GUC2F_HUMAN » Retinal guanylyl cyclase 2

GUC2F_HUMAN » Retinal guanylyl cyclase 2
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
GUC2F_HUMAN » Retinal guanylyl cyclase 2 » RETGC-2; Guanylate cyclase 2F, retinal;Guanylate cyclase F; GC-F; Rod outer segment membrane guanylate cyclase 2;ROS-GC2;
Hydrophobic Thickness 35.2 ± 1.8 Å
Tilt Angle 23 ± 4°
ΔGtransfer -23.0 kcal/mol
ΔGfold -19.4 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 466-490 (466-493)
Pathways

Phototransduction (KEGG)

Purine metabolism (KEGG)

PDB none
OPM none
Complexes none
Interactions none
Domains

AA: 71-415, PDBID: 3OLZ, Subunit A, Seq Identity:20%, Receptor family ligand binding region

AA: 583-809, PDBID: 4L68, Subunit B, Seq Identity:43%, Protein tyrosine kinase

AA: 813-869, PDBID: 3HLS, Subunit E, Seq Identity:10%, Heme NO binding associated

AA: 875-1062, PDBID: 3UVJ, Subunit A, Seq Identity:44%, Adenylate and Guanylate cyclase catalytic domain

UniProt annotation for GUC2F_HUMAN » Retinal guanylyl cyclase 2
FUNCTION: Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction.

CATALYTIC ACTIVITY: GTP = 3",5"-cyclic GMP + diphosphate.

ENZYME REGULATION: Activated by GCAP-1; inhibited by calcium.

TISSUE SPECIFICITY: Retina. Localized exclusively in the outer nuclear layer and inner segments of the rod and cone photoreceptor cells.

DOMAIN: The protein kinase domain is predicted to be catalytically inactive.

UniProt features for GUC2F_HUMAN » Retinal guanylyl cyclase 2
SIGNAL 1 50 Potential.
CHAIN 51 1108 Retinal guanylyl cyclase 2.
DOMAIN 532 812 Protein kinase.
DOMAIN 884 1014 Guanylate cyclase.
DISULFID 104 132 By similarity.
DISULFID 452 452 Interchain (By similarity).
DISULFID 460 460 Interchain (By similarity).
Amino Acid Sequence for GUC2F_HUMAN » Retinal guanylyl cyclase 2
MFLGLGRFSR LVLWFAAFRK LLGHHGLASA KFLWCLCLLS VMSLPQQVWT LPYKIGVVGP WACDSLFSKA LPEVAARLAI ERINRDPSFD LSYSFEYVIL NEDCQTSRAL SSFISHHQMA SGFIGPTNPG YCEAASLLGN SWDKGIFSWA CVNYELDNKI SYPTFSRTLP SPIRVLVTVM KYFQWAHAGV ISSDEDIWVH TANRVASALR SHGLPVGVVL TTGQDSQSMR KALQRIHQAD RIRIIIMCMH SALIGGETQM HLLECAHDLK MTDGTYVFVP YDALLYSLPY KHTPYQVLRN NPKLREAYDA VLTITVESQE KTFYQAFTEA AARGEIPEKL EFDQVSPLFG TIYNSIYFIA QAMNNAMKEN GQAGAASLVQ HSRNMQFHGF NQLMRTDSNG NGISEYVILD TNLKEWELHS TYTVDMEMEL LRFGGTPIHF PGGRPPRADA KCWFAEGKIC HGGIDPAFAM MVCLTLLIAL LSINGFAYFI RRRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQITSEVQS GRSPRLSFSS GSLTPATYEN SNIAIYEGDW VWLKKFSLGD FGDLKSIKSR ASDVFEMMKD LRHENINPLL GFFYDSGMFA IVTEFCSRGS LEDILTNQDV KLDWMFKSSL LLDLIKGMKY LHHREFVHGR LKSRNCVVDG RFVLKVTDYG FNDILEMLRL SEEESSMEEL LWTAPELLRA PRGSRLGSFA GDVYSFAIIM QEVMVRGTPF CMMDLPAQEI INRLKKPPPV YRPVVPPEHA PPECLQLMKQ CWAEAAEQRP TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR ERTEELEIEK QKTEKLLTQM LPPSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA AEIANMSLDI LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY RIHVSLSTVT ILQNLSEGYE VELRGRTELK GKGTEETFWL IGKKGFMKPL PVPPPVDKDG QVGHGLQPVE IAAFQRRKAE RQLVRNKP