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8FY5

Human TMEM175-LAMP1 full-length complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005267molecular_functionpotassium channel activity
A0005515molecular_functionprotein binding
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005768cellular_componentendosome
A0010008cellular_componentendosome membrane
A0015252molecular_functionproton channel activity
A0016020cellular_componentmembrane
A0022841molecular_functionpotassium ion leak channel activity
A0035751biological_processregulation of lysosomal lumen pH
A0035752biological_processlysosomal lumen pH elevation
A0050544molecular_functionarachidonic acid binding
A0070050biological_processneuron cellular homeostasis
A0071805biological_processpotassium ion transmembrane transport
A0090385biological_processphagosome-lysosome fusion
A1902600biological_processproton transmembrane transport
B0005267molecular_functionpotassium channel activity
B0005515molecular_functionprotein binding
B0005764cellular_componentlysosome
B0005765cellular_componentlysosomal membrane
B0005768cellular_componentendosome
B0010008cellular_componentendosome membrane
B0015252molecular_functionproton channel activity
B0016020cellular_componentmembrane
B0022841molecular_functionpotassium ion leak channel activity
B0035751biological_processregulation of lysosomal lumen pH
B0035752biological_processlysosomal lumen pH elevation
B0050544molecular_functionarachidonic acid binding
B0070050biological_processneuron cellular homeostasis
B0071805biological_processpotassium ion transmembrane transport
B0090385biological_processphagosome-lysosome fusion
B1902600biological_processproton transmembrane transport
C0016020cellular_componentmembrane
D0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00310
Number of Residues15
DetailsLAMP_1 Lysosome-associated membrane glycoproteins duplicated domain signature. ACIMAnFsaaFsvnY
ChainResidueDetails
CALA40-TYR54
CTHR230-TYR244

site_idPS00311
Number of Residues41
DetailsLAMP_2 LAMP glycoproteins transmembrane and cytoplasmic domain signature. CllDensmLIPIaVGgaLaGLVlIVLIAYlVgrKRshAGYQ
ChainResidueDetails
CCYS375-GLN415

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues706
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
CALA29-MET382
DALA29-MET382
BMET1-SER33
BLEU470-CYS504

site_idSWS_FT_FI2
Number of Residues54
DetailsTRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00740, ECO:0000305|PubMed:37390818, ECO:0007744|PDB:8FY5, ECO:0007744|PDB:8FYF
ChainResidueDetails
CLEU383-SER410
DLEU383-SER410

site_idSWS_FT_FI3
Number of Residues12
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255|PROSITE-ProRule:PRU00740
ChainResidueDetails
APHE206-SER210
AASP283-ARG309
AGLN361-ARG375
ASER441-ARG442
BHIS57-ARG77
BLEU129-LEU138
BPHE206-SER210
BASP283-ARG309
BGLN361-ARG375
BSER441-ARG442
CHIS411-ILE417
DHIS411-ILE417

site_idSWS_FT_FI4
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8323299
ChainResidueDetails
CASN37
CASN45
CASN107
CASN241
CASN322
DASN37
DASN45
DASN107
DASN241
DASN322

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (polylactosaminoglycan) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218
ChainResidueDetails
CASN62
DASN62
AARG231-SER257
AHIS333-THR338
AALA397-HIS416
BVAL101-ASP106
BALA161-HIS184
BARG231-SER257
BHIS333-THR338
BALA397-HIS416

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2243102
ChainResidueDetails
CASN76
DASN76

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
CASN84
CASN293
DASN84
DASN293

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
CASN103
DASN103

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) (polylactosaminoglycan) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
CASN121
CASN130
DASN121
DASN130

site_idSWS_FT_FI10
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2243102, ECO:0000269|PubMed:8323299
ChainResidueDetails
CASN165
CASN181
CASN261
DASN165
DASN181
DASN261

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) serine; partial => ECO:0000269|PubMed:8323299
ChainResidueDetails
CSER197
DSER197

site_idSWS_FT_FI12
Number of Residues4
DetailsCARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:8323299
ChainResidueDetails
CTHR199
CTHR200
DTHR199
DTHR200

site_idSWS_FT_FI13
Number of Residues6
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:8323299
ChainResidueDetails
CSER207
CSER209
CSER211
DSER207
DSER209
DSER211

site_idSWS_FT_FI14
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) (polylactosaminoglycan) asparagine => ECO:0000269|PubMed:8323299
ChainResidueDetails
CASN223
CASN228
DASN223
DASN228

site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
CASN249
DASN249

site_idSWS_FT_FI16
Number of Residues2
DetailsSITE: Hydrophobic filter residue 1-1 => ECO:0000269|PubMed:28723891
ChainResidueDetails
AILE46
BILE46

site_idSWS_FT_FI17
Number of Residues2
DetailsSITE: Hydrophobic filter residue 2-1 => ECO:0000250|UniProtKB:K9UJK2
ChainResidueDetails
AVAL50
BVAL50

site_idSWS_FT_FI18
Number of Residues2
DetailsSITE: Hydrophobic filter residue 3-1 => ECO:0000250|UniProtKB:K9UJK2
ChainResidueDetails
ALEU53
BLEU53

site_idSWS_FT_FI19
Number of Residues2
DetailsSITE: Hydrophobic filter residue 1-2 => ECO:0000269|PubMed:28723891
ChainResidueDetails
AILE271
BILE271

site_idSWS_FT_FI20
Number of Residues2
DetailsSITE: Hydrophobic filter residue 2-2 => ECO:0000250|UniProtKB:K9UJK2
ChainResidueDetails
ALEU275
BLEU275

site_idSWS_FT_FI21
Number of Residues2
DetailsSITE: Hydrophobic filter residue 3-2 => ECO:0000250|UniProtKB:K9UJK2
ChainResidueDetails
ALEU278
BLEU278

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ATHR6
BTHR6

221051

PDB entries from 2024-06-12

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