Q9MZS1

PR
Gene name
HCN1
Protein name
Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
Names
rbHCN1
Species
Oryctolagus cuniculus (Rabbit)
KEGG Pathway
ocu:100008732
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

549-822 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9MZS1

Entry ID Method Resolution Chain Position Source
AF-Q9MZS1-F1 Predicted AlphaFoldDB

No variants for Q9MZS1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9MZS1

No associated diseases with Q9MZS1

4 regional properties for Q9MZS1

Type Name Position InterPro Accession
domain Cyclic nucleotide-binding domain 411 - 527 IPR000595
domain Ion transport domain 79 - 338 IPR005821
domain Ion transport N-terminal 34 - 77 IPR013621
conserved_site Cyclic nucleotide-binding, conserved site 438 - 454 IPR018488

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
HCN channel complex A cation ion channel with a preference for K+ over Na+ ions, which is activated by membrane hyperpolarization, and consists of a tetramer of HCN family members. Some members of this family (HCN1, HCN2 and HCN4) are also activated when cAMP binds to their cyclic nucleotide binding domain (CNBD). Channel complexes of this family play an important role in the control of pacemaker activity in the heart.
integral component of plasma membrane The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

5 GO annotations of molecular function

Name Definition
cAMP binding Binding to cAMP, the nucleotide cyclic AMP (adenosine 3',5'-cyclophosphate).
intracellular cAMP-activated cation channel activity Enables the transmembrane transfer of a cation by a channel that opens when intracellular cAMP has been bound by the channel complex or one of its constituent parts.
sodium channel activity Enables the facilitated diffusion of a sodium ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism.
voltage-gated cation channel activity Enables the transmembrane transfer of a cation by a voltage-gated channel. A cation is a positively charged ion. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.
voltage-gated potassium channel activity Enables the transmembrane transfer of a potassium ion by a voltage-gated channel. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded.

4 GO annotations of biological process

Name Definition
cellular response to cAMP Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus.
potassium ion transmembrane transport A process in which a potassium ion is transported from one side of a membrane to the other.
protein homotetramerization The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
regulation of ion transmembrane transport Any process that modulates the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MATASSPPRR PRRARGLEDA EGPRRQYGFM QRQFTSMLQP GVNKFSLRMF GSQKAVEKEQ
70 80 90 100 110 120
ERVKTAGFWI IHPYSDFRFY WDLIMLIMMV GNLVIIPVGI TFFTEQTTTP WIIFNVASDT
130 140 150 160 170 180
VFLLDLIMNF RTGTVNEDSS EIILDPKVIK MNYLKSWFVV DFISSIPVDY IFLIVEKGMD
190 200 210 220 230 240
SEVYKTARAL RIVRFTKILS LLRLLRLSRL IRYIHQWEEI FHMTYDLASA VVRIFNLIGM
250 260 270 280 290 300
MLLLCHWDGC LQFLVPLLQD FPPDCWVSLN EMVNDSWGKQ YSYALFKAMS HMLCIGYGAQ
310 320 330 340 350 360
APVSMSDLWI TMLSMIVGAT CYAMFVGHAT ALIQSLDSSR RQYQEKYKQV EQYMSFHKLP
370 380 390 400 410 420
ADMRQKIHDY YEHRYQGKIF DEENILNELN DPLREEIVNF NCRKLVATMP LFANADPNFV
430 440 450 460 470 480
TAMLSKLRFE VFQPGDYIIR EGAVGKKMYF IQHGVAGVIT KSSKEMKLTD GSYFGEICLL
490 500 510 520 530 540
TKGRRTASVR ADTYCRLYSL SVDNFNEVLE EYPMMRRAFE TVAIDRLDRI GKKNSILLQK
550 560 570 580 590 600
FQKDLNTGVF NNQENEILKQ IVKHDREMVQ AIAPISYPQM TALNSTSSTA TPTSRMRTQS
610 620 630 640 650 660
PPVYTATSLS HSNLHSPSPS TQTPQPSAIL SPCSYTTAVC SPPVQSPLAT RTFHYASPTA
670 680 690 700 710 720
SQLSLMPQQQ QQPQAPQTQP QQPPQQPQTP GSATPKNEVH RSTQALPNTS LTREVRPLSA
730 740 750 760 770 780
SQPSLPHEVS TLISRPHPTV GESLASIPQP VAAVHSAGLQ AAGRSTVPQR VTLFRQMSSG
790 800 810 820
AIPPNRGVPP APPPPAAPLQ REASSVLNTD PEAEKPRFAS NL