P90747

PR
Gene name
catp-8
Protein name
Probable manganese-transporting ATPase catp-8
Names
Cation transporting ATPase 8
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_C10C6.6
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

827-959 (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 P90747

Entry ID Method Resolution Chain Position Source
AF-P90747-F1 Predicted AlphaFoldDB

No variants for P90747

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P90747

No associated diseases with P90747

3 regional properties for P90747

Type Name Position InterPro Accession
domain DnaJ domain 4 - 80 IPR001623
domain Chaperone DnaJ, C-terminal 120 - 276 IPR002939
conserved_site DnaJ domain, conserved site 46 - 65 IPR018253

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
integral component of endoplasmic reticulum membrane The component of the endoplasmic reticulum 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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

6 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 cation transmembrane 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 + cation(out) = ADP + phosphate + cation(in).
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.
protein transporter activity Directly binding to a specific protein and delivering it to a specific cellular location.

3 GO annotations of biological process

Name Definition
cellular calcium ion homeostasis Any process involved in the maintenance of an internal steady state of calcium ions at the level of a cell.
dendrite morphogenesis The process in which the anatomical structures of a dendrite are generated and organized.
transmembrane transport The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGVDQLVETI IPYNLRSIAT HLYVPPFTII TAIWTYVWLN IFGYEEYYEL GMLGYAAIFV
70 80 90 100 110 120
ILALVLLFCH WMMPVRCFLM CSKQEDVRIA SHVCVIPTQN NGWPELVKLM RTTRDKQTKL
130 140 150 160 170 180
WFEFQRVHYT WDEESREFQT KTLDTAKPMV FFQKSHGFEV EEHVKDAKYL LGDNKTEMIV
190 200 210 220 230 240
PQFLEMFIER ATAPFFVFQV FCVGLWCLED MWYYSLFTLF MLMTFEATLV KQQMKNMSEI
250 260 270 280 290 300
RNMGNKTYMI NVLRGKKWQK IKIEELVAGD IVSIGRGAEE ECVPCDLLLL RGPCIVDESM
310 320 330 340 350 360
LTGESVPQMK EPIEDVEKDK IFDIETDSRL HVIFGGTKIV QHTAPGKAAE GMVKSPDGNC
370 380 390 400 410 420
ICYVIRTGFN TSQGKLLRTI MFGVKKATAN NLETFCFILF LLIFAIAAAA YLWIKGSVDE
430 440 450 460 470 480
TRSKYKLFLE CTLILTSVIP PELPIELSLA VNSSLMALQK LGIFCTEPFR IPFAGKVDIC
490 500 510 520 530 540
CFDKTGTLTT DNLVVEGVAL NNQKEGMIRN AEDLPHESLQ VLASCHSLVR FEEDLVGDPL
550 560 570 580 590 600
EKACLSWCGW NLTKGDAVMP PKTAAKGISG IKIFHRYHFS SAMKRMTVVA GYQSPGTSDT
610 620 630 640 650 660
TFIVAVKGAP EVLRNMYADL PSDYDETYTR LTRQGSRVLA MGIRKLGETR VGELRDKKRE
670 680 690 700 710 720
NFENDLAFAG FVVISCPLKS DTKTMIREIM DSSHVVAMIT GDNPLTACHV SKVLKFTKKS
730 740 750 760 770 780
LPTLVLDEPA DGVDWMWKSV DGTIELPLKP ETKNKMERKA FFNSHEFCLT GSAFHHLVHN
790 800 810 820 830 840
EHTFLRELIL HVKVFARMAP KQKERIINEL KSLGKVTLMC GDGTNDVGAL KHANVGVALL
850 860 870 880 890 900
TNPYDAEKAA EKEKEKKAKI EEARSLVRSG AQLPQRPGAP GAPPAANAAR RDAPPGARAR
910 920 930 940 950 960
APLPPMANAA QARLDNLMKE LEEEEKAQVI KLGDASIAAP FTSKYTSIAS ICHVIKQGRC
970 980 990 1000 1010 1020
TLVTTLQMFK ILALNALVSA YSLSALYLDG VKFSDTQATI QGLLLAACFL FISKSKPLKT
1030 1040 1050 1060 1070 1080
LSRQRPMANI FNAYTLLTVT LQFIVHFSCL LYIVGLAHEA NTEKAPVDLE AKFTPNILNT
1090 1100 1110 1120 1130 1140
TVYIISMALQ VCTFAVNYRG RPFMESLFEN KAMLYSIMFS GGAVFTLASG QATDLMIQFE
1150 1160 1170
LVVLPEALRN ALLMCVTADL VICYIIDRGL NFLLGDMF