##gff-version 3 P51681 UniProtKB Chain 1 352 . . . ID=PRO_0000069257;Note=C-C chemokine receptor type 5 P51681 UniProtKB Topological domain 1 30 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Transmembrane 31 58 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Topological domain 59 68 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Transmembrane 69 89 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Topological domain 90 102 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Transmembrane 103 124 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Topological domain 125 141 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Transmembrane 142 166 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Topological domain 167 198 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Transmembrane 199 218 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Topological domain 219 235 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Transmembrane 236 260 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Topological domain 261 277 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Transmembrane 278 301 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Topological domain 302 352 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Modified residue 3 3 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10089882;Dbxref=PMID:10089882 P51681 UniProtKB Modified residue 10 10 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21763489;Dbxref=PMID:21763489 P51681 UniProtKB Modified residue 14 14 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21763489;Dbxref=PMID:21763489 P51681 UniProtKB Modified residue 15 15 . . . Note=Sulfotyrosine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51681 UniProtKB Modified residue 336 336 . . . Note=Phosphoserine%3B by BARK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085131;Dbxref=PMID:10085131 P51681 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine%3B by BARK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085131;Dbxref=PMID:10085131 P51681 UniProtKB Modified residue 342 342 . . . Note=Phosphoserine%3B by BARK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085131;Dbxref=PMID:10085131 P51681 UniProtKB Modified residue 349 349 . . . Note=Phosphoserine%3B by BARK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10085131;Dbxref=PMID:10085131 P51681 UniProtKB Lipidation 321 321 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11323418;Dbxref=PMID:11323418 P51681 UniProtKB Lipidation 323 323 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11323418;Dbxref=PMID:11323418 P51681 UniProtKB Lipidation 324 324 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11323418;Dbxref=PMID:11323418 P51681 UniProtKB Glycosylation 6 6 . . . Note=O-linked (GalNAc...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11733580;Dbxref=PMID:11733580 P51681 UniProtKB Glycosylation 7 7 . . . Note=O-linked (GalNAc...) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11733580;Dbxref=PMID:11733580 P51681 UniProtKB Disulfide bond 20 269 . . . Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PDB:4MBS,ECO:0007744|PDB:5UIW P51681 UniProtKB Disulfide bond 101 178 . . . Ontology_term=ECO:0000255,ECO:0007744,ECO:0007744;evidence=ECO:0000255|PROSITE-ProRule:PRU00521,ECO:0007744|PDB:4MBS,ECO:0007744|PDB:5UIW P51681 UniProtKB Natural variant 10 10 . . . ID=VAR_003481;Note=In INCCR5-71A%3B results in absent sulfation and greatly decreased binding CCL4 and CCL5 when associated with D-3%2C D-10 and D-15%3B restored most CCL4 binding when associated with D-3 and D-15. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11733580;Dbxref=PMID:11733580 P51681 UniProtKB Natural variant 12 12 . . . ID=VAR_024066;Note=I->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9399903;Dbxref=PMID:9399903 P51681 UniProtKB Natural variant 20 20 . . . ID=VAR_024067;Note=C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs145061115,PMID:9399903 P51681 UniProtKB Natural variant 29 29 . . . ID=VAR_011839;Note=A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs1800939,PMID:9399903 P51681 UniProtKB Natural variant 31 31 . . . ID=VAR_003482;Note=In INCCR5-72A. R->H;Dbxref=dbSNP:rs56340326 P51681 UniProtKB Natural variant 34 34 . . . ID=VAR_003483;Note=In TZCCR5-179. P->L P51681 UniProtKB Natural variant 42 42 . . . ID=VAR_024068;Note=I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs1475319259,PMID:9399903 P51681 UniProtKB Natural variant 55 55 . . . ID=VAR_011840;Note=L->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9207783,ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs1799863,PMID:9207783,PMID:9399903 