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 Q9SA65

Entry ID Method Resolution Chain Position Source
AF-Q9SA65-F1 Predicted AlphaFoldDB

58 variants for Q9SA65

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH04511757 10 I>M No 1000Genomes
ENSVATH04511758 12 A>T No 1000Genomes
ENSVATH00003594 16 Q>K No 1000Genomes
ENSVATH10512028 24 V>F No 1000Genomes
ENSVATH04511760 50 E>G No 1000Genomes
ENSVATH13850508 52 K>R No 1000Genomes
ENSVATH01007943 54 I>F No 1000Genomes
tmp_1_707913_A_C 63 Y>S No 1000Genomes
ENSVATH10512029 92 L>V No 1000Genomes
tmp_1_708002_A_G 93 I>V No 1000Genomes
tmp_1_708015_G_A 97 R>K No 1000Genomes
tmp_1_708063_C_T 113 A>V No 1000Genomes
tmp_1_708071_C_G 116 R>G No 1000Genomes
tmp_1_708083_C_T 120 L>F No 1000Genomes
tmp_1_708133_C_G 136 D>E No 1000Genomes
ENSVATH04511766 167 C>S No 1000Genomes
ENSVATH04511767 213 L>F No 1000Genomes
tmp_1_708501_G_A 221 R>H No 1000Genomes
ENSVATH04511770 231 V>L No 1000Genomes
ENSVATH13850510 274 D>Y No 1000Genomes
ENSVATH00003597 281 K>N No 1000Genomes
ENSVATH04511771 352 E>K No 1000Genomes
tmp_1_708996_G_A 356 E>K No 1000Genomes
tmp_1_709002_G_A 358 E>K No 1000Genomes
ENSVATH04511772 370 P>L No 1000Genomes
ENSVATH01007947 375 D>E No 1000Genomes
ENSVATH04511773 387 V>M No 1000Genomes
tmp_1_709142_T_A 404 N>K No 1000Genomes
tmp_1_709140_A_T 404 N>Y No 1000Genomes
tmp_1_709146_A_C 406 N>H No 1000Genomes
tmp_1_709152_G_T 408 G>C No 1000Genomes
ENSVATH13850512 423 D>E No 1000Genomes
tmp_1_709208_C_A 426 Y>* No 1000Genomes
tmp_1_709222_G_A 431 G>D No 1000Genomes
ENSVATH10512032 440 A>T No 1000Genomes
ENSVATH13850513 454 Q>H No 1000Genomes
tmp_1_709308_T_A 460 S>T No 1000Genomes
ENSVATH04511775 462 Q>H No 1000Genomes
tmp_1_709315_A_C 462 Q>P No 1000Genomes
tmp_1_709353_C_T 475 L>F No 1000Genomes
tmp_1_709368_C_A 480 Q>K No 1000Genomes
ENSVATH04511777 490 T>I No 1000Genomes
ENSVATH04511778 494 Y>C No 1000Genomes
ENSVATH04511778 494 Y>S No 1000Genomes
ENSVATH00003599 499 S>N No 1000Genomes
tmp_1_709443_T_C 505 F>L No 1000Genomes
ENSVATH13850514 513 A>V No 1000Genomes
tmp_1_709619_C_A 520 A>E No 1000Genomes
ENSVATH04511781 522 S>* No 1000Genomes
ENSVATH00003601 522 S>A No 1000Genomes
ENSVATH04511782 527 N>I No 1000Genomes
ENSVATH00003602 528 A>V No 1000Genomes
ENSVATH10512106 531 I>N No 1000Genomes
tmp_1_709666_C_A 536 P>T No 1000Genomes
tmp_1_709684_G_A 542 A>T No 1000Genomes
tmp_1_709699_G_T 547 A>S No 1000Genomes
ENSVATH04511783 589 Q>H No 1000Genomes
tmp_1_709847_C_T 596 T>I No 1000Genomes

No associated diseases with Q9SA65

2 regional properties for Q9SA65

Type Name Position InterPro Accession
domain AP180 N-terminal homology (ANTH) domain 33 - 324 IPR011417
domain ENTH domain 26 - 162 IPR013809

Functions

Description
EC Number
Subcellular Localization
  • Membrane, clathrin-coated pit
  • Golgi apparatus
  • Cytoplasmic vesicle, clathrin-coated vesicle
  • Colocalized with clathrin in the Golgi area
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
clathrin-coated pit A part of the endomembrane system in the form of an invagination of a membrane upon which a clathrin coat forms, and that can be converted by vesicle budding into a clathrin-coated vesicle. Coated pits form on the plasma membrane, where they are involved in receptor-mediated selective transport of many proteins and other macromolecules across the cell membrane, in the trans-Golgi network, and on some endosomes.
clathrin-coated vesicle A vesicle with a coat formed of clathrin connected to the membrane via one of the clathrin adaptor complexes.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
pollen tube A tubular cell projection that is part of a pollen tube cell and extends from a pollen grain.
pollen tube tip The region at growing end of the pollen tube cell, where polarized growth occurs.

4 GO annotations of molecular function

Name Definition
1-phosphatidylinositol binding Binding to a phosphatidylinositol, a glycophospholipid with its sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
clathrin heavy chain binding Binding to a clathrin heavy chain.
phosphatidylinositol-4,5-bisphosphate binding Binding to phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.
SNARE binding Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein.

5 GO annotations of biological process

Name Definition
clathrin coat assembly The process that results in the assembly of clathrin triskelia into the ordered structure known as a clathrin cage.
clathrin-dependent endocytosis An endocytosis process that begins when material is taken up into clathrin-coated pits, which then pinch off to form clathrin-coated endocytic vesicles.
pollen tube growth Growth of pollen via tip extension of the intine wall.
protein localization to plasma membrane A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane.
vesicle budding from membrane The evagination of a membrane, resulting in formation of a vesicle.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8H0W9 At5g10410 Putative clathrin assembly protein At5g10410 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MGSSKFKRAI GAVKDQTSVG LAKVNGRSAS LSELDVAIVK ATRHEEFPAE EKYIREILSL
70 80 90 100 110 120
TSYSRSYINA CVSTLSRRLN KTKCWTVALK TLILIQRLLG EGDQAYEQEI FFATRRGTRL
130 140 150 160 170 180
LNMSDFRDVS RSNSWDYSAF VRTYALYLDE RLDFRMQARH GKRGVYCVGG EADEEEQDQA
190 200 210 220 230 240
AADLSTAIVV RSQPIAEMKT EQIFIRIQHL QQLLDRFLAC RPTGNARNNR VVIVALYPIV
250 260 270 280 290 300
KESFQIYYDV TEIMGILIER FMELDIPDSI KVYDIFCRVS KQFEELDQFY SWCKNMGIAR
310 320 330 340 350 360
SSEYPEIEKI TQKKLDLMDE FIRDKSALEH TKQSKSVKSE ADEDDDEART EEVNEEQEDM
370 380 390 400 410 420
NAIKALPEPP PKEEDDVKPE EEAKEEVIIE KKQEEMGDLL DLGNTNGGEA GQAGDSLALA
430 440 450 460 470 480
LFDGPYASGS GSESGPGWEA FKDDSADWET ALVQTATNLS GQKSELGGGF DMLLLNGMYQ
490 500 510 520 530 540
HGAVNAAVKT STAYGASGSA SSMAFGSAGR PAATMLALPA PSTANGNAGN INSPVPMDPF
550 560 570 580 590
AASLEVAPPA YVQMNDMEKK QRMLMEEQMM WDQYSRDGRQ GHMNLRQNQN QPYSYTPQY