GUC1B_MOUSE
ID GUC1B_MOUSE Reviewed; 201 AA.
AC Q8VBV8;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Guanylyl cyclase-activating protein 2;
DE Short=GCAP 2;
DE AltName: Full=Guanylate cyclase activator 1B;
GN Name=Guca1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9620085;
RA Cuenca N., Lopez S., Howes K., Kolb H.;
RT "The localization of guanylyl cyclase-activating proteins in the mammalian
RT retina.";
RL Invest. Ophthalmol. Vis. Sci. 39:1243-1250(1998).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15961391; DOI=10.1074/jbc.m501789200;
RA Strissel K.J., Lishko P.V., Trieu L.H., Kennedy M.J., Hurley J.B.,
RA Arshavsky V.Y.;
RT "Recoverin undergoes light-dependent intracellular translocation in rod
RT photoreceptors.";
RL J. Biol. Chem. 280:29250-29255(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25673692; DOI=10.1074/jbc.m115.639591;
RA Sakurai K., Chen J., Khani S.C., Kefalov V.J.;
RT "Regulation of mammalian cone phototransduction by recoverin and rhodopsin
RT kinase.";
RL J. Biol. Chem. 290:9239-9250(2015).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=29435986; DOI=10.1113/jp275779;
RA Morshedian A., Woodruff M.L., Fain G.L.;
RT "Role of recoverin in rod photoreceptor light adaptation.";
RL J. Physiol. (Lond.) 596:1513-1526(2018).
CC -!- FUNCTION: Stimulates two retinal guanylyl cyclase (GCs) GUCY2E and
CC GUCY2F when free calcium ions concentration is low, and inhibits GUCY2E
CC and GUCY2F when free calcium ions concentration is elevated (By
CC similarity). This Ca(2+)-sensitive regulation of GCs is a key event in
CC recovery of the dark state of rod photoreceptors following light
CC exposure (By similarity). May be involved in cone photoreceptor
CC response and recovery of response in bright light (PubMed:25673692).
CC {ECO:0000250|UniProtKB:P51177, ECO:0000269|PubMed:25673692}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51177};
CC Lipid-anchor {ECO:0000250|UniProtKB:P51177}. Photoreceptor inner
CC segment {ECO:0000269|PubMed:9620085}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000269|PubMed:15961391,
CC ECO:0000269|PubMed:9620085}. Note=Subcellular location is not affected
CC by light or dark conditions. {ECO:0000269|PubMed:15961391}.
CC -!- TISSUE SPECIFICITY: Expressed in rod photoreceptors in the retina (at
CC protein level). Expressed in cone photoreceptor cells (PubMed:9620085).
CC {ECO:0000269|PubMed:15961391, ECO:0000269|PubMed:9620085}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:P51177}.
CC -!- DISRUPTION PHENOTYPE: Guca1a and Guca1b double knockout mice show an
CC increase in response to light in dark-adapted cone photoreceptors
CC (PubMed:25673692). Dark-adapted cone photoreceptors show a delayed
CC response time and a delayed recovery time in response to light
CC (PubMed:25673692). Guca1a, Guca1b and Rcvrn triple knockout mice show
CC rod photoreceptors have a reduced current decay during light response
CC (PubMed:29435986). {ECO:0000269|PubMed:25673692,
CC ECO:0000269|PubMed:29435986}.
CC -!- MISCELLANEOUS: Binds three calcium ions. {ECO:0000250}.
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DR EMBL; AK033052; BAC28139.1; -; mRNA.
DR EMBL; BC018480; AAH18480.1; -; mRNA.
DR EMBL; BC018258; AAH18258.1; -; mRNA.
DR EMBL; BC029017; AAH29017.1; -; mRNA.
DR EMBL; BC029661; AAH29661.1; -; mRNA.
DR EMBL; BC031367; AAH31367.1; -; mRNA.
DR EMBL; BC031916; AAH31916.1; -; mRNA.
DR EMBL; BC033358; AAH33358.1; -; mRNA.
DR EMBL; BC033380; AAH33380.1; -; mRNA.
DR EMBL; BC033383; AAH33383.1; -; mRNA.
DR EMBL; BC034331; AAH34331.1; -; mRNA.
DR EMBL; BC034595; AAH34595.1; -; mRNA.
DR CCDS; CCDS28847.1; -.
DR RefSeq; NP_666191.1; NM_146079.1.
DR AlphaFoldDB; Q8VBV8; -.
DR SMR; Q8VBV8; -.
DR BioGRID; 223323; 1.
DR STRING; 10090.ENSMUSP00000024774; -.
DR PhosphoSitePlus; Q8VBV8; -.
DR PaxDb; Q8VBV8; -.
DR PRIDE; Q8VBV8; -.
DR ProteomicsDB; 269845; -.
DR Antibodypedia; 30141; 145 antibodies from 22 providers.
DR DNASU; 107477; -.
DR Ensembl; ENSMUST00000024774; ENSMUSP00000024774; ENSMUSG00000023979.
DR GeneID; 107477; -.
DR KEGG; mmu:107477; -.
DR UCSC; uc008cvb.1; mouse.
DR CTD; 2979; -.
DR MGI; MGI:1194489; Guca1b.
DR VEuPathDB; HostDB:ENSMUSG00000023979; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000157530; -.
DR HOGENOM; CLU_072366_4_0_1; -.
DR InParanoid; Q8VBV8; -.
DR OMA; HEFKGFF; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q8VBV8; -.
DR TreeFam; TF333971; -.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR BioGRID-ORCS; 107477; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Guca1b; mouse.
DR PRO; PR:Q8VBV8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8VBV8; protein.
DR Bgee; ENSMUSG00000023979; Expressed in layer of retina and 49 other tissues.
DR ExpressionAtlas; Q8VBV8; baseline and differential.
DR Genevisible; Q8VBV8; MM.
DR GO; GO:0120199; C:cone photoreceptor outer segment; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activator activity; IDA:MGI.
DR GO; GO:0030249; F:guanylate cyclase regulator activity; IGI:MGI.
DR GO; GO:0007602; P:phototransduction; IMP:MGI.
DR GO; GO:0031282; P:regulation of guanylate cyclase activity; IGI:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR015756; GCAP-2.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR PANTHER; PTHR23055:SF11; PTHR23055:SF11; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 5.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cell projection; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Reference proteome; Repeat; Sensory transduction;
KW Vision.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..201
FT /note="Guanylyl cyclase-activating protein 2"
FT /id="PRO_0000073809"
FT DOMAIN 14..31
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 34..52
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 53..88
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 89..124
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 142..177
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 201 AA; 23520 MW; 75209102B3CDC208 CRC64;
MGQQLSWEEA EAAGEMDVAE LQEWYKKFVV ECPSGTLFMH EFKRFFKVTG NEEASQYVES
MFRAFDKNGD NTIDFLEYVA ALNLVLRGSL EHKLKWTFKI YDKDRNGCID RLELLDIVEA
IYKLKKACRA ELDLEHQGQL LTPEEVVDRI FLLVDENGDG QLSLTEFIEG ARRDKWVMKM
LQMDINPGCW ITQQRRRSAM F
