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2.A.3.10.2
General amino acid permease (all L-amino acids and some D-amino acids as well as β-alanine, polyamines and GABA). Systematic mutational analysis of the intracellular regions of yeast Gap1 permease revealed multiple intracellular regions involved in its secretion, transport activity, and down-regulation (Igarashi and Kashiwagi 2010; Merhi et al., 2011). GAP1 is a "transceptor", fuctioning in both transport and reception, necessary for cAMP-independent activation of the Protein Kinase A pathway under conditions of re-addition of amino acids to cells previously starved for amino acids (Diallinas 2017).

Accession Number:P19145
Protein Name:Gap1 aka YKR039W
Length:602
Molecular Weight:65656.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate all L-amino acids, some D-amino acids, beta-alanine, Polyamines, gamma-amino butyric acid

Cross database links:

Genevestigator: P19145
eggNOG: fuNOG05282
HEGENOM: HBG492579
DIP: DIP-8010N
RefSeq: NP_012965.1   
Entrez Gene ID: 853912   
Pfam: PF00324   
KEGG: sce:YKR039W   

Gene Ontology

GO:0030134 C:ER to Golgi transport vesicle
GO:0000328 C:fungal-type vacuole lumen
GO:0005887 C:integral to plasma membrane
GO:0005771 C:multivesicular body
GO:0042802 F:identical protein binding
GO:0015193 F:L-proline transmembrane transporter activity
GO:0015203 F:polyamine transmembrane transporter activity
GO:0006865 P:amino acid transport
GO:0019676 P:ammonia assimilation cycle
GO:0015846 P:polyamine transport
GO:0055085 P:transmembrane transport

References (8)

[1] “GAP1, the general amino acid permease gene of Saccharomyces cerevisiae. Nucleotide sequence, protein similarity with the other bakers yeast amino acid permeases, and nitrogen catabolite repression.”  Jauniaux J.-C.et.al.   2194797
[2] “Complete DNA sequence of yeast chromosome XI.”  Dujon B.et.al.   8196765
[3] “Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.”  Hu Y.et.al.   17322287
[4] “Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple permeases.”  During-Olsen L.et.al.   10467005
[5] “The fenpropimorph resistance gene FEN2 from Saccharomyces cerevisiae encodes a plasma membrane H+-pantothenate symporter.”  Stolz J.et.al.   10373490
[6] “A proteomics approach to understanding protein ubiquitination.”  Peng J.et.al.   12872131
[7] “A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.”  Hitchcock A.L.et.al.   14557538
[8] “A global topology map of the Saccharomyces cerevisiae membrane proteome.”  Kim H.et.al.   16847258

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSNTSSYEKN NPDNLKHNGI TIDSEFLTQE PITIPSNGSA VSIDETGSGS KWQDFKDSFK 
61:	RVKPIEVDPN LSEAEKVAII TAQTPLKHHL KNRHLQMIAI GGAIGTGLLV GSGTALRTGG 
121:	PASLLIGWGS TGTMIYAMVM ALGELAVIFP ISGGFTTYAT RFIDESFGYA NNFNYMLQWL 
181:	VVLPLEIVSA SITVNFWGTD PKYRDGFVAL FWLAIVIINM FGVKGYGEAE FVFSFIKVIT 
241:	VVGFIILGII LNCGGGPTGG YIGGKYWHDP GAFAGDTPGA KFKGVCSVFV TAAFSFAGSE 
301:	LVGLAASESV EPRKSVPKAA KQVFWRITLF YILSLLMIGL LVPYNDKSLI GASSVDAAAS 
361:	PFVIAIKTHG IKGLPSVVNV VILIAVLSVG NSAIYACSRT MVALAEQRFL PEIFSYVDRK 
421:	GRPLVGIAVT SAFGLIAFVA ASKKEGEVFN WLLALSGLSS LFTWGGICIC HIRFRKALAA 
481:	QGRGLDELSF KSPTGVWGSY WGLFMVIIMF IAQFYVAVFP VGDSPSAEGF FEAYLSFPLV 
541:	MVMYIGHKIY KRNWKLFIPA EKMDIDTGRR EVDLDLLKQE IAEEKAIMAT KPRWYRIWNF 
601:	WC