P41586 (PACR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pituitary adenylate cyclase-activating polypeptide type I receptor
Short name=PACAP type I receptor
Short name=PACAP-R-1
Short name=PACAP-R1

Gene names

Name:

ADCYAP1R1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is a receptor for PACAP-27 and PACAP-38. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. May regulate the release of adrenocorticotropin, luteinizing hormone, growth hormone, prolactin, epinephrine, and catecholamine. May play a role in spermatogenesis and sperm motility. Causes smooth muscle relaxation and secretion in the gastrointestinal tract.
Subunit structure	Interacts (via N-terminal extracellular domain) with ADCYAP1.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Most abundant in the brain, low expression in the lung, liver, thymus, spleen, pancreas and placenta.
Sequence similarities	Belongs to the G-protein coupled receptor 2 family.
Sequence caution	The sequence BAA04466.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of adenylate cyclase activity Traceable author statement. Source: Reactome activation of phospholipase C activity Inferred from electronic annotation. Source: Compara cAMP-mediated signaling Inferred from electronic annotation. Source: Compara cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW development of primary female sexual characteristics Inferred from electronic annotation. Source: Compara multicellular organismal response to stress Inferred from electronic annotation. Source: Compara negative regulation of cell death Inferred from electronic annotation. Source: Compara nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome positive regulation of calcium ion transport into cytosol Inferred from electronic annotation. Source: Compara positive regulation of inositol phosphate biosynthetic process Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	caveola Inferred from electronic annotation. Source: Compara cell surface Inferred from electronic annotation. Source: Compara endosome Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc neuron projection Inferred from electronic annotation. Source: Compara rough endoplasmic reticulum Inferred from electronic annotation. Source: Compara tight junction Inferred from electronic annotation. Source: Compara
Molecular_function	neuropeptide binding Inferred from electronic annotation. Source: Compara receptor activity Traceable author statement Ref.1. Source: ProtInc vasoactive intestinal polypeptide receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform N (identifier: P41586-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform N-HOP1 (identifier: P41586-2)

The sequence of this isoform differs from the canonical sequence as follows:
     348-348: Y → YFSCVQKCYCKPQRAQQHSCKMSELSTIT

Note: Ref.7 (AAI43680) sequence is in conflict in position: 350:S->Missing.

Isoform S (identifier: P41586-3)

The sequence of this isoform differs from the canonical sequence as follows:
     89-109: Missing.

Isoform S-HOP1 (identifier: P41586-4)

The sequence of this isoform differs from the canonical sequence as follows:
     89-109: Missing.
     348-348: Y → YFSCVQKCYCKPQRAQQHSCKMSELSTIT

Isoform VS (identifier: P41586-5)

The sequence of this isoform differs from the canonical sequence as follows:
     53-88: Missing.
     89-109: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 468

448

Pituitary adenylate cyclase-activating polypeptide type I receptor

PRO_0000012841

Regions

Topological domain

21 – 155

135

Extracellular Potential

Transmembrane

156 – 178

23

Helical; Name=1; Potential

Topological domain

179 – 186

8

Cytoplasmic Potential

Transmembrane

187 – 205

19

Helical; Name=2; Potential

Topological domain

206 – 227

22

Extracellular Potential

Transmembrane

228 – 253

26

Helical; Name=3; Potential

Topological domain

254 – 268

15

Cytoplasmic Potential

Transmembrane

269 – 291

23

Helical; Name=4; Potential

Topological domain

292 – 309

18

Extracellular Potential

Transmembrane

310 – 332

23

Helical; Name=5; Potential

Topological domain

333 – 350

18

Cytoplasmic Potential

Transmembrane

351 – 371

21

Helical; Name=6; Potential

Topological domain

372 – 385

14

Extracellular Potential

Transmembrane

386 – 405

20

Helical; Name=7; Potential

Topological domain

406 – 468

63

Cytoplasmic Potential

Region

125 – 139

15

Important for ligand binding and specificity

Amino acid modifications

Glycosylation

48

1

N-linked (GlcNAc...) Potential

Glycosylation

60

1

N-linked (GlcNAc...) Potential

Glycosylation

117

1

N-linked (GlcNAc...) Potential

Glycosylation

300

1

N-linked (GlcNAc...) Potential

Glycosylation

375

1

N-linked (GlcNAc...) Potential

Disulfide bond

34 ↔ 63

Ref.10 Ref.11

Disulfide bond

54 ↔ 118

Ref.10 Ref.11

Disulfide bond

77 ↔ 134

Ref.10 Ref.11

Natural variations

Alternative sequence

53 – 88

36

Missing in isoform VS.

