| General information | | DisProt: | DP00628 | | Name: | Prostatic acid phosphatase [Isoform 1] | | Synonym(s): | PPAP_HUMAN
EC=3.1.3.2
hPAP
| | First appeared in release: | Release 5.2 (08/07/2010) | | UniProt: | P15309-1 | | UniGene: | Hs.433060 | | SwissProt: | PPAP_HUMAN | | TrEMBL: | | | NCBI (GI): | 130730 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 386 | | Percent disordered: | 10% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MRAAPLLLAR AASLSLGFLF LLFFWLDRSV LAKELKFVTL VFRHGDRSPI DTFPTDPIKE - 60
SSWPQGFGQL TQLGMEQHYE LGEYIRKRYR KFLNESYKHE QVYIRSTDVD RTLMSAMTNL - 120
AALFPPEGVS IWNPILLWQP IPVHTVPLSE DQLLYLPFRN CPRFQELESE TLKSEEFQKR - 180
LHPYKDFIAT LGKLSGLHGQ DLFGIWSKVY DPLYCESVHN FTLPSWATED TMTKLRELSE - 240
LSLLSLYGIH KQKEKSRLQG GVLVNEILNH MKRATQIPSY KKLIMYSAHD TTVSGLQMAL - 300
DVYNGLLPPY ASCHLTELYF EKGEYFVEMY YRNETQHEPY PLMLPGCSPS CPLERFAELV - 360
GPVIPQDWST ECMTTNSHQG TEDSTD
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| Functional narrative |
A peptide segment, PAP 248-286 appears to enhance HIV infection by forming amyloid fibers called SEVI, which enhance the attachment of the HIV. This segment is mostly disordered when bound to the surface of the micelle, as opposed to the helical structures typically bound to most amyloid proteins.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | SEVI | | Location: | 248 - 286 | | Length: | 39 | | Region sequence: |
GIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMY | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Phosphorylation
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7.3; 120mM NaCl)
| References:
- Jakob CG, Lewinski K, Kuciel R, Ostrowski W, Lebioda L. "Crystal structure of human prostatic acid phosphatase ." Prostate. 2000; 42(3): 211-8. PubMed: 10639192
- Nanga RP, Brender JR, Vivekanandan S, Popovych N, Ramamoorthy A. "NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286)." J Am Chem Soc. 2009; 131(49): 17972-9. PubMed: 19995078
| Comments:The 248-286 region is ordered in the native crystal structure, but disordered in solution and also when bound to membrane mimetics
(unusual for amyloid proteins). The degree of disorder in the final active amyloid product is currently unknown.
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| References |
- Nanga RP, Brender JR, Vivekanandan S, Popovych N, Ramamoorthy A. "NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286)." J Am Chem Soc. 2009; 131(49): 17972-9. PubMed: 19995078
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| Comments |
AV completed (7-29-2010) PubMed: 19995078
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