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2.A.4.2.1 Mitochondrial Co²⁺/Zn²⁺ uptake (into mitochondria) permease. A single mutation (N45I) increases the specificity for Fe²⁺ and decreases it for Co²⁺ (Lin et al., 2008).
Accession Number:	P32798
Protein Name:	Cotl aka YOR316C aka O6131
Length:	439
Molecular Weight:	48155.00
Species:	Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:	5
Location¹ / Topology² / Orientation³:	Mitochondrion membrane¹ / Multi-pass membrane protein²
Substrate	cobalt(2+), iron(2+), zinc(2+)

DIP:	DIP-7554N
RefSeq:	NP_014961.1
Entrez Gene ID:	854494
Pfam:	PF01545
KEGG:	sce:YOR316C
Gene Ontology GO:0000324 C:fungal-type vacuole GO:0016021 C:integral to membrane GO:0031966 C:mitochondrial membrane GO:0015087 F:cobalt ion transmembrane transporter activity GO:0005515 F:protein binding GO:0005385 F:zinc ion transmembrane transporter activity GO:0006882 P:cellular zinc ion homeostasis GO:0006824 P:cobalt ion transport GO:0055085 P:transmembrane transport GO:0006829 P:zinc ion transport
References (7) [1] “COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae.” Conklin D.S.et.al. 1508175 [2] “Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII.” Pearson B.M.et.al. 8896266 [3] “The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.” Dujon B.et.al. 9169874 [4] “Global analysis of protein expression in yeast.” Ghaemmaghami S.et.al. 14562106 [5] “A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.” Hitchcock A.L.et.al. 14557538 [6] “Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.” Chi A.et.al. 17287358 [7] “A multidimensional chromatography technology for in-depth phosphoproteome analysis.” Albuquerque C.P.et.al. 18407956

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FASTA formatted sequence

1:	MKLGSKQVKI ISLLLLDTVF FGIEITTGYL SHSLALIADS FHMLNDIISL VVALWAVNVA 
61:	KNRNPDSTYT YGWKRAEILG ALINAVFLIA LCVSILIEAL QRIIAPPVIE NPKFVLYVGV 
121:	AGLISNTVGL FLFHDNDQEH GHGHGHSHGG IFADHEMHMP SSHTHTHAHV DGIENTTPMD 
181:	STDNISEIMP NAIVDSFMNE NTRLLTPENA SKTPSYSTSS HTIASGGNYT EHNKRKRSLN 
241:	MHGVFLHVLG DALGNIGVML SAFFIWKTDY SWKYYTDPLV SLIITGIIFS SALPLSCKAS 
301:	KILLQATPST LSGDQVEGDL LKIPGIIAIH DFHIWNLTES IFIASLHIQL DISPEQFTDL 
361:	AKIVRSKLHR YGIHSATLQP EFITREVTST ERAGDSQGDH LQNDPLSLRP KTYGTGISGS 
421:	TCLIDDAANC NTADCLEDH

2.A.4.2.1
Mitochondrial Co²⁺/Zn²⁺ uptake (into mitochondria) permease. A single mutation (N45I) increases the specificity for Fe²⁺ and decreases it for Co²⁺ (Lin et al., 2008).

Cross database links:

Gene Ontology

References (7)

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2.A.4.2.1Mitochondrial Co2+/Zn2+ uptake (into mitochondria) permease. A single mutation (N45I) increases the specificity for Fe2+ and decreases it for Co2+ (Lin et al., 2008).

Cross database links:

Gene Ontology

References (7)

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2.A.4.2.1
Mitochondrial Co²⁺/Zn²⁺ uptake (into mitochondria) permease. A single mutation (N45I) increases the specificity for Fe²⁺ and decreases it for Co²⁺ (Lin et al., 2008).