VSP_042669

Alternative sequence

89 – 109

21

Missing in isoform S, isoform S-HOP1 and isoform VS.

VSP_042670

Alternative sequence

348

1

Y → YFSCVQKCYCKPQRAQQHSC KMSELSTIT in isoform N-HOP1 and isoform S-HOP1.

VSP_042671

Experimental info

Mutagenesis

114

1

V → A: Reduced affinity for ADCYAP1. Ref.10

Mutagenesis

125

1

E → R: Reduced affinity for ADCYAP1. Ref.10 Ref.11

Mutagenesis

128

1

P → A: Reduced affinity for ADCYAP1. Ref.10

Mutagenesis

138

1

E → R: Reduced affinity for ADCYAP1. Ref.10

Mutagenesis

139

1

Y → A: Strongly reduced affinity for ADCYAP1. Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

468

Helix Strand Turn

Details...

Helix

26 – 47

22

Turn

48 – 50

3

Beta strand

72 – 76

5

Helix

79 – 83

5

Beta strand

113 – 119

7

Helix

130 – 134

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform N [UniParc]. Last modified November 1, 1995. Version 1. Checksum: BB515B84E9F28977	FASTA	468	53,314
	10 20 30 40 50 60 MAGVVHVSLA ALLLLPMAPA MHSDCIFKKE QAMCLEKIQR ANELMGFNDS SPGCPGMWDN 70 80 90 100 110 120 ITCWKPAHVG EMVLVSCPEL FRIFNPDQVW ETETIGESDF GDSNSLDLSD MGVVSRNCTE 130 140 150 160 170 180 DGWSEPFPHY FDACGFDEYE SETGDQDYYY LSVKALYTVG YSTSLVTLTT AMVILCRFRK 190 200 210 220 230 240 LHCTRNFIHM NLFVSFMLRA ISVFIKDWIL YAEQDSNHCF ISTVECKAVM VFFHYCVVSN 250 260 270 280 290 300 YFWLFIEGLY LFTLLVETFF PERRYFYWYT IIGWGTPTVC VTVWATLRLY FDDTGCWDMN 310 320 330 340 350 360 DSTALWWVIK GPVVGSIMVN FVLFIGIIVI LVQKLQSPDM GGNESSIYLR LARSTLLLIP 370 380 390 400 410 420 LFGIHYTVFA FSPENVSKRE RLVFELGLGS FQGFVVAVLY CFLNGEVQAE IKRKWRSWKV 430 440 450 460 NRYFAVDFKH RHPSLASSGV NGGTQLSILS KSSSQIRMSG LPADNLAT
	Isoform N-HOP1 [UniParc]. Checksum: CBA040A9924D367A	FASTA	496	56,531
	10 20 30 40 50 60 MAGVVHVSLA ALLLLPMAPA MHSDCIFKKE QAMCLEKIQR ANELMGFNDS SPGCPGMWDN 70 80 90 100 110 120 ITCWKPAHVG EMVLVSCPEL FRIFNPDQVW ETETIGESDF GDSNSLDLSD MGVVSRNCTE 130 140 150 160 170 180 DGWSEPFPHY FDACGFDEYE SETGDQDYYY LSVKALYTVG YSTSLVTLTT AMVILCRFRK 190 200 210 220 230 240 LHCTRNFIHM NLFVSFMLRA ISVFIKDWIL YAEQDSNHCF ISTVECKAVM VFFHYCVVSN 250 260 270 280 290 300 YFWLFIEGLY LFTLLVETFF PERRYFYWYT IIGWGTPTVC VTVWATLRLY FDDTGCWDMN 310 320 330 340 350 360 DSTALWWVIK GPVVGSIMVN FVLFIGIIVI LVQKLQSPDM GGNESSIYFS CVQKCYCKPQ 370 380 390 400 410 420 RAQQHSCKMS ELSTITLRLA RSTLLLIPLF GIHYTVFAFS PENVSKRERL VFELGLGSFQ 430 440 450 460 470 480 GFVVAVLYCF LNGEVQAEIK RKWRSWKVNR YFAVDFKHRH PSLASSGVNG GTQLSILSKS 490 SSQIRMSGLP ADNLAT
	Isoform S [UniParc]. Checksum: 71C127C1056CA6AD	FASTA	447	51,030
	10 20 30 40 50 60 MAGVVHVSLA ALLLLPMAPA MHSDCIFKKE QAMCLEKIQR ANELMGFNDS SPGCPGMWDN 70 80 90 100 110 120 ITCWKPAHVG EMVLVSCPEL FRIFNPDQDM GVVSRNCTED GWSEPFPHYF DACGFDEYES 130 140 150 160 170 180 ETGDQDYYYL SVKALYTVGY STSLVTLTTA MVILCRFRKL HCTRNFIHMN LFVSFMLRAI 190 200 210 220 230 240 SVFIKDWILY AEQDSNHCFI STVECKAVMV FFHYCVVSNY FWLFIEGLYL FTLLVETFFP 250 260 270 280 290 300 ERRYFYWYTI IGWGTPTVCV TVWATLRLYF DDTGCWDMND STALWWVIKG PVVGSIMVNF 310 320 330 340 350 360 VLFIGIIVIL VQKLQSPDMG GNESSIYLRL ARSTLLLIPL FGIHYTVFAF SPENVSKRER 370 380 390 400 410 420 LVFELGLGSF QGFVVAVLYC FLNGEVQAEI KRKWRSWKVN RYFAVDFKHR HPSLASSGVN 430 440 GGTQLSILSK SSSQIRMSGL PADNLAT
	Isoform S-HOP1 [UniParc]. Checksum: 11ECA8F276CE00B9	FASTA	475	54,248
	10 20 30 40 50 60 MAGVVHVSLA ALLLLPMAPA MHSDCIFKKE QAMCLEKIQR ANELMGFNDS SPGCPGMWDN 70 80 90 100 110 120 ITCWKPAHVG EMVLVSCPEL FRIFNPDQDM GVVSRNCTED GWSEPFPHYF DACGFDEYES 130 140 150 160 170 180 ETGDQDYYYL SVKALYTVGY STSLVTLTTA MVILCRFRKL HCTRNFIHMN LFVSFMLRAI 190 200 210 220 230 240 SVFIKDWILY AEQDSNHCFI STVECKAVMV FFHYCVVSNY FWLFIEGLYL FTLLVETFFP 250 260 270 280 290 300 ERRYFYWYTI IGWGTPTVCV TVWATLRLYF DDTGCWDMND STALWWVIKG PVVGSIMVNF 310 320 330 340 350 360 VLFIGIIVIL VQKLQSPDMG GNESSIYFSC VQKCYCKPQR AQQHSCKMSE LSTITLRLAR 370 380 390 400 410 420 STLLLIPLFG IHYTVFAFSP ENVSKRERLV FELGLGSFQG FVVAVLYCFL NGEVQAEIKR 430 440 450 460 470 KWRSWKVNRY FAVDFKHRHP SLASSGVNGG TQLSILSKSS SQIRMSGLPA DNLAT
