Q5A762
Gene name |
MLT1 (ABC1, BPT1, YCF1) |
Protein name |
Multiple drug resistance-associated protein-like transporter 1 |
Names |
MRP-like transporter 1, Vacuolar multi-drug resistance ABC transporter MTL1 |
Species |
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
KEGG Pathway |
cal:CAALFM_C108210CA |
EC number |
|
Protein Class |
|
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 Q5A762
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5A762-F1 | Predicted | AlphaFoldDB |
No variants for Q5A762
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5A762 | |||||
No associated diseases with Q5A762
10 regional properties for Q5A762
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ABC transporter-like, ATP-binding domain | 672 - 905 | IPR003439-1 |
| domain | ABC transporter-like, ATP-binding domain | 1345 - 1600 | IPR003439-2 |
| domain | AAA+ ATPase domain | 696 - 898 | IPR003593-1 |
| domain | AAA+ ATPase domain | 1371 - 1577 | IPR003593-2 |
| domain | ABC transporter type 1, transmembrane domain | 326 - 613 | IPR011527-1 |
| domain | ABC transporter type 1, transmembrane domain | 1027 - 1308 | IPR011527-2 |
| conserved_site | ABC transporter-like, conserved site | 805 - 819 | IPR017871-1 |
| conserved_site | ABC transporter-like, conserved site | 1502 - 1516 | IPR017871-2 |
| domain | ABC transporter C family, six-transmembrane helical domain 2 | 1023 - 1320 | IPR044726 |
| domain | ABC transporter C family, six-transmembrane helical domain 1 | 327 - 621 | IPR044746 |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| fungal-type vacuole | A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure. |
| fungal-type vacuole membrane | The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae. |
| 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. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| 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 |
|---|---|
| ABC-type peptide transporter activity | Catalysis of the reaction: ATP + H2O + peptide(in) = ADP + phosphate + peptide(out). Peptides exported include alpha-hemolysin, cyclolysin, colicin V and siderophores from Gram-negative bacteria, and bacteriocin, subtilin, competence factor and pediocin from Gram-positive bacteria. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATPase-coupled transmembrane transporter activity | Primary active transporter of a solute across a membrane, via the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of a substance across a membrane. The transport protein may be transiently phosphorylated (P-type transporters), or not (ABC-type transporters and other families of transporters). Primary active transport occurs up the solute's concentration gradient and is driven by a primary energy source. |
| bilirubin transmembrane transporter activity | Enables the transfer of bilirubin from one side of a membrane to the other. Bilirubin is a linear tetrapyrrole produced in the reticuloendothelial system from biliverdin and transported to the liver as a complex with serum albumin. In the liver, bilirubin is converted to bilirubin bisglucuronide, which is excreted in the bile. |
| cadmium ion transmembrane transporter activity | Enables the transfer of cadmium (Cd) ions from one side of a membrane to the other. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to starvation | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of nourishment. |
| filamentous growth | The process in which a multicellular organism, a unicellular organism or a group of unicellular organisms grow in a threadlike, filamentous shape. |
| filamentous growth of a population of unicellular organisms in response to biotic stimulus | The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a biotic (living) stimulus. |
