P14772

PR
Gene name
BPT1 (YLL015W, L1313)
Protein name
Bile pigment transporter 1
Names
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YLL015W
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

839-986 (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 P14772

Entry ID Method Resolution Chain Position Source
AF-P14772-F1 Predicted AlphaFoldDB

32 variants for P14772

Variant ID(s) Position Change Description Diseaes Association Provenance
s12-116598 56 N>K No SGRP
s12-116612 61 R>I No SGRP
s12-116635 69 P>S No SGRP
s12-116934 168 E>D No SGRP
s12-116959 177 T>A No SGRP
s12-117243 271 L>F No SGRP
s12-117390 320 L>F No SGRP
s12-117589 387 E>K No SGRP
s12-117706 426 T>A No SGRP
s12-118242 604 D>E No SGRP
s12-118321 631 T>A No SGRP
s12-118336 636 G>R No SGRP
s12-118517 696 R>K No SGRP
s12-118639 737 D>N No SGRP
s12-118657 743 I>V No SGRP
s12-118664 745 A>V No SGRP
s12-118864 812 V>I No SGRP
s12-118975 849 I>V No SGRP
s12-118984 852 Q>K No SGRP
s12-119011 861 R>G No SGRP
s12-119099 890 E>G No SGRP
s12-119170 914 V>I No SGRP
s12-119275 949 K>Q No SGRP
s12-119290 954 K>E No SGRP
s12-119329 967 I>V No SGRP
s12-119422 998 N>D No SGRP
s12-119509 1027 I>L No SGRP
s12-120194 1255 W>* No SGRP
s12-120215 1262 T>M No SGRP
s12-120271 1281 P>S No SGRP
s12-120325 1299 K>E No SGRP
s12-120493 1355 P>A No SGRP

2 associated diseases with P14772

[MIM: 614893]: Immunodeficiency 32A (IMD32A)

An immunologic disorder characterized by abnormal peripheral blood myeloid phenotype with a marked loss of CD11C-positive/CD1C dendritic cells, resulting in selective susceptibility to mycobacterial infections. {ECO:0000269|PubMed:21524210}. Note=The disease is caused by variants affecting the gene represented in this entry.

[MIM: 226990]: Immunodeficiency 32B (IMD32B)

An autosomal recessive primary immunodeficiency characterized by monocyte and dendritic cell deficiency, myeloproliferation, and susceptibility to severe opportunistic infections, including disseminated BCG infection and oral candidiasis. {ECO:0000269|PubMed:21524210, ECO:0000269|PubMed:25122610}. Note=The disease is caused by variants affecting the gene represented in this entry.

Without disease ID
  • An immunologic disorder characterized by abnormal peripheral blood myeloid phenotype with a marked loss of CD11C-positive/CD1C dendritic cells, resulting in selective susceptibility to mycobacterial infections. {ECO:0000269|PubMed:21524210}. Note=The disease is caused by variants affecting the gene represented in this entry.
  • An autosomal recessive primary immunodeficiency characterized by monocyte and dendritic cell deficiency, myeloproliferation, and susceptibility to severe opportunistic infections, including disseminated BCG infection and oral candidiasis. {ECO:0000269|PubMed:21524210, ECO:0000269|PubMed:25122610}. Note=The disease is caused by variants affecting the gene represented in this entry.

5 regional properties for P14772

Type Name Position InterPro Accession
domain Ras-associating domain 779 - 866 IPR000159
domain Ras-like guanine nucleotide exchange factor, N-terminal 111 - 239 IPR000651
domain Ras guanine-nucleotide exchange factors catalytic domain 363 - 630 IPR001895
domain Ral guanine nucleotide dissociation stimulator, RA domain 779 - 864 IPR015758
conserved_site Ras guanine-nucleotide exchange factor, conserved site 545 - 575 IPR019804

Functions

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

5 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).
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.

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.

4 GO annotations of biological process

Name Definition
bilirubin transport The directed movement of bilirubin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
cadmium ion transport The directed movement of cadmium (Cd) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
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.