	Isoform VS [UniParc]. Checksum: 614BB6FB467ABD2A	FASTA	411	46,957
	10 20 30 40 50 60 MAGVVHVSLA ALLLLPMAPA MHSDCIFKKE QAMCLEKIQR ANELMGFNDS SPDMGVVSRN 70 80 90 100 110 120 CTEDGWSEPF PHYFDACGFD EYESETGDQD YYYLSVKALY TVGYSTSLVT LTTAMVILCR 130 140 150 160 170 180 FRKLHCTRNF IHMNLFVSFM LRAISVFIKD WILYAEQDSN HCFISTVECK AVMVFFHYCV 190 200 210 220 230 240 VSNYFWLFIE GLYLFTLLVE TFFPERRYFY WYTIIGWGTP TVCVTVWATL RLYFDDTGCW 250 260 270 280 290 300 DMNDSTALWW VIKGPVVGSI MVNFVLFIGI IVILVQKLQS PDMGGNESSI YLRLARSTLL 310 320 330 340 350 360 LIPLFGIHYT VFAFSPENVS KRERLVFELG LGSFQGFVVA VLYCFLNGEV QAEIKRKWRS 370 380 390 400 410 WKVNRYFAVD FKHRHPSLAS SGVNGGTQLS ILSKSSSQIR MSGLPADNLA T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional expression of a cDNA encoding a human pituitary adenylate cyclase activating polypeptide receptor." Ogi K., Miyamoto Y., Masuda Y., Habata Y., Hosoya M., Ohtaki T., Masuo Y., Onda H., Fujino M. Biochem. Biophys. Res. Commun. 196:1511-1521(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N). Tissue: Pituitary.
[2]	"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes." Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." King M., Aronstam R.S., Sharma S.V. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM N). Tissue: Brain.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM N). Tissue: Hippocampus.
[5]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM N-HOP1). Tissue: Brain and Testis.
[8]	"Human type I pituitary adenylate cyclase activating polypeptide receptor (ADCYAP1R): localization to chromosome band 7p14 and integration into the cytogenetic, physical and genetic map of chromosome 7." Stoffel M., Espinosa R., Trabb J.B., le Beau M.M., Bell G.I. Genomics 23:697-699(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 418-468. Tissue: Placenta.
[9]	"N-terminal splice variants of the type I PACAP receptor: isolation, characterization and ligand binding/selectivity determinants." Dautzenberg F.M., Mevenkamp G., Wille S., Hauger R.L. J. Neuroendocrinol. 11:941-949(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[10]	"Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RS." Sun C., Song D., Davis-Taber R.A., Barrett L.W., Scott V.E., Richardson P.L., Pereda-Lopez A., Uchic M.E., Solomon L.R., Lake M.R., Walter K.A., Hajduk P.J., Olejniczak E.T. Proc. Natl. Acad. Sci. U.S.A. 104:7875-7880(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 22-143 IN COMPLEX WITH ADCYAP1, MUTAGENESIS OF VAL-114; GLU-125; PRO-128; GLU-138 AND TYR-139, DISULFIDE BONDS.
[11]	"Crystal structure of the PAC1R extracellular domain unifies a consensus fold for hormone recognition by class B G-protein coupled receptors." Kumar S., Pioszak A., Zhang C., Swaminathan K., Xu H.E. PLoS ONE 6:E19682-E19682(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 26-140, MUTAGENESIS OF GLU-125, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D17516 mRNA. Translation: BAA04466.1. Different initiation.
AB065700 Genomic DNA. Translation: BAC05923.1.
AY366498 mRNA. Translation: AAQ72806.1.
AK290046 mRNA. Translation: BAF82735.1.
AC006466 Genomic DNA. No translation available.
BC117116 mRNA. Translation: AAI17117.1.
BC136267 mRNA. Translation: AAI36268.1.
BC143679 mRNA. Translation: AAI43680.1.
CH471073 Genomic DNA. Translation: EAW93978.1.
U09216 Genomic DNA. Translation: AAA19323.1.