P51681 UniProtKB Natural variant 60 60 . . . ID=VAR_011841;Note=Risk factor for HIV-1%3B reduced cell surface expression%3B confers reduced susceptibility to infection by microbes that depend on these molecules as their receptors. R->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11369664,ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs1800940,PMID:11369664,PMID:9399903 P51681 UniProtKB Natural variant 62 62 . . . ID=VAR_003484;Note=In UGCCR5-145B. K->R P51681 UniProtKB Natural variant 68 68 . . . ID=VAR_003485;Note=In ZWCCR5-7. Y->H;Dbxref=dbSNP:rs758090461 P51681 UniProtKB Natural variant 73 73 . . . ID=VAR_024069;Note=A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs56198941,PMID:9399903 P51681 UniProtKB Natural variant 95 95 . . . ID=VAR_003486;Note=In MWCCR5-107. D->N;Dbxref=dbSNP:rs149975182 P51681 UniProtKB Natural variant 97 97 . . . ID=VAR_003487;Note=In INCCR5-467. G->E P51681 UniProtKB Natural variant 106 106 . . . ID=VAR_080410;Note=Protects against HIV-1 infection%3B CD4+ T-cells from R-106 carriers are less susceptible to infection by HIV-1 R5%3B results in reduced CCR5 surface expression. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17092330;Dbxref=dbSNP:rs183662584,PMID:17092330 P51681 UniProtKB Natural variant 122 122 . . . ID=VAR_003488;Note=In ZWCCR5-7. L->P P51681 UniProtKB Natural variant 158 158 . . . ID=VAR_003489;Note=In UGCCR5-145A. F->S P51681 UniProtKB Natural variant 176 176 . . . ID=VAR_003490;Note=In KECCR5-116. Y->C P51681 UniProtKB Natural variant 177 177 . . . ID=VAR_003491;Note=In INCCR5-45C. T->A P51681 UniProtKB Natural variant 178 178 . . . ID=VAR_012481;Note=Protects against HIV-1 infection%3B CD4+ T-cells from R-178 carriers are less susceptible to infection by HIV-1 R5%3B results in reduced CCR5 surface expression. C->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10917742,ECO:0000269|PubMed:17092330;Dbxref=dbSNP:rs199824195,PMID:10917742,PMID:17092330 P51681 UniProtKB Natural variant 185 185 . . . ID=VAR_003492;Note=In UGCCR5-145A. S->N P51681 UniProtKB Natural variant 210 210 . . . ID=VAR_003493;Note=In ZWCCR5-7. M->V P51681 UniProtKB Natural variant 214 214 . . . ID=VAR_003494;Note=In KECCR5-3B. Y->C P51681 UniProtKB Natural variant 215 215 . . . ID=VAR_024070;Note=S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9207783;Dbxref=dbSNP:rs1017863136,PMID:9207783 P51681 UniProtKB Natural variant 223 223 . . . ID=VAR_011842;Note=R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9207783,ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs1800452,PMID:9207783,PMID:9399903 P51681 UniProtKB Natural variant 228 228 . . . ID=VAR_024071;Note=Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9399903;Dbxref=PMID:9399903 P51681 UniProtKB Natural variant 239 239 . . . ID=VAR_003495;Note=In INCCR5-71A. T->S P51681 UniProtKB Natural variant 246 246 . . . ID=VAR_003496;Note=In UGCCR5-145A. L->P;Dbxref=dbSNP:rs143181119 P51681 UniProtKB Natural variant 288 288 . . . ID=VAR_003497;Note=In INCCR5-72A. T->M;Dbxref=dbSNP:rs534088482 P51681 UniProtKB Natural variant 301 301 . . . ID=VAR_011843;Note=G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs1800943,PMID:9399903 P51681 UniProtKB Natural variant 302 302 . . . ID=VAR_003498;Note=In TZCCR5-179. E->G P51681 UniProtKB Natural variant 303 303 . . . ID=VAR_003499;Note=In THCCR5-5. K->E P51681 UniProtKB Natural variant 306 306 . . . ID=VAR_003500;Note=In MWCCR5-1567. N->S P51681 UniProtKB Natural variant 322 322 . . . ID=VAR_003501;Note=In THCCR5-5. K->R P51681 UniProtKB Natural variant 333 333 . . . ID=VAR_003502;Note=In THCCR5-2. E->G P51681 UniProtKB Natural variant 335 335 . . . ID=VAR_003503;Note=In MWCCR5-1567%2C MWCCR5-1568%2C ZWCCR5-14 and ZWCCR5-112. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9207783,ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs1800944,PMID:9207783,PMID:9399903 P51681 UniProtKB Natural variant 339 339 . . . ID=VAR_003504;Note=In TZCCR5-181A and MWCCR5-107. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9207783,ECO:0000269|PubMed:9399903;Dbxref=dbSNP:rs1800945,PMID:9207783,PMID:9399903 P51681 UniProtKB Natural variant 345 345 . . . ID=VAR_003505;Note=In UGCCR5-145C. E->G P51681 UniProtKB Mutagenesis 3 3 . . . Note=No sulfation and strongly decreases binding with CCL4 and CCL5%3B when associated with D-10%3B D-14 and D-15. Restores most CCL4 binding%3B when associated with D-10 and D-15. Y->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10089882,ECO:0000269|PubMed:11733580;Dbxref=PMID:10089882,PMID:11733580 P51681 UniProtKB Mutagenesis 3 3 . . . Note=No sulfation and strongly decreases binding with CCL4 and CCL5%3B when associated with F-10%3B F-14 and F-15. