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 Q3SWX5

Entry ID Method Resolution Chain Position Source
AF-Q3SWX5-F1 Predicted AlphaFoldDB

60 variants for Q3SWX5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs517247571 41 S>P No EVA
rs436901297 71 Y>S No EVA
rs469852884 72 Q>R No EVA
rs481017948 73 Y>F No EVA
rs448010932 73 Y>N No EVA
rs466059542 74 V>G No EVA
rs451090417 98 G>R No EVA
rs477601850 132 N>D No EVA
rs524352772 154 D>G No EVA
rs1115370100 274 Q>H No EVA
rs441135229 277 T>N No EVA
rs521933979 299 E>V No EVA
rs723034697 322 Q>K No EVA
rs483309242 383 F>C No EVA
rs443561699 383 F>I No EVA
rs433471179 451 L>V No EVA
rs450974136 456 I>S No EVA
rs479646013 468 Q>* No EVA
rs457822900 473 P>A No EVA
rs439683416 484 N>T No EVA
rs475680802 488 F>L No EVA
rs463599726 500 A>P No EVA
rs464511268 505 L>V No EVA
rs437020238 507 Q>H No EVA
rs452283256 507 Q>K No EVA
rs448165292 510 R>L No EVA
rs448165292 510 R>P No EVA
rs466210850 511 A>D No EVA
rs109184909 512 I>F No EVA
rs477446996 514 K>T No EVA
rs523284838 524 S>P No EVA
rs458888452 541 D>E No EVA
rs450418034 542 N>D No EVA
rs442979816 549 I>S No EVA
rs459375629 551 T>N No EVA
rs474751221 551 T>S No EVA
rs470582205 553 K>E No EVA
rs451945221 554 N>H No EVA
rs437082057 557 N>K No EVA
rs476282066 572 D>E No EVA
rs721641778 597 M>V No EVA
rs454614913 615 A>S No EVA
rs461868968 629 T>K No EVA
rs800860362 638 R>Q No EVA
rs473466247 726 D>A No EVA
rs458009758 728 T>P No EVA
rs136415463 740 Y>C No EVA
rs439549298 757 T>A No EVA
rs475956859 761 D>E No EVA
rs457474345 764 Y>S No EVA
rs442245850 765 D>G No EVA
rs475247754 766 Y>S No EVA
rs433690070 771 G>V No EVA
rs466647455 777 L>V No EVA
rs451353633 778 A>E No EVA
rs432733656 780 M>I No EVA
rs450768528 783 G>A No EVA
rs469318449 783 G>W No EVA
rs468409142 784 V>E No EVA
rs446588206 787 D>V No EVA

No associated diseases with Q3SWX5

8 regional properties for Q3SWX5

Type Name Position InterPro Accession
domain Cadherin, Y-type LIR-motif 723 - 782 IPR000233
domain Cadherin-like 74 - 159 IPR002126-1
domain Cadherin-like 159 - 279 IPR002126-2
domain Cadherin-like 269 - 383 IPR002126-3
domain Cadherin-like 384 - 488 IPR002126-4
domain Cadherin-like 488 - 610 IPR002126-5
conserved_site Cadherin conserved site 256 - 266 IPR020894-1
conserved_site Cadherin conserved site 476 - 486 IPR020894-2

Functions

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

4 GO annotations of cellular component

Name Definition
adherens junction A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules.
catenin complex Complex of peripheral cytoplasmic proteins (alpha-, beta- and gamma-catenin) that interact with the cytoplasmic region of uvomorulin/E-cadherin to connect it to the actin cytoskeleton.
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.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

2 GO annotations of molecular function

Name Definition
cadherin binding Binding to cadherin, a type I membrane protein involved in cell adhesion.
calcium ion binding Binding to a calcium ion (Ca2+).

7 GO annotations of biological process

Name Definition
adherens junction organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an adherens junction. An adherens junction is a cell-cell junction composed of the epithelial cadherin-catenin complex at which the cytoplasmic face of the plasma membrane is attached to actin filaments.
calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules The attachment of one cell to another cell via adhesion molecules that require the presence of calcium for the interaction.
cell morphogenesis The developmental process in which the size or shape of a cell is generated and organized.
cell-cell adhesion via plasma-membrane adhesion molecules The attachment of one cell to another cell via adhesion molecules that are at least partially embedded in the plasma membrane.
cell-cell junction assembly The aggregation, arrangement and bonding together of a set of components to form a junction between cells.
homophilic cell adhesion via plasma membrane adhesion molecules The attachment of a plasma membrane adhesion molecule in one cell to an identical molecule in an adjacent cell.
Notch signaling pathway The series of molecular signals initiated by an extracellular ligand binding to the receptor Notch on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.