IPI

IPI00299406.
IPI00437612.
IPI00917967.

PIR

JN0902.

RefSeq

NP_001109.2. NM_001118.4.
NP_001186564.1. NM_001199635.1.
NP_001186565.1. NM_001199636.1.
NP_001186566.1. NM_001199637.1.

UniGene

Hs.377783.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JOD	NMR	-	A	22-143	[»]
3N94	X-ray	1.80	A	26-140	[»]

ProteinModelPortal

P41586.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1217291.

STRING

9606.ENSP00000306620.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P41586.

Polymorphism databases

DMDM

1171986.

Proteomic databases

PaxDb

P41586.

PRIDE

P41586.

Protocols and materials databases

DNASU

117.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000304166; ENSP00000306620; ENSG00000078549.
ENST00000396211; ENSP00000379514; ENSG00000078549.
ENST00000409363; ENSP00000387335; ENSG00000078549.

GeneID

117.

KEGG

hsa:117.

UCSC

uc003tca.2. human.

Organism-specific databases

CTD

117.

GeneCards

GC07P031058.

HGNC

HGNC:242. ADCYAP1R1.

HPA

HPA049877.

MIM

102981. gene.

neXtProt

NX_P41586.

PharmGKB

PA24565.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG330024.

HOGENOM

HOG000008249.

HOVERGEN

HBG008318.

KO

K04587.

OrthoDB

EOG4B5P5B.

PhylomeDB

P41586.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P41586.

Bgee

P41586.

CleanEx

HS_ADCYAP1R1.

Genevestigator

P41586.

GermOnline

ENSG00000078549. Homo sapiens.

Family and domain databases

InterPro

IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR002285. GPCR_2_PACAP_1_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]

PANTHER

PTHR12011:SF30. PTHR12011:SF30. 1 hit.

Pfam

PF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]

PRINTS

PR00249. GPCRSECRETIN.
PR01156. PACAPRECEPTR.

SMART

SM00008. HormR. 1 hit.
[Graphical view]

PROSITE

PS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

ProtoNet

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Other

BindingDB

P41586.

ChEMBL

CHEMBL5399.

ChiTaRS

ADCYAP1R1. human.

EvolutionaryTrace

P41586.

GenomeRNAi

117.

NextBio

455.

SOURCE

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Entry information

Entry name

PACR_HUMAN

Accession

Primary (citable) accession number: P41586
Secondary accession number(s): A8K1Y1 , B7ZLA7, B8ZZK3, Q17S10

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.