13 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P38735 VMR1 ABC transporter ATP-binding protein/permease VMR1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P0CE68 NFT1 ABC transporter NFT1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q8HXQ5 ABCC1 Multidrug resistance-associated protein 1 Bos taurus (Bovine) PR
Q6UR05 ABCC1 Multidrug resistance-associated protein 1 Canis lupus familiaris (Dog) (Canis familiaris) PR
Q92887 ABCC2 ATP-binding cassette sub-family C member 2 Homo sapiens (Human) SS
O15438 ABCC3 ATP-binding cassette sub-family C member 3 Homo sapiens (Human) PR
O95255 ABCC6 ATP-binding cassette sub-family C member 6 Homo sapiens (Human) PR
P33527 ABCC1 Multidrug resistance-associated protein 1 Homo sapiens (Human) PR
Q8VI47 Abcc2 ATP-binding cassette sub-family C member 2 Mus musculus (Mouse) SS
B2RX12 Abcc3 ATP-binding cassette sub-family C member 3 Mus musculus (Mouse) PR
O35379 Abcc1 Multidrug resistance-associated protein 1 Mus musculus (Mouse) PR
Q63120 Abcc2 ATP-binding cassette sub-family C member 2 Rattus norvegicus (Rat) EV
Q8CG09 Abcc1 Multidrug resistance-associated protein 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSSLEVVDGC PYGYRPYPDS GTNALNPCFI SVISAWQAVF FLLIGSYQLW KLYKNNKVPP
70 80 90 100 110 120
RFKNFPTLPS KINSRHLTHL TNVCFQSTLI ICELALVSQS SDRVYPFILK KALYLNLLFN
130 140 150 160 170 180
LGISLPTQYL AYFKSTFSMG NQLFYYMFQI LLQLFLILQR YYHGSSNERL TVISGQTAMI
190 200 210 220 230 240
LEVLLLFNSV AIFIYDLCIF EPINELSEYY KKNGWYPPVH VLSYITFIWM NKLIVETYRN
250 260 270 280 290 300
KKIKDPNQLP LPPVDLNIKS ISKEFKANWE LEKWLNRNSL WRAIWKSFGR TISVAMLYET
310 320 330 340 350 360
TSDLLSVVQP QFLRIFIDGL NPETSSKYPP LNGVFIALTL FVISVVSVFL TNQFYIGIFE
370 380 390 400 410 420
AGLGIRGSLA SLVYQKSLRL TLAERNEKST GDILNLMSVD VLRIQRFFEN AQTIIGAPIQ
430 440 450 460 470 480
IIVVLTSLYW LLGKAVIGGL VTMAIMMPIN AFLSRKVKKL SKTQMKYKDM RIKTITELLN
490 500 510 520 530 540
AIKSIKLYAW EEPMMARLNH VRNDMELKNF RKIGIVSNLI YFAWNCVPLM VTCSTFGLFS
550 560 570 580 590 600
LFSDSPLSPA IVFPSLSLFN ILNSAIYSVP SMINTIIETS VSMERLKSFL LSDEIDDSFI
610 620 630 640 650 660
ERIDPSADER ALPAIEMNNI TFLWKSKEVL TSSQSGDNLR TDEESIIGSS QIALKNIDHF
670 680 690 700 710 720
EAKRGDLVCV VGRVGAGKST FLKAILGQLP CMSGSRDSIP PKLIIRSSSV AYCSQESWIM
730 740 750 760 770 780
NASVRENILF GHKFDQDYYD LTIKACQLLP DLKILPDGDE TLVGEKGISL SGGQKARLSL
790 800 810 820 830 840
ARAVYSRADI YLLDDILSAV DAEVSKNIIE YVLIGKTALL KNKTIILTTN TVSILKHSQM
850 860 870 880 890 900
IYALENGEIV EQGNYEDVMN RKNNTSKLKK LLEEFDSPID NGNESDVQTE HRSESEVDEP
910 920 930 940 950 960
LQLKVTESET EDEVVTESEL ELIKANSRRA SLATLRPRPF VGAQLDSVKK TAQKAEKTEV
970 980 990 1000 1010 1020
GRVKTKIYLA YIKACGVLGV VLFFLFMILT RVFDLAENFW LKYWSESNEK NGSNERVWMF
1030 1040 1050 1060 1070 1080
VGVYSLIGVA SAAFNNLRSI MMLLYCSIRG SKKLHESMAK SVIRSPMTFF ETTPVGRIIN
1090 1100 1110 1120 1130 1140
RFSSDMDAVD SNLQYIFSFF FKSILTYLVT VILVGYNMPW FLVFNMFLVV IYIYYQTFYI
1150 1160 1170 1180 1190 1200
VLSRELKRLI SISYSPIMSL MSESLNGYSI IDAYDHFERF IYLNYEKIQY NVDFVFNFRS
1210 1220 1230 1240 1250 1260
TNRWLSVRLQ TIGATIVLAT AILALATMNT KRQLSSGMVG LLMSYSLEVT GSLTWIVRTT
1270 1280 1290 1300 1310 1320
VTIETNIVSV ERIVEYCELP PEAQSINPEK RPDENWPSKG GIEFKNYSTK YRENLDPVLN
1330 1340 1350 1360 1370 1380
NINVKIEPCE KVGIVGRTGA GKSTLSLALF RILEPTEGKI IIDGIDISDI GLFDLRSHLA
1390 1400 1410 1420 1430 1440
IIPQDAQAFE GTVKTNLDPF NRYSEDELKR AVEQAHLKPH LEKMLHSKPR GDDSNEEDGN
1450 1460 1470 1480 1490 1500
VNDILDVKIN ENGSNLSVGQ RQLLCLARAL LNRSKILVLD EATASVDMET DKIIQDTIRR
1510 1520 1530 1540 1550
EFKDRTILTI AHRIDTVLDS DKIIVLDQGS VREFDSPSKL LSDKTSIFYS LCEKGGYLK