) from inside a cell, across the plasma membrane and into the extracellular region.
proton transmembrane transport The directed movement of a proton across a membrane.
regulation of intracellular pH Any process that modulates the internal pH of a cell, measured by the concentration of the hydrogen ion.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQRNNGEGRP EGMHRISRFL HGNPFKNNAS PQDDSTTRTE VYEEGGVEDS AVDYDNASGN
70 80 90 100 110 120
AAPRLTAAPN THAQQANLQS GNTSITHETQ STSRGQEATT SPSLSASHEK PARPQTGEGS
130 140 150 160 170 180
DNEDEDEDID ALIEDLYSQD QEEEQVEEEE SPGPAGAAKV VPEELLETDP KYGLTESEVE
190 200 210 220 230 240
ERKKKYGLNQ MKEEKTNNIK KFLSFFVGPI QFVMELAAAL AAGLRDWVDF GVICALLLLN
250 260 270 280 290 300
ATVGFVQEYQ AGSIVDELKK TMALKASVLR DGRVKEIEAS EIVPGDILHL DEGTICPADG
310 320 330 340 350 360
RLITKDCFLQ VDQSAITGES LAVDKHQNDT MYSSSTVKRG EAFMVVTATA DSTFVGRAAS
370 380 390 400 410 420
LVGAAGQSQG HFTEVLNGIG TILLVLVILT LLCIYTAAFY RSVRLAALLE YTLAITIIGV
430 440 450 460 470 480
PVGLPAVVTT TMAVGAAYLA KKKAIVQKLS AIESLAGVEI LCSDKTGTLT KNRLSLGEPY
490 500 510 520 530 540
CVEGVSPDDL MLTACLASSR KKKGLDAIDK AFLKALRNYP KAKDQLSKYK VLDFHPFDPV
550 560 570 580 590 600
SKKITAYVEA PDGQRITCVK GAPLWVFKTV QDDHEVPEAI TDAYREQVND MASRGFRSLG
610 620 630 640 650 660
VARKADGKQW EILGIMPCSD PPRHDTARTI HEAIGLGLRI KMLTGDAVGI AKETARQLGM
670 680 690 700 710 720
GTNVYNAERL GLSGGGDMPG SEVNDFVEAA DGFAEVFPQH KYAVVDILQQ RGYLVAMTGD
730 740 750 760 770 780
GVNDAPSLKK ADAGIAVEGA SDAARSAADI VFLAPGLSAI IDALKTSRQI FHRMYAYVVY
790 800 810 820 830 840
RIALSLHLEI FLGLWLIIRN QLLNLELIVF IAIFADVATL AIAYDNAPYA MKPVKWNLPR
850 860 870 880 890 900
LWGLATIVGI LLAIGTWIVN TTMIAQGQNR GIVQNFGVQD EVLFLQISLT ENWLIFITRC
910 920 930 940 950 960
SGPFWSSFPS WQLSGAVLVV DILATLFCIF GWFKGGHQTS IVAVIRIWMY SFGIFCLIAG
970 980 990 1000
VYYILSESSS FDRWMHGKHK ERGTTRKLED FVMQLQRTST HHEAEGKVTS