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10089882,ECO:0000269|PubMed:11733580;Dbxref=PMID:10089882,PMID:11733580 P51681 UniProtKB Mutagenesis 6 7 . . . Note=Loss of molecular mass of 2 kDa compared to wild type when treated with O-glycosidase. Dramatically reduces binding with CCL4. Loss of molecular mass of about 2 kDa as compared to wild type%2C dramatically reduces binding by CCL4%3B when associated with A-16-17-A. SS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11733580;Dbxref=PMID:11733580 P51681 UniProtKB Mutagenesis 6 6 . . . Note=Strongly decreases CCL4 binding. No change in glycosylation status. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11733580;Dbxref=PMID:11733580 P51681 UniProtKB Mutagenesis 7 7 . . . Note=No change in glycosylation status and binds CCL4 as efficiently as wild type. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11733580;Dbxref=PMID:11733580 P51681 UniProtKB Mutagenesis 10 10 . . . Note=No sulfation and greatly decreases binding of CCL4 and CCL5%3B when associated with F-3%3B F-14 and F-15. Small loss of sulfation%3B when associated with F-14 and F-15. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10089882,ECO:0000269|PubMed:11733580;Dbxref=PMID:10089882,PMID:11733580 P51681 UniProtKB Mutagenesis 14 14 . . . Note=No sulfation and greatly decreased binding of CCL4 and CCL5%3B when associated with D-3%3B D-10 and D-14. No restoration of CCL4 binding%3B when associated with D-10 and D-15. Y->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10089882,ECO:0000269|PubMed:11733580;Dbxref=PMID:10089882,PMID:11733580 P51681 UniProtKB Mutagenesis 14 14 . . . Note=No sulfation and greatly decreases binding of CCL4 and CCL5%3B when associated with F-3%3B F-10%3B and F-15. Small loss of sulfation%3B when associated with F-10 and F-15. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10089882,ECO:0000269|PubMed:11733580;Dbxref=PMID:10089882,PMID:11733580 P51681 UniProtKB Mutagenesis 15 15 . . . Note=No sulfation and greatly decreased binding of CCL4 and CCL5%3B when associated with D-3%3B D-10 and D-14. Restored most CCL4 binding%3B when associated with D-3 and D-10. Y->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10089882,ECO:0000269|PubMed:11733580;Dbxref=PMID:10089882,PMID:11733580 P51681 UniProtKB Mutagenesis 15 15 . . . Note=No sulfation and greatly decreases binding of CCL4 and CCL5%3B when associated with F-3%3B F-10 and F-14. Small loss of sulfation%3B when associated with F-10 and F-14. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10089882,ECO:0000269|PubMed:11733580;Dbxref=PMID:10089882,PMID:11733580 P51681 UniProtKB Mutagenesis 16 17 . . . Note=Similar decrease in molecular mass when treated with O-glycosidase as for wild type. Loss of molecular mass of about 2 kDa as compared to wild type%2C dramatically reduces binding by CCL4%3B when associated with A-6-7-A. TS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11733580;Dbxref=PMID:11733580 P51681 UniProtKB Mutagenesis 20 20 . . . Note=Decreases to 40%25 surface expression. No effect on conformational integrity. Disrupts binding of CCL4. Decreases cell HIV infection. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10383387;Dbxref=PMID:10383387 P51681 UniProtKB Mutagenesis 101 101 . . . Note=Decreases to 40%25 surface expression. Disrupts conformational integrity. Disrupts binding of CCL4. Decreases HIV cell infection. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10383387;Dbxref=PMID:10383387 P51681 UniProtKB Mutagenesis 178 178 . . . Note=Decreases to 40%25 surface expression. Disrupts conformational integrity. Disrupts binding of CCL4. Decreases HIV cell infection. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10383387;Dbxref=PMID:10383387 P51681 UniProtKB Mutagenesis 269 269 . . . Note=Decreases to 40%25 surface expression. No effect on conformational integrity. Disrupts binding of CCL4. Decreases cell HIV infection. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10383387;Dbxref=PMID:10383387 P51681 UniProtKB Mutagenesis 321 321 . . . Note=Small reduction in palmitoylation. Cell surface expression reduced by 50%25. Greatly reduced palmitoylation. Cell surface expression greatly reduced%3B when associated with A-323 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%25%3B when associated with A-323 and A-324. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11323418;Dbxref=PMID:11323418 P51681 UniProtKB Mutagenesis 323 323 . . . Note=Small reduction in palmitoylation. Cell surface expression reduced by 50%25. Greatly reduced palmitoylation. Cell surface expression greatly reduced%3B when associated with A-321 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%25%3B when associated with A-321 and A-324. