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 P34230

Entry ID Method Resolution Chain Position Source
AF-P34230-F1 Predicted AlphaFoldDB

21 variants for P34230

Variant ID(s) Position Change Description Diseaes Association Provenance
s11-88781 4 T>I No SGRP
s11-88623 57 E>K No SGRP
s11-88590 68 E>K No SGRP
s11-88539 85 D>Y No SGRP
s11-88484 103 G>A No SGRP
s11-88481 104 G>V No SGRP
s11-87843 317 L>V No SGRP
s11-87427 455 E>D No SGRP
s11-87415 459 R>S No SGRP
s11-87401 464 I>T No SGRP
s11-87342 484 N>D No SGRP
s11-87317 492 S>T No SGRP
s11-87122 557 Y>C No SGRP
s11-87048 582 H>D No SGRP
s11-86928 622 S>P No SGRP
s11-86645 716 Y>S No SGRP
s11-86577 739 N>D No SGRP
s11-86418 792 S>P No SGRP
s11-86394 800 A>T No SGRP
s11-86373 807 T>S No SGRP
s11-86351 814 T>I No SGRP

No associated diseases with P34230

3 regional properties for P34230

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 472 - 747 IPR003439
domain AAA+ ATPase domain 497 - 747 IPR003593
domain ABC transporter type 1, transmembrane domain 116 - 383 IPR011527

Functions

Description
EC Number
Subcellular Localization
  • Peroxisome 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
ATP-binding cassette (ABC) transporter complex A complex for the transport of metabolites into and out of the cell, typically comprised of four domains; two membrane-associated domains and two ATP-binding domains at the intracellular face of the membrane, that form a central pore through the plasma membrane. Each of the four core domains may be encoded as a separate polypeptide or the domains can be fused in any one of a number of ways into multidomain polypeptides. In Bacteria and Archaebacteria, ABC transporters also include substrate binding proteins to bind substrate external to the cytoplasm and deliver it to the transporter.
integral component of peroxisomal membrane The component of the peroxisomal 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.
peroxisomal membrane The lipid bilayer surrounding a peroxisome.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

4 GO annotations of molecular function

Name Definition
ABC-type transporter activity Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane.
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.
long-chain fatty acid transporter activity Enables the transfer of long-chain fatty acids from one side of a membrane to the other. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22.

7 GO annotations of biological process

Name Definition
fatty acid beta-oxidation A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
fatty acid transmembrane transport The process in which a fatty acid is transported across a membrane.
fatty-acyl-CoA transport The directed movement of fatty acyl coenzyme A into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Fatty acyl coenzyme A is an acyl group linked to 3'-phosphoadenosine-(5')diphospho(4')pantatheine (coenzyme A).
long-chain fatty acid catabolic process The chemical reactions and pathways resulting in the breakdown of long-chain fatty acids, a fatty acid with a chain length between C13 and C22.
long-chain fatty acid import into peroxisome The directed movement of long-chain fatty acids into a peroxisome. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22.
peroxisome organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a peroxisome. A peroxisome is a small, membrane-bounded organelle that uses dioxygen (O2) to oxidize organic molecules.
very long-chain fatty acid catabolic process The chemical reactions and pathways resulting in the breakdown of a fatty acid which has a chain length greater than C22.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P31826 yddA Inner membrane ABC transporter ATP-binding protein YddA Escherichia coli (strain K12) PR
P33897 ABCD1 ATP-binding cassette sub-family D member 1 Homo sapiens (Human) PR
Q9UBJ2 ABCD2 ATP-binding cassette sub-family D member 2 Homo sapiens (Human) PR
P48410 Abcd1 ATP-binding cassette sub-family D member 1 Mus musculus (Mouse) PR
Q61285 Abcd2 ATP-binding cassette sub-family D member 2 Mus musculus (Mouse) PR
Q9QY44 Abcd2 ATP-binding cassette sub-family D member 2 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MISTASAFYQ KHRVNLLRSS YIILLLATLY NSNSSSSNNK TDKKDSESTV LENKKIEEGK
70 80 90 100 110 120
ETAVDREEDE SSKEELTIVS KHSTDSEDGA IIIDKESKTN HKGGERKGKV DFLFKLLLHD
130 140 150 160 170 180
KKCLILFITQ AILLNIRTLL SLRVATLDGQ LVSTLVRAQY ANFTKILLGK WMILGIPASF
190 200 210 220 230 240
INSLISYTTK LCAVTINRKV SDFLLSKYLS NHHTFYSVAS AESVSEIQDN LTKDIYTFSM
250 260 270 280 290 300
NSSLLLNQLL KPMLDLILCS FKLLTSNTSV MGEGTLALGL IVYASNSLLK LIQPNFTRLT
310 320 330 340 350 360
MASASLESWF RSLHSNLHSS NEEIALLRGQ KRELENVDYS FYRLVLFLNR EIKARAIYDV
370 380 390 400 410 420
ATAFVIKYTW GAAGLVLCSI PIFFKNKPSE DTLQLKEPGN DMTADFITNR RLLVTASSSI
430 440 450 460 470 480
GRFVELKRNI QQLRGIRLRL NKFNDLLDAN KGDDEKEPRD ERCIVEYDDS RIKFENIPLI
490 500 510 520 530 540
TPANQVLVPE LSFDLKHGNH LLIIGPNGCG KSSLFRILGG LWPIRATPNK NHQSKLIMPR
550 560 570 580 590 600
RTVDRDCAIF YLPQRPYMGN RSTFREQIIY PDSIEQFKER YHNDYDLGDA DLIKILQLLD
610 620 630 640 650 660
LEDLVTENMS LLLAQRTSKN DSQQLSTEDN QSPCAIKVRD AFSIVRNWSE ELTIGVQQRL
670 680 690 700 710 720
AMARMYYHKP KFAVLDECTS AVAPEMEQRM YENAQNFGIS LISVCHRTSL WHFHNYLLKF
730 740 750 760 770 780
DGKGGYQFGP FNPKERLCNE EKLLELNAIL DQQVPLWERK LKDLTIAKES NIIRKSETNL
790 800 810 820 830 840
NLFEKIEDPK TSKSNALFNA NKGQRITSPT GQETSKRLPL FSQPSSSASS NLLRNNKSLN
850
KKVKTKKEEG KER