Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8CRT

Local refinement of Rh trimer, glycophorin B and Band3-III transmembrane region, class 1a of erythrocyte ankyrin-1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0016020	cellular_component	membrane
C	0005452	molecular_function	solute:inorganic anion antiporter activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005886	cellular_component	plasma membrane
C	0006811	biological_process	monoatomic ion transport
C	0006820	biological_process	monoatomic anion transport
C	0006821	biological_process	chloride transport
C	0006873	biological_process	intracellular monoatomic ion homeostasis
C	0008092	molecular_function	cytoskeletal protein binding
C	0008509	molecular_function	monoatomic anion transmembrane transporter activity
C	0009898	cellular_component	cytoplasmic side of plasma membrane
C	0015106	molecular_function	bicarbonate transmembrane transporter activity
C	0015108	molecular_function	chloride transmembrane transporter activity
C	0015297	molecular_function	antiporter activity
C	0015701	biological_process	bicarbonate transport
C	0016020	cellular_component	membrane
C	0016323	cellular_component	basolateral plasma membrane
C	0030018	cellular_component	Z disc
C	0030492	molecular_function	hemoglobin binding
C	0030506	molecular_function	ankyrin binding
C	0030863	cellular_component	cortical cytoskeleton
C	0042803	molecular_function	protein homodimerization activity
C	0043495	molecular_function	protein-membrane adaptor activity
C	0051453	biological_process	regulation of intracellular pH
C	0055085	biological_process	transmembrane transport
C	0070062	cellular_component	extracellular exosome
C	0072562	cellular_component	blood microparticle
C	0140900	molecular_function	chloride:bicarbonate antiporter activity
C	0170014	cellular_component	ankyrin-1 complex
C	1902476	biological_process	chloride transmembrane transport
D	0016020	cellular_component	membrane
E	0005452	molecular_function	solute:inorganic anion antiporter activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005886	cellular_component	plasma membrane
E	0006811	biological_process	monoatomic ion transport
E	0006820	biological_process	monoatomic anion transport
E	0006821	biological_process	chloride transport
E	0006873	biological_process	intracellular monoatomic ion homeostasis
E	0008092	molecular_function	cytoskeletal protein binding
E	0008509	molecular_function	monoatomic anion transmembrane transporter activity
E	0009898	cellular_component	cytoplasmic side of plasma membrane
E	0015106	molecular_function	bicarbonate transmembrane transporter activity
E	0015108	molecular_function	chloride transmembrane transporter activity
E	0015297	molecular_function	antiporter activity
E	0015701	biological_process	bicarbonate transport
E	0016020	cellular_component	membrane
E	0016323	cellular_component	basolateral plasma membrane
E	0030018	cellular_component	Z disc
E	0030492	molecular_function	hemoglobin binding
E	0030506	molecular_function	ankyrin binding
E	0030863	cellular_component	cortical cytoskeleton
E	0042803	molecular_function	protein homodimerization activity
E	0043495	molecular_function	protein-membrane adaptor activity
E	0051453	biological_process	regulation of intracellular pH
E	0055085	biological_process	transmembrane transport
E	0070062	cellular_component	extracellular exosome
E	0072562	cellular_component	blood microparticle
E	0140900	molecular_function	chloride:bicarbonate antiporter activity
E	0170014	cellular_component	ankyrin-1 complex
E	1902476	biological_process	chloride transmembrane transport
K	0005886	cellular_component	plasma membrane
K	0008519	molecular_function	ammonium channel activity
K	0016020	cellular_component	membrane
K	0072488	biological_process	ammonium transmembrane transport
K	0097272	biological_process	ammonium homeostasis
K	0170014	cellular_component	ankyrin-1 complex
L	0005515	molecular_function	protein binding
L	0005886	cellular_component	plasma membrane
L	0006873	biological_process	intracellular monoatomic ion homeostasis
L	0008519	molecular_function	ammonium channel activity
L	0015200	molecular_function	methylammonium transmembrane transporter activity
L	0015670	biological_process	carbon dioxide transport
L	0015701	biological_process	bicarbonate transport
L	0016020	cellular_component	membrane
L	0022840	molecular_function	leak channel activity
L	0030506	molecular_function	ankyrin binding
L	0035378	biological_process	carbon dioxide transmembrane transport
L	0035379	molecular_function	carbon dioxide transmembrane transporter activity
L	0055085	biological_process	transmembrane transport
L	0072488	biological_process	ammonium transmembrane transport
L	0072489	biological_process	methylammonium transmembrane transport
L	0097272	biological_process	ammonium homeostasis
L	0170014	cellular_component	ankyrin-1 complex
P	0016020	cellular_component	membrane
Q	0005515	molecular_function	protein binding
Q	0005886	cellular_component	plasma membrane
Q	0006873	biological_process	intracellular monoatomic ion homeostasis
Q	0008519	molecular_function	ammonium channel activity
Q	0015200	molecular_function	methylammonium transmembrane transporter activity
Q	0015670	biological_process	carbon dioxide transport
Q	0015701	biological_process	bicarbonate transport
Q	0016020	cellular_component	membrane
Q	0022840	molecular_function	leak channel activity
Q	0030506	molecular_function	ankyrin binding
Q	0035378	biological_process	carbon dioxide transmembrane transport
Q	0035379	molecular_function	carbon dioxide transmembrane transporter activity
Q	0055085	biological_process	transmembrane transport
Q	0072488	biological_process	ammonium transmembrane transport
Q	0072489	biological_process	methylammonium transmembrane transport
Q	0097272	biological_process	ammonium homeostasis
Q	0170014	cellular_component	ankyrin-1 complex

Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. KYGFSSVGINLLVAAL

Chain	Residue	Details
L	LYS74-LEU89

site_id	PS00219
Number of Residues	12
Details	ANION_EXCHANGER_1 Anion exchangers family signature 1. FGGLVRDIRRRY

Chain	Residue	Details
C	PHE379-TYR390

site_id	PS00220
Number of Residues	15
Details	ANION_EXCHANGER_2 Anion exchangers family signature 2. FLISLIFIYETFsKL

Chain	Residue	Details
C	PHE526-LEU540

site_id	PS00312
Number of Residues	10
Details	GLYCOPHORIN_A Glycophorin A signature. IIlCVMAGII

Chain	Residue	Details
P	ILE66-ILE75
B	ILE95-ILE104

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	669
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	165
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	70
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	44
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	46
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	164
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	150
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	32
Details	Transmembrane: {"description":"Discontinuously helical; Name=3","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	44
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	36
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	34
Details	Transmembrane: {"description":"Discontinuously helical; Name=10","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	36
Details	Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	60
Details	Intramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"26542571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	142
Details	Region: {"description":"Involved in anion transport"}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Site: {"description":"Important for anion transport"}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Site: {"description":"Important for anion-proton cotransport"}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"1885574","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"10861210","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24121512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35835865","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)