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 Q61609

Entry ID Method Resolution Chain Position Source
AF-Q61609-F1 Predicted AlphaFoldDB

16 variants for Q61609

Variant ID(s) Position Change Description Diseaes Association Provenance
rs27433473 101 E>K No EVA
rs27433472 103 Q>R No EVA
rs3388586223 120 W>* No EVA
rs27433446 336 R>W No EVA
rs3388592740 369 V>I No EVA
rs3388592576 394 L>R No EVA
rs3388593996 422 T>N No EVA
rs3388577447 497 K>E No EVA
rs3388585086 500 S>C No EVA
rs27433443 500 S>N No EVA
rs27433442 507 Y>C No EVA
rs3388586199 542 I>N No EVA
rs3388586176 622 I>S No EVA
rs3388590397 644 V>I No EVA
rs3388590114 679 L>V No EVA
rs3388590442 680 P>Q No EVA

No associated diseases with Q61609

1 regional properties for Q61609

Type Name Position InterPro Accession
domain Major facilitator superfamily domain 320 - 539 IPR020846

Functions

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

2 GO annotations of cellular component

Name Definition
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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
high-affinity inorganic phosphate:sodium symporter activity Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: HPO42-(out) + Na+(out) = HPO42-(in) + Na+(in). In high-affinity transport the transporter is able to bind the solute even if it is only present at very low concentrations.
inorganic phosphate transmembrane transporter activity Enables the transfer of a inorganic phosphate 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 a chemiosmotic source of energy. Secondary active transporters include symporters and antiporters.

4 GO annotations of biological process

Name Definition
biomineral tissue development Formation of hard tissues that consist mainly of inorganic compounds, and also contain a small amounts of organic matrices that are believed to play important roles in their formation.
phosphate ion transmembrane transport The process in which a phosphate is transported across a membrane.
phosphate ion transport The directed movement of phosphate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
sodium ion transport The directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q95L97 SLC20A2 Sodium-dependent phosphate transporter 2 Felis catus (Cat) (Felis silvestris catus) PR
O97596 Slc20a1 Sodium-dependent phosphate transporter 1 Felis catus (Cat) (Felis silvestris catus) PR
Q08357 SLC20A2 Sodium-dependent phosphate transporter 2 Homo sapiens (Human) PR
Q8WUM9 SLC20A1 Sodium-dependent phosphate transporter 1 Homo sapiens (Human) PR
Q5BL44 slc20a1 Sodium-dependent phosphate transporter 1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MESTVATITS TLAAVTASAP PKYDNLWMLI LGFIIAFVLA FSVGANDVAN SFGTAVGSGV
70 80 90 100 110 120
VTLKQACILA SIFETVGSAL LGAKVSETIR NGLIDVELYN ETQDLLMAGS VSAMFGSAVW
130 140 150 160 170 180
QLVASFLKLP ISGTHCIVGA TIGFSLVANG QKGVKWSELI KIVMSWFVSP LLSGIMSGIL
190 200 210 220 230 240
FFLVRAFILR KADPVPNGLR ALPIFYACTI GINLFSIMYT GAPLLGFDKL PLWGTILISV
250 260 270 280 290 300
GCAVFCALIV WFFVCPRMKR KIEREVKSSP SESPLMEKKS NLKEDHEETK MAPGDVEHRN
310 320 330 340 350 360
PVSEVVCATG PLRAVVEERT VSFKLGDLEE APERERLPMD LKEETSIDST INGAVQLPNG
370 380 390 400 410 420
NLVQFSQTVS NQINSSGHYQ YHTVHKDSGL YKELLHKLHL AKVGDCMGDS GDKPLRRNNS
430 440 450 460 470 480
YTSYTMAICG MPLDSFRAKE GEQKGDEMET LTWPNADTKK RIRMDSYTSY CNAVSDLHSE
490 500 510 520 530 540
SEMDMSVKAE MGLGDRKGSS GSLEEWYDQD KPEVSLLFQF LQILTACFGS FAHGGNDVSN
550 560 570 580 590 600
AIGPLVALYL VYKQEASTKA ATPIWLLLYG GVGICMGLWV WGRRVIQTMG KDLTPITPSS
610 620 630 640 650 660
GFSIELASAL TVVIASNIGL PISTTHCKVG SVVSVGWLRS KKAVDWRLFR NIFMAWFVTV
670 680
PISGVISAAI MAVFKYIILP V