SitesBLAST
Comparing GFF2718 FitnessBrowser__psRCH2:GFF2718 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P0AER0 Glycerol uptake facilitator protein; Aquaglyceroporin; Glycerol facilitator from Escherichia coli (strain K12) (see 3 papers)
71% identity, 93% coverage: 8:279/293 of query aligns to 6:271/281 of P0AER0
- HLN 66:68 (= HLN 68:70) binding
- Y138 (= Y140) binding
- GFA 199:201 (= GFA 201:203) binding
- N203 (= N205) binding
- R206 (= R208) binding
- PL 236:237 (≠ PI 238:239) mutation to FW: No detectable water or glycerol permeability.
1fx8A Crystal structure of the e. Coli glycerol facilitator (glpf) with substrate glycerol (see paper)
74% identity, 87% coverage: 8:261/293 of query aligns to 1:254/254 of 1fx8A
B1VB61 Propanediol uptake facilitator PduF from Citrobacter freundii (see paper)
68% identity, 93% coverage: 8:279/293 of query aligns to 4:269/269 of B1VB61
P37451 Propanediol uptake facilitator PduF from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
69% identity, 87% coverage: 8:262/293 of query aligns to 4:258/264 of P37451
Q96PS8 Aquaporin-10; AQP-10; Aquaglyceroporin-10; Small intestine aquaporin from Homo sapiens (Human) (see 2 papers)
38% identity, 92% coverage: 9:279/293 of query aligns to 20:286/301 of Q96PS8
- E27 (= E16) mutation to Q: Abolishes permeability to glycerol.
- G73 (≠ A61) mutation to A: Increased permeability to glycerol at acidic pH.; mutation to F: Abolishes permeability to glycerol.
- S77 (= S65) mutation S->A,D: Nearly abolishes permeability to glycerol.
- H80 (= H68) mutation to A: Abolishes permeability to glycerol.
- F85 (≠ V73) mutation to A: Nearly abolishes permeability to glycerol.
- R94 (≠ T82) mutation to A: Abolishes permeability to glycerol.
- N133 (≠ Q121) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Abolishes N-glycosylation.
6f7hC Crystal structure of human aqp10 (see paper)
38% identity, 86% coverage: 9:260/293 of query aligns to 5:252/253 of 6f7hC
O14520 Aquaporin-7; AQP-7; Aquaglyceroporin-7; Aquaporin adipose; AQPap; Aquaporin-7-like from Homo sapiens (Human) (see 4 papers)
36% identity, 95% coverage: 12:290/293 of query aligns to 36:312/342 of O14520
- V59 (≠ K35) to L: in dbSNP:rs4008659
- Y135 (≠ S111) Important for permeability to glycerol; mutation to A: Strongly decreased permeability to glycerol. Mildly decreased water permeability.
- H165 (≠ S144) mutation to A: Decreased permeability to glycerol. Mildly decreased water permeability.
- G264 (= G245) to V: affects water and glycerol transport; dbSNP:rs62542743
Sites not aligning to the query:
- 1:32 mutation Missing: Decreased interaction with PLIN1.
- 12 R → C: in dbSNP:rs139297434
8c9hA Aqp7_inhibitor
38% identity, 84% coverage: 12:257/293 of query aligns to 11:251/253 of 8c9hA
6n1gA Crystal structure of aquaglyceroporin aqp7 (see paper)
38% identity, 84% coverage: 12:257/293 of query aligns to 5:245/249 of 6n1gA
I1CR68 Aquaporin-1 from Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar) (see paper)
41% identity, 81% coverage: 12:249/293 of query aligns to 60:292/306 of I1CR68
- H275 (≠ P233) mutation to A: Affects pH sensing; when associated with A-85.
3c02A X-ray structure of the aquaglyceroporin from plasmodium falciparum (see paper)
34% identity, 84% coverage: 12:258/293 of query aligns to 5:236/242 of 3c02A
2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
33% identity, 85% coverage: 8:256/293 of query aligns to 3:243/245 of 2evuA
P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
30% identity, 94% coverage: 6:281/293 of query aligns to 34:262/271 of P08995
- S262 (≠ E281) modified: Phosphoserine; by CPK
P09011 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 93% coverage: 15:287/293 of query aligns to 13:253/261 of P09011
- S233 (≠ A267) modified: Phosphoserine
- N244 (≠ A278) mutation to D: No effects.
3nkaA Crystal structure of aqpz h174g,t183f (see paper)
34% identity, 72% coverage: 12:221/293 of query aligns to 6:202/230 of 3nkaA
Q9SAI4 Aquaporin NIP6-1; NOD26-like intrinsic protein 6-1; AtNIP6;1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 90% coverage: 15:279/293 of query aligns to 84:302/305 of Q9SAI4
- A119 (≠ W50) mutation to W: 6-fold increase in water transport activity, but impaired in urea transport.