42 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P79995 CDH10 Cadherin-10 Gallus gallus (Chicken) PR
Q8UVJ7 CDHR1 Cadherin-related family member 1 Gallus gallus (Chicken) PR
Q5DRC8 PCDHB6 Protocadherin beta-6 Pan troglodytes (Chimpanzee) PR
Q5DRE4 PCDHA8 Protocadherin alpha-8 Pan troglodytes (Chimpanzee) PR
Q5DRE6 PCDHA6 Protocadherin alpha-6 Pan troglodytes (Chimpanzee) PR
Q5DRF0 PCDHA2 Protocadherin alpha-2 Pan troglodytes (Chimpanzee) PR
Q5DRE7 PCDHA5 Protocadherin alpha-5 Pan troglodytes (Chimpanzee) PR
Q9VJB6 CadN2 Putative neural-cadherin 2 Drosophila melanogaster (Fruit fly) PR
Q9ULB4 CDH9 Cadherin-9 Homo sapiens (Human) PR
Q9Y5E3 PCDHB6 Protocadherin beta-6 Homo sapiens (Human) PR
Q9Y5F1 PCDHB12 Protocadherin beta-12 Homo sapiens (Human) PR
O60330 PCDHGA12 Protocadherin gamma-A12 Homo sapiens (Human) PR
P12830 CDH1 Cadherin-1 Homo sapiens (Human) PR
Q9H159 CDH19 Cadherin-19 Homo sapiens (Human) PR
Q9P2E7 PCDH10 Protocadherin-10 Homo sapiens (Human) PR
Q9Y6N8 CDH10 Cadherin-10 Homo sapiens (Human) PR
P19022 CDH2 Cadherin-2 Homo sapiens (Human) PR
Q9Y5I2 PCDHA10 Protocadherin alpha-10 Homo sapiens (Human) PR
Q6ZTQ4 CDHR3 Cadherin-related family member 3 Homo sapiens (Human) PR
Q9Y5H3 PCDHGA10 Protocadherin gamma-A10 Homo sapiens (Human) PR
Q9UN75 PCDHA12 Protocadherin alpha-12 Homo sapiens (Human) PR
Q9Y5I1 PCDHA11 Protocadherin alpha-11 Homo sapiens (Human) PR
Q9Y5I3 PCDHA1 Protocadherin alpha-1 Homo sapiens (Human) PR
Q9Y5H8 PCDHA3 Protocadherin alpha-3 Homo sapiens (Human) PR
Q9Y5H9 PCDHA2 Protocadherin alpha-2 Homo sapiens (Human) PR
Q9UN73 PCDHA6 Protocadherin alpha-6 Homo sapiens (Human) PR
Q9Y5H6 PCDHA8 Protocadherin alpha-8 Homo sapiens (Human) PR
Q9UN74 PCDHA4 Protocadherin alpha-4 Homo sapiens (Human) PR
Q9UN72 PCDHA7 Protocadherin alpha-7 Homo sapiens (Human) PR
Q9Y5H7 PCDHA5 Protocadherin alpha-5 Homo sapiens (Human) PR
Q9Y5G4 PCDHGA9 Protocadherin gamma-A9 Homo sapiens (Human) PR
Q9Y5G0 PCDHGB5 Protocadherin gamma-B5 Homo sapiens (Human) PR
P55285 CDH6 Cadherin-6 Homo sapiens (Human) PR
P09803 Cdh1 Cadherin-1 Mus musculus (Mouse) PR
P15116 Cdh2 Cadherin-2 Mus musculus (Mouse) PR
P70407 Cdh9 Cadherin-9 Mus musculus (Mouse) PR
P70408 Cdh10 Cadherin-10 Mus musculus (Mouse) PR
Q8VHF2 Cdhr5 Cadherin-related family member 5 Mus musculus (Mouse) PR
P97326 Cdh6 Cadherin-6 Mus musculus (Mouse) PR
Q9Z1Y3 Cdh2 Cadherin-2 Rattus norvegicus (Rat) PR
Q767I8 Pcdha4 Protocadherin alpha-4 Rattus norvegicus (Rat) PR
P55280 Cdh6 Cadherin-6 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MRTYRYFLLL FWVGQPYPTF STPLSKRTSG FPAKKRTLEL SGNSKNELSR SKRSWMWNQF
70 80 90 100 110 120
FLLEEYTGSD YQYVGKLHSD QDRGDGSLKY ILSGDGAGDL FIINENTGDI QATKRLDREE
130 140 150 160 170 180
KPVYILRAQA INRKTGRPVE PESEFIIKIH DINDNEPIFT KEVYTATVPE MSDVGTFVVQ
190 200 210 220 230 240
VTATDADDPT YGNSAKVVYS ILQGQPYFSV ESETGIIKTA LLNMDRENRE QYQVVIQAKD
250 260 270 280 290 300
MGGQMGGLSG TTTVNITLTD VNDNPPRFPQ STYQFKTPES SPPGTPIGRI KASDADVGEN
310 320 330 340 350 360
AEIEYSITEG EGLDMFDVIT DQETQEGIIT VKKLLDFEKK KVYTLKVEAS NPHVEPRFLY
370 380 390 400 410 420
LGPFKDSATV RIMVEDVDEP PVFSKLAYIL QIREDAQINT TIGSVTAQDP DAARNPVKYS
430 440 450 460 470 480
VDRHTDMDRI FNIDSGNGSI FTSKLLDRET LLWHNITVIA TEINNPKQSS RVPLYIKVLD
490 500 510 520 530 540
VNDNPPEFAE FYETFVCEKA KADQLIQTLR AIDKDDPYSG HQFSFSLAPE AASGSNFTIQ
550 560 570 580 590 600
DNKDNTAGIF TRKNGYNRHE MSTYLLPVVI SDNDYPVQSS TGTVTVRVCA CDHQGNMQSC
610 620 630 640 650 660
HAEALVHPTG LSTGALIAIL LCIVTLLVTV VLFAALRRQR KKEPLIISKE DIRDNIVSYN
670 680 690 700 710 720
DEGGGEEDTQ AFDIGTLRNP EAIEDSKLRR DIVPEALFLP RRTPAARDNT DVRDFINQRL
730 740 750 760 770 780
KENDTDPTAP PYDSLATYAY EGAGSVADSL SSLESVTTDG DQDYDYLSDW GPRFKKLADM
YGGVDSDKDS