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Q75T13 (PGAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GPI inositol-deacylase

EC=3.1.-.-
Alternative name(s):
Post-GPI attachment to proteins factor 1
Short name=hPGAP1
Gene names
Name:PGAP1
ORF Names:UNQ3024/PRO9822
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length922 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the GPI inositol-deacylase family.

Sequence caution

The sequence AAQ88987.1 differs from that shown. Reason: Erroneous initiation.

The sequence BC040517 differs from that shown. Reason: Frameshift at position 333.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processC-terminal protein lipidation

Traceable author statement. Source: Reactome

anterior/posterior axis specification

Inferred from electronic annotation. Source: Ensembl

attachment of GPI anchor to protein

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

embryonic pattern specification

Inferred from electronic annotation. Source: Ensembl

forebrain regionalization

Inferred from electronic annotation. Source: Ensembl

head development

Inferred from electronic annotation. Source: Ensembl

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

myo-inositol transport

Inferred from sequence or structural similarity. Source: UniProtKB

post-translational protein modification

Traceable author statement. Source: Reactome

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionnuclease activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphoric ester hydrolase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q75T13-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q75T13-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q75T13-3)

The sequence of this isoform differs from the canonical sequence as follows:
     592-592: R → A
     593-922: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q75T13-4)

The sequence of this isoform differs from the canonical sequence as follows:
     50-269: Missing.
     652-922: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 922922GPI inositol-deacylase
PRO_0000277623

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Helical; Potential
Topological domain33 – 641609Lumenal Potential
Transmembrane642 – 66221Helical; Potential
Topological domain663 – 6686Cytoplasmic Potential
Transmembrane669 – 68921Helical; Potential
Topological domain690 – 73344Lumenal Potential
Transmembrane734 – 75421Helical; Potential
Topological domain755 – 81763Cytoplasmic Potential
Transmembrane818 – 83821Helical; Potential
Topological domain839 – 85315Lumenal Potential
Transmembrane854 – 87421Helical; Potential
Topological domain875 – 89319Cytoplasmic Potential
Transmembrane894 – 91421Helical; Potential
Topological domain915 – 9228Lumenal Potential

Sites

Active site1741 By similarity

Amino acid modifications

Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation5581N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 174174Missing in isoform 2.
VSP_023040
Alternative sequence50 – 269220Missing in isoform 4.
VSP_023041
Alternative sequence5921R → A in isoform 3.
VSP_023042
Alternative sequence593 – 922330Missing in isoform 3.
VSP_023043
Alternative sequence652 – 922271Missing in isoform 4.
VSP_023044

Experimental info

Sequence conflict3041D → G in BAB14035. Ref.2
Sequence conflict3891T → A in CAH10543. Ref.3
Sequence conflict7011S → P in CAH10543. Ref.3
Sequence conflict8091A → T in CAH10543. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 0305D18F5BF292D6

FASTA922105,383
        10         20         30         40         50         60 
MFLHSVNLWN LAFYVFMVFL ATLGLWDVFF GFEENKCSMS YMFEYPEYQK IELPKKLAKR 

        70         80         90        100        110        120 
YPAYELYLYG EGSYAEEHKI LPLTGIPVLF LPGNAGSYKQ VRSIGSIALR KAEDIDFKYH 

       130        140        150        160        170        180 
FDFFSVNFNE ELVALYGGSL QKQTKFVHEC IKTILKLYKG QEFAPKSVAI IGHSMGGLVA 

       190        200        210        220        230        240 
RALLTLKNFK HDLINLLITQ ATPHVAPVMP LDRFITDFYT TVNNYWILNA RHINLTTLSV 

       250        260        270        280        290        300 
AGGFRDYQVR SGLTFLPKLS HHTSALSVVS SAVPKTWVST DHLSIVWCKQ LQLTTVRAFF 

       310        320        330        340        350        360 
DLIDADTKQI TQNSKKKLSV LYHHFIRHPS KHFEENPAII SDLTGTSMWV LVKVSKWTYV 

       370        380        390        400        410        420 
AYNESEKIYF TFPLENHRKI YTHVYCQSTM LDTNSWIFAC INSTSMCLQG VDLSWKAELL 

       430        440        450        460        470        480 
PTIKYLTLRL QDYPSLSHLV VYVPSVRGSK FVVDCEFFKK EKRYIQLPVT HLFSFGLSSR 