- V252 (≠ A207) mutation to A: No effect.
P41181 Aquaporin-2; AQP-2; ADH water channel; Aquaporin-CD; AQP-CD; Collecting duct water channel protein; WCH-CD; Water channel protein for renal collecting duct from Homo sapiens (Human) (see 12 papers)
33% identity, 82% coverage: 15:254/293 of query aligns to 15:220/271 of P41181
- G64 (= G66) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
- G78 (≠ F80) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
- C79 (≠ G81) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
- S148 (≠ I168) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to D: Retained in the endoplasmic reticulum.
- R187 (= R208) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
- A190 (≠ G211) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
- V194 (≠ M215) to I: in dbSNP:rs772051028
- S216 (≠ A250) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
- L217 (≠ A251) mutation to A: Abolishes interaction with MIAC; when associated with A-221.
Sites not aligning to the query:
- 221 Y→A: Abolishes interaction with MIAC; when associated with A-217.
- 229 S→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; S→D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- 231 S→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; S→D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- 232 E→A: Reduces interaction with MIAC.
- 244 T→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; T→E: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- 254 R → L: in NDI2; results in the loss of arginine vasopressin-mediated phosphorylation at S-256; R → Q: in NDI2; exerts a dominant-negative effect on wild-type-AQP2 in that it interferes with its trafficking to the apical membrane; is a loss of function instead of a gain of function mutation on dominant nephrogenic diabetes insipidus
- 256 modified: Phosphoserine; by PKA; S→A: Retained in vesicles.; S→D: Expressed in the apical membrane.
- 258 E → K: in NDI2; retained in the Golgi compartment; dbSNP:rs104894332
- 262 P → L: in NDI2; mutant protein folds properly and is functional but is retained in intracellular vesicles; able to assemble into tetramers with wild-type AQP2 that properly localize to the apical membrane; dbSNP:rs104894339; P→A: No effect on expression at the apical cell membrane.
4nefA X-ray structure of human aquaporin 2 (see paper)
33% identity, 82% coverage: 15:254/293 of query aligns to 14:219/239 of 4nefA
P06624 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Bos taurus (Bovine) (see 4 papers)
28% identity, 94% coverage: 15:290/293 of query aligns to 15:252/263 of P06624
- Y149 (≠ T169) mutation to G: Increases constitutive water permeability. Abolishes regulation by cytoplasmic calcium levels.; mutation to L: Strongly decreases water permeability. Abolishes regulation by cytoplasmic calcium levels.; mutation to S: Slightly decreases water permeability, but has a minor effect on the regulation by cytoplasmic calcium levels.
- L227 (= L261) mutation to A: Strongly reduced CALM binding.
- 227:237 (vs. 261:269, 18% identical) Interaction with CALM
- V230 (= V264) mutation to A: Strongly reduced CALM binding.
- S235 (≠ A267) modified: Phosphoserine
- S243 (≠ K275) modified: Phosphoserine; by PKA
- S245 (≠ K277) modified: Phosphoserine
- N246 (≠ S284) Interaction with BFSP1; modified: Deamidated asparagine
- E250 (≠ D288) interaction with BFSP1
P56402 Aquaporin-2; AQP-2; ADH water channel; Aquaporin-CD; AQP-CD; Collecting duct water channel protein; WCH-CD; Water channel protein for renal collecting duct from Mus musculus (Mouse) (see 2 papers)
31% identity, 83% coverage: 14:257/293 of query aligns to 14:223/271 of P56402
- T126 (≠ S146) mutation to M: Does not cause loss of water channel activity, but impairs trafficking from cytoplasmic vesicles to the cell membrane.
Sites not aligning to the query:
- 256 modified: Phosphoserine; S → L: in cph; loss of a phosphorylation site and loss of trafficking to the apical cell membrane; causes aberrant location at the basolateral cell membrane
Query Sequence
>GFF2718 FitnessBrowser__psRCH2:GFF2718
MSTPIVPTLKGQCIAEFLGTALLIFFGTGCVAALKLGGAELGLWEISIIWGIGVSMAVYL
AAGVSGAHLNPAVTIALWLFGTFERHRVPAYILAQVAGAFCSAALVYGLYSSLFFDFEQA
QQMVRGSVESLELASIFSTYPHASLSFGQAFLVEMVITAILLAMIMAITDDGNGLPSGPL
APLLIGLLIAVIGGAMGPLTGFAMNPARDFGPKLMTFFAGWGDVAFTGGKDIPYFLVPIF
APILGACLGAAGYKALICRHLPGVGSAACDAPKPKEKASAEVGSAQPDISKVR
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory