ISC1/YER019W Protein Information

Standard Name	Isc1p
Systematic Name	Yer019wp
ORF Classification	Verified
Description	Mitochondrial membrane localized inositol phosphosphingolipid phospholipase C, hydrolyzes complex sphingolipids to produce ceramide; activated by phosphatidylserine, cardiolipin, and phosphatidylglycerol; mediates Na+ and Li+ halotolerance (1, 2, 3)
Name Description	Inositol phosphoSphingolipid phospholipase C 1

Experimental Data
Molecules/cell	2170 4

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	477
Molecular Weight (Da)	53,940
Isoelectric Point (pI)	7.5

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Isc1p (InterPro)
Transmembrane Domains	There are 2 total predicted transmembrane domains (TMHMM)
Physical Interactions	There are 4 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000012D8CF \| P40015 MIPS: YER019W NCBI: 603611 \| 6320856 \| 731443 \| NP_010935.1 GenBank/EMBL/DDBJ: DAA07671.1 \| U18778
External Classifications	EC: 3.1.4.- [Phosphoric Diester Hydrolases]

Amino Acid Sequence (or in FASTA format)
1 MYNRKDRDVH ERKEDGQSEF EALNGTNAIM SDNSKAYSIK FLTFNTWGLK 51 YVSKHRKERL RAIADKLAGH SMLTPISDEL LPNGGDSNEN EDYDVIALQE 101 IWCVEDWKYL ASACASKYPY QRLFHSGILT GPGLAILSKV PIESTFLYRF 151 PINGRPSAVF RGDWYVGKSI AITVLNTGTR PIAIMNSHMH APYAKQGDAA 201 YLCHRSCQAW DFSRLIKLYR QAGYAVIVVG DLNSRPGSLP HKFLTQEAGL 251 VDSWEQLHGK QDLAVIARLS PLQQLLKGCT TCDSLLNTWR AQRQPDEACR 301 LDYALIDPDF LQTVDAGVRF TERIPHLDCS VSDHFAYSCT LNIVPQGTES 351 RPSTSVKRAK THDRELILQR YSNYETMIEC IHTYLKTAQR QKFFRGLHFW 401 ASILLLIASL VVTTFTANKA GWSSIFWVLF AIAVSISGTI DGAISFLFGR 451 SEIRALIEVE QEVLDAEHHL QTFLSEK*

Amino Acid Sequence (or in FASTA format)

       1  MYNRKDRDVH ERKEDGQSEF EALNGTNAIM SDNSKAYSIK FLTFNTWGLK
      51  YVSKHRKERL RAIADKLAGH SMLTPISDEL LPNGGDSNEN EDYDVIALQE
     101  IWCVEDWKYL ASACASKYPY QRLFHSGILT GPGLAILSKV PIESTFLYRF
     151  PINGRPSAVF RGDWYVGKSI AITVLNTGTR PIAIMNSHMH APYAKQGDAA
     201  YLCHRSCQAW DFSRLIKLYR QAGYAVIVVG DLNSRPGSLP HKFLTQEAGL
     251  VDSWEQLHGK QDLAVIARLS PLQQLLKGCT TCDSLLNTWR AQRQPDEACR
     301  LDYALIDPDF LQTVDAGVRF TERIPHLDCS VSDHFAYSCT LNIVPQGTES
     351  RPSTSVKRAK THDRELILQR YSNYETMIEC IHTYLKTAQR QKFFRGLHFW
     401  ASILLLIASL VVTTFTANKA GWSSIFWVLF AIAVSISGTI DGAISFLFGR
     451  SEIRALIEVE QEVLDAEHHL QTFLSEK*

external links for Isc1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Candida (CGD)	BioPIXIE	MIPS
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Isc1p

1)	Sawai H, et al. (2000) Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae. J Biol Chem 275(50):39793-8
2)	Betz C, et al. (2002) ISC1-encoded inositol phosphosphingolipid phospholipase C is involved in Na+/Li+ halotolerance of Saccharomyces cerevisiae. Eur J Biochem 269(16):4033-9
3)	Okamoto Y, et al. (2002) Structural requirements for selective binding of ISC1 to anionic phospholipids. J Biol Chem 277(48):46470-7
4)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41