       490        500        510        520        530        540 
KVVLNTNGLY YNLELLNFGQ IYQAFKINVV SKCSAVKEEI TSIYRLHIPW SYEDSLTIAQ 

       550        560        570        580        590        600 
APSSTEISLK LHIAQPENNT HVALFKMYTS SDCRYEVTVK TSFSQILGQV VRFHGGALPA 

       610        620        630        640        650        660 
YVVSNILLAY RGQLYSLFST GCCLEYATML DKEAKPYKVD PFVIIIKFLL GYKWFKELWD 

       670        680        690        700        710        720 
VLLLPELDAV ILTCQSMCFP LISLILFLFG TCTAYWSGLL SSASVRLLSS LWLALKRPSE 

       730        740        750        760        770        780 
LPKDIKMISP DLPFLTIVLI IVSWTTCGAL AILLSYLYYV FKVVHLQASL TTFKNSQPVN 

       790        800        810        820        830        840 
PKHSRRSEKK SNHHKDSSIH HLRLSANDAE DSLRMHSTVI NLLTWIVLLS MPSLIYWLKN 

       850        860        870        880        890        900 
LRYYFKLNPD PCKPLAFILI PTMAILGNTY TVSIKSSKLL KTTSQFPLPL AVGVIAFGSA 

       910        920 
HLYRLPCFVF IPLLLHALCN FM 

« Hide

Isoform 2 [UniParc].

Checksum: 5C67D37891F3FAAC
Show »

FASTA74885,239
Isoform 3 [UniParc].

Checksum: BD6B7BB40B8A0BC1
Show »

FASTA59267,974
Isoform 4 [UniParc].

Checksum: 86F82D676245A7E3
Show »

FASTA43149,845

References

« Hide 'large scale' references
[1]"Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is mediated by mammalian PGAP1 and yeast Bst1p."
Tanaka S., Maeda Y., Tashima Y., Kinoshita T.
J. Biol. Chem. 279:14256-14263(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Mammary gland.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal kidney.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Testis.
[6]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-922 (ISOFORMS 1/2).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB128038 mRNA. Translation: BAD13427.1.
AK022439 mRNA. Translation: BAB14035.1.
BX648642 mRNA. Translation: CAH10543.1.
AC017035 Genomic DNA. Translation: AAY15059.1.
AC012486 Genomic DNA. Translation: AAX88854.1.
BC040517 mRNA. No translation available.
AY358624 mRNA. Translation: AAQ88987.1. Different initiation.
RefSeqNP_079265.2. NM_024989.3.
XP_005246923.1. XM_005246866.1.
UniGeneHs.229988.

3D structure databases

ProteinModelPortalQ75T13.
SMRQ75T13. Positions 126-210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123093. 5 interactions.
IntActQ75T13. 2 interactions.
MINTMINT-4828389.
STRING9606.ENSP00000346809.

PTM databases

PhosphoSiteQ75T13.

Polymorphism databases

DMDM74758940.

Proteomic databases

PaxDbQ75T13.
PRIDEQ75T13.

Protocols and materials databases

DNASU80055.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354764; ENSP00000346809; ENSG00000197121. [Q75T13-1]
ENST00000409475; ENSP00000387028; ENSG00000197121. [Q75T13-3]
GeneID80055.
KEGGhsa:80055.
UCSCuc002utw.3. human. [Q75T13-1]
uc002uty.1. human. [Q75T13-3]

Organism-specific databases

CTD80055.
GeneCardsGC02M197697.
HGNCHGNC:25712. PGAP1.
MIM611655. gene.
neXtProtNX_Q75T13.
PharmGKBPA162399235.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG312611.
HOVERGENHBG082122.
InParanoidQ75T13.
KOK05294.
OMATKFVHEC.
OrthoDBEOG7KM5RZ.
PhylomeDBQ75T13.
TreeFamTF314565.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ75T13.
BgeeQ75T13.
CleanExHS_PGAP1.
GenevestigatorQ75T13.

Family and domain databases

InterProIPR012908. PGAP1-like.
[Graphical view]
PfamPF07819. PGAP1. 1 hit.
[Graphical view]
PROSITEPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi80055.
NextBio70254.
PROQ75T13.
SOURCESearch...

Entry information

Entry namePGAP1_HUMAN
AccessionPrimary (citable) accession number: Q75T13
Secondary accession number(s): Q4G0R8 expand/collapse secondary AC list , Q4ZG47, Q53SM0, Q6AW92, Q6UWV4, Q9HA24
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM