2ZZ9

Structure of aquaporin-4 S180D mutant at 2.8 A resolution by electron crystallography

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005768	cellular_component	endosome
A	0005886	cellular_component	plasma membrane
A	0005911	cellular_component	cell-cell junction
A	0006833	biological_process	water transport
A	0007565	biological_process	female pregnancy
A	0007605	biological_process	sensory perception of sound
A	0009897	cellular_component	external side of plasma membrane
A	0009925	cellular_component	basal plasma membrane
A	0009992	biological_process	intracellular water homeostasis
A	0010008	cellular_component	endosome membrane
A	0010574	biological_process	regulation of vascular endothelial growth factor production
A	0015250	molecular_function	water channel activity
A	0015267	molecular_function	channel activity
A	0015670	biological_process	carbon dioxide transport
A	0016020	cellular_component	membrane
A	0016323	cellular_component	basolateral plasma membrane
A	0030315	cellular_component	T-tubule
A	0031253	cellular_component	cell projection membrane
A	0032691	biological_process	negative regulation of interleukin-1 beta production
A	0032715	biological_process	negative regulation of interleukin-6 production
A	0032991	cellular_component	protein-containing complex
A	0033326	biological_process	cerebrospinal fluid secretion
A	0042383	cellular_component	sarcolemma
A	0042802	molecular_function	identical protein binding
A	0042995	cellular_component	cell projection
A	0045471	biological_process	response to ethanol
A	0050891	biological_process	multicellular organismal-level water homeostasis
A	0051289	biological_process	protein homotetramerization
A	0051384	biological_process	response to glucocorticoid
A	0051649	biological_process	establishment of localization in cell
A	0055085	biological_process	transmembrane transport
A	0060354	biological_process	negative regulation of cell adhesion molecule production
A	0070295	biological_process	renal water absorption
A	0071333	biological_process	cellular response to glucose stimulus
A	0071346	biological_process	cellular response to type II interferon
A	0071347	biological_process	cellular response to interleukin-1
A	0071354	biological_process	cellular response to interleukin-6
A	0071392	biological_process	cellular response to estradiol stimulus
A	0090660	biological_process	cerebrospinal fluid circulation
A	0097450	cellular_component	astrocyte end-foot
A	0098609	biological_process	cell-cell adhesion

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEE A 401

Chain	Residue
A	TYR134
A	LEU135
A	PEE403

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEE A 402

Chain	Residue
A	ASN229
A	HIS230
A	VAL235
A	PEE405

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEE A 403

Chain	Residue
A	TYR134
A	ILE223
A	PEE401
A	PEE404
A	LEU124
A	ILE132

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEE A 404

Chain	Residue
A	GLN32
A	LYS36
A	LEU43
A	PEE403

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEE A 405

Chain	Residue
A	VAL105
A	CYS106
A	ARG108
A	ILE112
A	PEE402

---

Functional Information from PROSITE/UniProt

site_id	PS00221
Number of Residues	9
Details	MIP MIP family signature. HINPAVTVA

Chain	Residue	Details
A	HIS95-ALA103

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	119
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"16325200","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19406128","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	23
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"16325200","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19406128","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	Intramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"16325200","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19406128","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	28
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"16325200","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19406128","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Motif: {"description":"NPA 1","evidences":[{"source":"PubMed","id":"16325200","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19406128","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Motif: {"description":"NPA 2","evidences":[{"source":"PubMed","id":"16325200","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19406128","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"UniProtKB","id":"P55088","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"19800950","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---