DRSC/TRiP Functional Genomics Resources

powered by:
logo

back to: DIOPT - Ortholog Prediction Tool / DIOPT for Diseases and Traits


Protein Alignment HTR2B and Htr2b

DIOPT Version :10

Sequence 1:NP_000858.3 Gene:HTR2B / 3357 HGNCID:5294 Length:481 Species:Homo sapiens
Sequence 2:NP_058946.2 Gene:Htr2b / 29581 RGDID:61801 Length:479 Species:Rattus norvegicus


Alignment Length:481 Identity:393/481 - (81%)
Similarity:426/481 - (88%) Gaps:2/481 - (0%)


- Green bases have known domain annotations that are detailed below.


Human     1 MALSYRVSELQSTIPEHILQSTFVHVISSNWSGLQTESIPEEMKQIVEEQGNKLHWAALLILMVI 65
            ||.||::|| ||||.|||||.|..|:|.::.|||:.||..|||||..|.|||.:|||||||..||
  Rat     1 MASSYKMSE-QSTISEHILQKTCDHLILTDRSGLKAESAAEEMKQTAENQGNTVHWAALLIFAVI 64

Human    66 IPTIGGNTLVILAVSLEKKLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEAMWPLPLVLCPA 130
            |||||||.||||||||||:|||||||||||||||||||||||||||||||||||.|||||.||||
  Rat    65 IPTIGGNILVILAVSLEKRLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFEATWPLPLALCPA 129

Human   131 WLFLDVLFSTASIMHLCAISVDRYIAIKKPIQANQYNSRATAFIKITVVWLISIGIAIPVPIKGI 195
            ||||||||||||||||||||:||||||||||||||.|||.|||:|||||||||||||||||||||
  Rat   130 WLFLDVLFSTASIMHLCAISLDRYIAIKKPIQANQCNSRTTAFVKITVVWLISIGIAIPVPIKGI 194

Human   196 ETDVDNPNNITCVLTKERFGDFMLFGSLAAFFTPLAIMIVTYFLTIHALQKKAYLVKNKPPQRLT 260
            |.||.|.:||||.|||:|||.|||||||||||.||.|||||||||||||:||||||:|:||||||
  Rat   195 EADVVNAHNITCELTKDRFGSFMLFGSLAAFFAPLTIMIVTYFLTIHALRKKAYLVRNRPPQRLT 259

Human   261 WLTVSTVFQRDETPCSSPEKVAMLDGSRKDKALPNSGDETLMRRTSTIGKKSVQTISNEQRASKV 325
            ..|||||.||:::..|||||:||||||.|||.||||.|||||||.|:.|||..||||||||||||
  Rat   260 RWTVSTVLQREDSSFSSPEKMAMLDGSHKDKILPNSIDETLMRRMSSAGKKPAQTISNEQRASKV 324

Human   326 LGIVFFLFLLMWCPFFITNITLVLCDSCNQTTLQMLLEIFVWIGYVSSGVNPLVYTLFNKTFRDA 390
            |||||..||||||||||||:||.||||||||||:.||:||||:||||||||||:|||||||||:|
  Rat   325 LGIVFLFFLLMWCPFFITNVTLALCDSCNQTTLKTLLQIFVWVGYVSSGVNPLIYTLFNKTFREA 389

Human   391 FGRYITCNYRATKSVKTLRKRSSKIYFRNPMAENSKFFKKHGIRNGINPAMYQSPMRLRSSTIQS 455
            |||||||||:||||||.|||.||.:||.|.|.||||||.||||||||||||||||:|||||||||
  Rat   390 FGRYITCNYQATKSVKVLRKCSSTLYFGNSMVENSKFFTKHGIRNGINPAMYQSPVRLRSSTIQS 454

Human   456 SSIILLDTLLLTENEGDKTEEQVSYV 481
            ||||||:| .||||:|||.|:||||:
  Rat   455 SSIILLNT-FLTENDGDKVEDQVSYI 479

Known Domains:


Indicated by green bases in alignment.

GeneSequenceDomainRegion External IDIdentity
HTR2BNP_000858.3 7tmA_5-HT2B 55..398 CDD:341347 293/342 (86%)
TM helix 1 56..82 CDD:341347 22/25 (88%)
TM helix 2 89..115 CDD:341347 25/25 (100%)
TM helix 3 128..158 CDD:341347 28/29 (97%)
DRY motif, important for ligand-induced conformation changes. /evidence=ECO:0000305|PubMed:23519215, ECO:0000305|PubMed:28129538 152..154 1/1 (100%)
TM helix 4 170..193 CDD:341347 20/22 (91%)
[DE]RFG motif, may stabilize a conformation that preferentially activates signaling via beta-arrestin family members. /evidence=ECO:0000305|PubMed:23519215, ECO:0000305|PubMed:28129538 212..215 1/2 (50%)
TM helix 5 214..243 CDD:341347 25/28 (89%)
TM helix 6 317..347 CDD:341347 26/29 (90%)
TM helix 7 359..384 CDD:341347 19/24 (79%)
NPxxY motif, important for ligand-induced conformation changes and signaling. /evidence=ECO:0000305|PubMed:23519215, ECO:0000305|PubMed:28129538 376..380 3/3 (100%)
PDZ-binding. /evidence=ECO:0000269|PubMed:11150294 479..481 1/1 (100%)
Htr2bNP_058946.2 7tm_GPCRs 54..397 CDD:475119 293/342 (86%)
TM helix 1 56..80 CDD:410628 20/23 (87%)
TM helix 2 89..111 CDD:410628 21/21 (100%)
TM helix 3 128..150 CDD:410628 21/21 (100%)
DRY motif, important for ligand-induced conformation changes. /evidence=ECO:0000250|UniProtKB:P41595 151..153 1/1 (100%)
TM helix 4 173..189 CDD:410628 14/15 (93%)
[DE]RFG motif, may stabilize a conformation that preferentially activates signaling via beta-arrestin family members. /evidence=ECO:0000250|UniProtKB:P41595 211..214 1/2 (50%)
TM helix 5 214..237 CDD:410628 19/22 (86%)
TM helix 6 322..344 CDD:410628 19/21 (90%)
TM helix 7 358..383 CDD:410628 19/24 (79%)
NPxxY motif, important for ligand-induced conformation changes and signaling. /evidence=ECO:0000250|UniProtKB:P41595 375..379 3/3 (100%)
PDZ-binding. /evidence=ECO:0000250|UniProtKB:P41595 477..479 1/1 (100%)

Return to query results.
Submit another query.