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 Q8EJZ5

Entry ID Method Resolution Chain Position Source
AF-Q8EJZ5-F1 Predicted AlphaFoldDB

No variants for Q8EJZ5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8EJZ5

No associated diseases with Q8EJZ5

4 regional properties for Q8EJZ5

Type Name Position InterPro Accession
domain PKD domain 808 - 880 IPR000601
domain VPS10 196 - 797 IPR006581
domain Sortilin, C-terminal 638 - 792 IPR031777
domain Sortilin, N-terminal 206 - 634 IPR031778

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
catalytic activity Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
iron ion binding Binding to an iron (Fe) ion.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQVESTLFSH PKYWAECFGT APFLPMSRKE MEKLGWDSCD IIIVTGDAYV DHPSFGMAVI
70 80 90 100 110 120
GRMLEAQGYR VGIIAQPDWS SKDAFMQLGR PNLFFGVTAG NMDSMINRYT ADRRIRSDDA
130 140 150 160 170 180
YTPGDVGGKR PDRAVTVYTQ RCKEAFKDVP VIIGGIEASL RRIAHYDYWS DKVRRSVIFD
190 200 210 220 230 240
AKADILMYGN AERPLAEVAR RLAAGEAIAD IQDVRGTAVI RKEPMPEWRG MDSRKIDQLH
250 260 270 280 290 300
KIDPIPNPYG ADDVGCANLS GPSDAKIFDN DAPKPISVQP PRPKPWDKTY VLLPAFEKVS
310 320 330 340 350 360
EDKYLYAHAS RILHQEQNPG CARALFQPHG DRGVWVNPPA WPLNTDEMDA VFDLPYKRVP
370 380 390 400 410 420
HPAYGKEKIP AYDMIKTSIN IMRGCFGGCS FCSITEHEGR IIQSRSQESI IKEIKDIQDK
430 440 450 460 470 480
VPGFTGVISD LGGPTANMYR LGCTSEKAEK TCRRLSCVYP SICGHLGTDH KHTIDLYRAA
490 500 510 520 530 540
RAVPGIKKIL IASGVRYDLA IEDPAYVKEL VQHHVGGYLK IAPEHTEEGP LSKMMKPGMG
550 560 570 580 590 600
AYDKFKELFD KFSKEAGKEQ FLIPYFISAH PGTTDEDMLN LALWLKERKF KLDQVQNFYP
610 620 630 640 650 660
SPMANATTIY HTELNSLKNV KHTSEVVPVP KKGRQRRLHK ALLRYHDPAG WPIIREGLIA
670 680 690 700 710 720
MGREDLIGNS PNHLVPPEGR NERGPKWMKD ANQGQKALTR FSGNQFDERK GKGDAKGKPS
730 740 750 760 770 780
ASKPKGPKSG ANAPQSQQPK TSRPGAKAPF GQSGFKGKAE QGKAGQNKAG HQGRAGKASS
GRQQAK