| filamentous growth of a population of unicellular organisms in response to starvation | The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to deprivation of nourishment. |
| transmembrane transport | The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other. |
| vacuole fusion, non-autophagic | The fusion of two vacuole membranes to form a single vacuole. |
| xenobiotic detoxification by transmembrane export across the plasma membrane | A process that reduces or removes the toxicity of a xenobiotic by exporting it outside the cell. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNESNRELIL | GLSPVHLSLF | NSESLLHTFN | FFGVGDGQAN | IASNYVTASK | FVIPQPLYSP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HGNALNPAFV | ELIGQAVNTF | FAIFMLFQLT | RLLLTKKKSH | RIYTPTPFSQ | TLKISLVLLQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VILVASLYFL | NKNSYFIGGI | AATVLALILH | LVEFRRSPIA | IESLLTYWSA | NTAFTFAVFI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QDSYSKHKIY | ANSGPAYVIE | IISLVNSFLI | FVFEVGYYKP | GFEITNEKFL | DTVNLFSYFT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FYYLQPLINK | IYATDDVQLT | DLPDILGNIT | CDDTKAKVAK | AWEEELKRTK | KPGLVSKVWS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FVTRRKVNSK | PQMFLAIAKA | FFDKFAISIT | LAIIVTGLSF | LQPFLLRKFI | QFFSTYFYSV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EKPPIIIGYF | WASVMFLTSV | ANFIAFNQAF | KTQFDLGYEI | QSSLTTLIYE | KALRLSPQSR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KNKPTGDIIN | HITMDIDIIF | WFCWQLGEYL | ASPLKLAVCL | AALYKLFSNA | TWAGVITAII |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VAPLATLVNA | SMSKNYIQLM | KDKDERTSLI | TEILNSAKSI | KFYSWEKPML | ARLSHIRNDR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ELNNIKKIGV | VSALAQFLWS | CIPFFISCAT | YATYAYFYNV | PLTPDIVFPA | LALFDLLSEP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MLLIPSFIVE | VIEVSTSLAR | IGELLCLDEL | ADDQHGYVKR | DPEPNDNSIY | SVIVKDATFV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| WSEETQQKQY | TDEESEVQEV | PASNVALKNI | NFSARKGELA | CIVGKVGSGK | STLIKAILGD |
| 730 | 740 | 750 | 760 | 770 | 780 |
| VPIKIPSYSD | DSTNPTPSVE | TFGSIAYCPQ | NPWILNGTVK | ENILFGHKYD | AEFYQKTIDA |
| 790 | 800 | 810 | 820 | 830 | 840 |
| CELISDFKNL | PDGDQTVVGE | KGISLSGGQK | ARISLARSVY | TRADIYLLDD | ILSAVDAHVG |
| 850 | 860 | 870 | 880 | 890 | 900 |
| KNIIKKVLSN | EGLIGNRCRI | LATNSVPVLH | EANDIYLIAG | GAFVEHGKFK | EVMKRNGDLA |
| 910 | 920 | 930 | 940 | 950 | 960 |
| KLIKEYGRKK | DEPTEEETTE | ASTEPKEEDH | SNGKSDTAVH | DELDTDELVD | EIVDYVGEQN |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| RGVVEQAILR | RASVVSYGHN | YENDEADNGQ | IRKTRHEQEE | SRKGTVPWDI | FKQYIIACDY |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| KYFSFYVAAT | FSVVLISAGE | KYLLSYWSQL | NSEQNDTVEP | VFFLGTYATL | GVVSGFLTYM |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| GALVIWSYCI | VKGSTYFHNK | MAESVLRSPM | SFFDTTPIGR | ILNRFTEDIG | KIDMNLPWTI |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| ISFITTLLNG | FVTFGVILSF | LPLMLVVIVS | LLFVYNYFRI | RFVPTTRELK | RLESIAKSPV |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| LATIQESING | VETIKAFHQR | ERFVYKSKKL | IDEKTLIGVV | QQNCNRWLSM | RLQTISSSIM |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| FFTALLAVVT | LGGKHPILPS | ILGFVMTYSM | SITYILNSLV | RIWAEMQAGG | VAIERIIEYC |
| 1330 | 1340 | 1350 | 1360 | 1370 | 1380 |
| DLPSEAPMII | EDKRPQDSWP | AHGVVKFKKY | STAYRKHLDP | VLREIELTIN | SKEKVGIVGR |
| 1390 | 1400 | 1410 | 1420 | 1430 | 1440 |
| TGAGKSSLTL | ALFRIIEATG | GNIEIDGVDT | SQIGLYDLRH | HLTIIPQEAH | TFRASVRENL |
| 1450 | 1460 | 1470 | 1480 | 1490 | 1500 |
| DPFGEYSDDK | LWKVLELAHL | KEHVTKMETD | PTEEEKKASK | NPDELSKKVG | LDAQIEEGGS |
| 1510 | 1520 | 1530 | 1540 | 1550 | 1560 |
| NLSSGQKQLL | CLARALLNET | SKILVLDEAT | AAVDFQTDKI | IQETIRTEFK | DKTILTIAHR |
| 1570 | 1580 | 1590 | 1600 | ||
| IDTIMDSDKI | LVLDSGKVAE | FDSPQNLLKN | KDSIFYSLAK | EGGYID |