A3LPR9

PR
Gene name
SFH5 (PICST_30049)
Protein name
Phosphatidylinositol transfer protein SFH5
Names
PITP SFH5
Species
Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis)
KEGG Pathway
pic:PICST_30049
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-72 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A3LPR9

Entry ID Method Resolution Chain Position Source
AF-A3LPR9-F1 Predicted AlphaFoldDB

No variants for A3LPR9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A3LPR9

No associated diseases with A3LPR9

1 regional properties for A3LPR9

Type Name Position InterPro Accession
domain CRAL-TRIO lipid binding domain 117 - 294 IPR001251

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Endoplasmic reticulum membrane ; Peripheral membrane protein
  • Microsome membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
phosphatidylinositol transfer activity Removes phosphatidylinositol from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle.

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
MSEPEKTDSV ETVKNTIKST QLTTEHAKKL TQVVNSIPTI LSKLDNSEYD EIFGHRINVD
70 80 90 100 110 120
SKKFVDVAVR NEILLKFLAA DEYDVELATK RLIDTLNWRN KFHPLSAAFD ENFNKALNDL
130 140 150 160 170 180
GAITNFVGLK SDNLNVVTWN FYGATTPKKL FEEYGDNAGT TTNQRPGSQF LRWRIGLMEK
190 200 210 220 230 240
SLQLVDFTDP KNNKIAQVHD YNNVSMFKVD KGMRAATKEI IKIFGDNYPE LLSTKFFINV
250 260 270 280 290 300
PSLMSWVFTF FKTIGVISEA TLKKFQVLNS GNLTEWFGKS NLPPTYGGDS KSSMKELNVA
310 320
SIKLSPYGEY ILEELGKKEI EDVIDEVE