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11323418;Dbxref=PMID:11323418 P51681 UniProtKB Mutagenesis 324 324 . . . Note=Small reduction in palmitoylation. Cell surface expression reduced by 50%25. Greatly reduced palmitoylation. Cell surface expression greatly reduced%3B when associated with A-321 or A-323. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%25%3B when associated with A-321 and A-323. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11323418;Dbxref=PMID:11323418 P51681 UniProtKB Mutagenesis 336 336 . . . Note=APO-RANTES-stimulated phosphorylation reduced by 15%25%3B APO-RANTES-stimulated phosphorylation reduced by 30-50%25%3B when associated with A-337 or A-342 or A-349%3B APO-RANTES-stimulated phosphorylation reduced by 80%25%3B when associated with A-337 and A-342 or A-349%3B No APO-RANTES-stimulated phosphorylation%3B when associated with A-337%3B A-342 and A349%3B abolishes interaction with ARRB2%3B when associated with S-337%3B S-342 and S-349. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10085131,ECO:0000269|PubMed:11448957;Dbxref=PMID:10085131,PMID:11448957 P51681 UniProtKB Mutagenesis 337 337 . . . Note=APO-RANTES-stimulated phosphorylation reduced by 18%25%3B APO-RANTES-stimulated phosphorylation reduced by 30-50%25 on APO-RANTES stimulation%3B when associated with A-336 or A-342 or A-349%3B APO-RANTES-stimulated phosphorylation reduced by 80%25%3B when associated with A-336 and A-342 or A-349%3B No APO-RANTES-stimulated phosphorylation%3B when associated with A-336%3B A-342 and A349%3B abolishes interaction with ARRB2%3B when associated with S-336%3B S-342 and S-349. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10085131,ECO:0000269|PubMed:11448957;Dbxref=PMID:10085131,PMID:11448957 P51681 UniProtKB Mutagenesis 342 342 . . . Note=APO-RANTES-stimulated phosphorylation reduced by 42%25. Phosphorylation reduced by 50%25 on APO-RANTES stimulation%3B when associated with A-336 or A-337 or A-349%3B APO-RANTES-stimulated phosphorylation reduced by 80%25 when associated with A-336 and A-337 or A-349%3B No APO-RANTES-stimulated phosphorylation%3B when associated with A-336%3B A-337 and A349%3B abolishes interaction with ARRB2%3B when associated with S-336%3B S-337 and S-349. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10085131,ECO:0000269|PubMed:11448957;Dbxref=PMID:10085131,PMID:11448957 P51681 UniProtKB Mutagenesis 349 349 . . . Note=APO-RANTES-stimulated phosphorylation reduced by 43%25%3B APO-RANTES-stimulated phosphorylation reduced by 30-50%25%3B when associated with A-336 or A-337 or A-342%3B APO-RANTES-stimulated phosphorylation reduced by 80%25%3B when associated with A-336 and A-337 or A-342%3B No APO-RANTES-stimulated phosphorylation stimulation%3B when associated with A-336%3B A-337 and A347%3B abolishes interaction with ARRB2%3B when associated with S-336%3B S-337 and S-342. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10085131,ECO:0000269|PubMed:11448957;Dbxref=PMID:10085131,PMID:11448957 P51681 UniProtKB Helix 10 13 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2L87 P51681 UniProtKB Helix 14 17 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2L87 P51681 UniProtKB Turn 20 22 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2L87 P51681 UniProtKB Helix 23 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Turn 58 61 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7F1S P51681 UniProtKB Helix 64 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 97 131 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Turn 133 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 136 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 142 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Beta strand 167 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Beta strand 175 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 184 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 187 202 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 204 221 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 227 259 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Turn 260 265 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 269 288 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 289 291 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 292 299 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW P51681 UniProtKB Helix 302 313 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5UIW