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

2 structures for Q9JIP7

Entry ID Method Resolution Chain Position Source
5A9D X-ray 210 A A/B 391-579 PDB
AF-Q9JIP7-F1 Predicted AlphaFoldDB

52 variants for Q9JIP7

Variant ID(s) Position Change Description Diseaes Association Provenance
rs1133546254 4 S>F No EVA
rs3389342867 10 F>Y No EVA
rs3389354701 21 V>I No EVA
rs45659504 50 N>D No EVA
rs3405466053 65 L>Q No EVA
rs3389350177 66 T>S No EVA
rs3406052333 68 I>S No EVA
rs3404918006 69 L>I No EVA
rs3389342870 90 V>F No EVA
rs3405820638 101 S>R No EVA
rs3404259495 105 D>E No EVA
rs3389359544 112 N>I No EVA
rs3389344065 118 L>H No EVA
rs230063489 127 V>I No EVA
rs3389354759 145 A>T No EVA
rs3389339272 145 A>V No EVA
rs3389300944 169 A>D No EVA
rs3389350179 173 G>E No EVA
rs246030141 235 K>R No EVA
rs3389339290 261 W>R No EVA
rs3389345700 289 P>S No EVA
rs3405819261 299 Q>LTSS* No EVA
rs3389342862 314 K>I No EVA
rs3389350229 321 Q>H No EVA
rs3389320088 326 Q>P No EVA
rs3389350199 404 N>I No EVA
rs1132355378 405 N>S No EVA
rs3389320079 450 T>I No EVA
rs3405819298 453 H>Q No EVA
rs3405254151 454 D>N No EVA
rs3404988053 455 F>L No EVA
rs3404259500 455 F>Y No EVA
rs3405465006 463 L>* No EVA
rs3389339300 477 G>D No EVA
rs3389271568 477 G>S No EVA
rs3405759889 484 K>R No EVA
rs3389300923 501 I>V No EVA
rs3389351932 507 V>I No EVA
rs3389347601 510 N>I No EVA
rs8255954 526 E>K No EVA
rs3389271537 532 N>K No EVA
rs239860901 535 A>E No EVA
rs3389354776 538 P>L No EVA
rs219031338 539 T>N No EVA
rs248399080 545 K>E No EVA
rs232389072 562 A>T No EVA
rs8245291 562 A>V No EVA
rs3389350168 618 V>M No EVA
rs240403848 640 A>G No EVA
rs8255946 664 F>L No EVA
rs3389339320 676 P>S No EVA
rs3389271506 693 G>E No EVA

No associated diseases with Q9JIP7

3 regional properties for Q9JIP7

Type Name Position InterPro Accession
domain Neutral trehalase Ca2+ binding 106 - 135 IPR011120
conserved_site Glycoside hydrolase, family 37, conserved site 299 - 312 IPR018232-1
conserved_site Glycoside hydrolase, family 37, conserved site 623 - 632 IPR018232-2

Functions

Description
EC Number
Subcellular Localization
  • Apical cell membrane ; Multi-pass membrane protein
  • Localized to the apical membrane of enterocytes
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
apical plasma membrane The region of the plasma membrane located at the apical end of the cell.
brush border The dense covering of microvilli on the apical surface of an epithelial cell in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell.
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.
integral component of plasma membrane The component of the plasma 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.

4 GO annotations of molecular function

Name Definition
channel inhibitor activity Binds to and stops, prevents, or reduces the activity of a channel.
dipeptide transmembrane transporter activity Enables the transfer of a dipeptide from one side of a membrane to the other. A dipeptide is a combination of two amino acids linked together by a peptide (-CO-NH-) bond.
peptide:proton symporter activity Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: peptide(out) + H+(out) = peptide(in) + H+(in), up its concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction and is driven by hydrogen ion movement.
proton-dependent oligopeptide secondary active transmembrane transporter activity Enables the transfer of a oligopeptide from one side of a membrane to the other, up its concentration gradient. The transporter binds the solute and undergoes a series of conformational changes. Transport works equally well in either direction and is driven by proton movement.

4 GO annotations of biological process

Name Definition
dipeptide import across plasma membrane The directed movement of a dipeptide from outside of a cell, across the plasma membrane and into the cytosol.
negative regulation of amino acid transport Any process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of amino acids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
oligopeptide transport The directed movement of oligopeptides into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Oligopeptides are molecules that contain a small number (2 to 20) of amino-acid residues connected by peptide linkages.
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P46059 SLC15A1 Solute carrier family 15 member 1 Homo sapiens (Human) PR
Q3E9B5 NPF7.1 Protein NRT1/ PTR FAMILY 7.1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MGMSKSRGCF GYPLSIFFIV VNEFCERFSY YGMRALLVLY FRNFLGWDDN LSTAIYHTFV
70 80 90 100 110 120
ALCYLTPILG ALIADSWLGK FKTIVSLSIV YTIGQAVISV SSINDLTDHD HNGSPDSLPV
130 140 150 160 170 180
HVALSMVGLA LIALGTGGIK PCVSAFGGDQ FEEGQEKQRN RFFSIFYLAI NGGSLLSTII
190 200 210 220 230 240
TPILRVQQCG IHSQQACYPL AFGVPAALMA VALIVFVLGS GMYKKFQPQG NIMGKVAKCI
250 260 270 280 290 300
GFAIKNRFRH RSKAYPKREH WLDWAKEKYD ERLISQIKMV TKVMFLYIPL PMFWALFDQQ
310 320 330 340 350 360
GSRWTLQATT MNGKIGAIEI QPDQMQTVNA ILIVIMVPIV DAVVYPLIAK CGFNFTSLKK
370 380 390 400 410 420
MTVGMFLASM AFVVAAIVQV EIDKTLPVFP GGNQVQIKVL NIGNNNMTVH FPGNSVTLAQ
430 440 450 460 470 480
MSQTDTFMTF DIDKLTSINI SSSGSPGVTT VAHDFEQGHR HTLLVWNPSQ YRVVKDGLNQ
490 500 510 520 530 540
KPEKGENGIR FVNTLNEMVT IKMSGKVYEN VTSHNASGYQ FFPSGEKQYT INTTAVAPTC
550 560 570 580 590 600
LTDFKSSNLD FGSAYTYVIR RASDGCLEVK EFEDIPPNTV NMALQIPQYF LLTCGEVVFS
610 620 630 640 650 660
VTGLEFSYSQ APSNMKSVLQ AGWLLTVAVG NIIVLIVAGA GHFPKQWAEY ILFASLLLVV
670 680 690 700
CVIFAIMARF YTYINPAEIE AQFDEDEKKK GIGKENPYSS LEPVSQTNM