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Protein

Pituitary adenylate cyclase-activating polypeptide type I receptor

Gene

ADCYAP1R1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • neuropeptide binding Source: Ensembl
  • receptor activity Source: ProtInc
  • vasoactive intestinal polypeptide receptor activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Differentiation, Spermatogenesis

Enzyme and pathway databases

ReactomeiREACT_11046. NGF-independant TRKA activation.
REACT_18377. Glucagon-type ligand receptors.
REACT_19327. G alpha (s) signalling events.

Protein family/group databases

TCDBi9.A.14.4.8. the g-protein-coupled receptor (gpcr) family.

Names & Taxonomyi

Protein namesi
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 namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:242. ADCYAP1R1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 155135ExtracellularSequence AnalysisAdd
BLAST
Transmembranei156 – 17823Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini179 – 1868CytoplasmicSequence Analysis
Transmembranei187 – 20519Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini206 – 22722ExtracellularSequence AnalysisAdd
BLAST
Transmembranei228 – 25326Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini254 – 26815CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei269 – 29123Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini292 – 30918ExtracellularSequence AnalysisAdd
BLAST
Transmembranei310 – 33223Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini333 – 35018CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei351 – 37121Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini372 – 38514ExtracellularSequence AnalysisAdd
BLAST
Transmembranei386 – 40520Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini406 – 46863CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • bicellular tight junction Source: Ensembl
  • caveola Source: Ensembl
  • cell surface Source: Ensembl
  • endosome Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • neuron projection Source: Ensembl
  • plasma membrane Source: Reactome
  • receptor complex Source: MGI
  • rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141V → A: Reduced affinity for ADCYAP1. 1 Publication
Mutagenesisi125 – 1251E → R: Reduced affinity for ADCYAP1. 2 Publications
Mutagenesisi128 – 1281P → A: Reduced affinity for ADCYAP1. 1 Publication
Mutagenesisi138 – 1381E → R: Reduced affinity for ADCYAP1. 1 Publication
Mutagenesisi139 – 1391Y → A: Strongly reduced affinity for ADCYAP1. 1 Publication

Organism-specific databases

PharmGKBiPA24565.

Polymorphism and mutation databases

BioMutaiADCYAP1R1.
DMDMi1171986.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 468448Pituitary adenylate cyclase-activating polypeptide type I receptorPRO_0000012841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 63
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi54 ↔ 118
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi77 ↔ 134
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP41586.
PaxDbiP41586.
PRIDEiP41586.

PTM databases

PhosphoSiteiP41586.

Expressioni

Tissue specificityi

Most abundant in the brain, low expression in the lung, liver, thymus, spleen, pancreas and placenta.

Gene expression databases

BgeeiP41586.
CleanExiHS_ADCYAP1R1.
ExpressionAtlasiP41586. baseline and differential.
GenevisibleiP41586. HS.

Organism-specific databases

HPAiHPA049877.

Interactioni

Subunit structurei

Interacts (via N-terminal extracellular domain) with ADCYAP1.1 Publication

Protein-protein interaction databases

DIPiDIP-42467N.
MINTiMINT-1217291.

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi30 – 4415Combined sources
Turni48 – 503Combined sources
Beta strandi73 – 753Combined sources
Beta strandi114 – 1163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JODNMR-A22-143[»]
3N94X-ray1.80A26-140[»]
ProteinModelPortaliP41586.
SMRiP41586. Positions 26-140, 150-410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41586.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni125 – 13915Important for ligand binding and specificityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG330024.
GeneTreeiENSGT00760000118800.
HOGENOMiHOG000008249.
HOVERGENiHBG008318.
InParanoidiP41586.
KOiK04587.
OrthoDBiEOG7TF78W.
PhylomeDBiP41586.
TreeFamiTF315710.

Family and domain databases

InterProiIPR017981. 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]
PfamiPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01156. PACAPRECEPTR.
SMARTiSM00008. HormR. 1 hit.
[Graphical view]
PROSITEiPS00649. 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]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform N (identifier: P41586-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGVVHVSLA ALLLLPMAPA MHSDCIFKKE QAMCLEKIQR ANELMGFNDS
60 70 80 90 100
SPGCPGMWDN ITCWKPAHVG EMVLVSCPEL FRIFNPDQVW ETETIGESDF
110 120 130 140 150
GDSNSLDLSD MGVVSRNCTE DGWSEPFPHY FDACGFDEYE SETGDQDYYY
160 170 180 190 200
LSVKALYTVG YSTSLVTLTT AMVILCRFRK LHCTRNFIHM NLFVSFMLRA
210 220 230 240 250
ISVFIKDWIL YAEQDSNHCF ISTVECKAVM VFFHYCVVSN YFWLFIEGLY
260 270 280 290 300
LFTLLVETFF PERRYFYWYT IIGWGTPTVC VTVWATLRLY FDDTGCWDMN
310 320 330 340 350
DSTALWWVIK GPVVGSIMVN FVLFIGIIVI LVQKLQSPDM GGNESSIYLR
360 370 380 390 400
LARSTLLLIP LFGIHYTVFA FSPENVSKRE RLVFELGLGS FQGFVVAVLY
410 420 430 440 450
CFLNGEVQAE IKRKWRSWKV NRYFAVDFKH RHPSLASSGV NGGTQLSILS
460
KSSSQIRMSG LPADNLAT
Length:468
Mass (Da):53,314
Last modified:November 1, 1995 - v1
Checksum:iBB515B84E9F28977
GO
Isoform N-HOP1 (identifier: P41586-2) [UniParc]FASTAAdd to basket

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

Show »
Length:496
Mass (Da):56,531
Checksum:iCBA040A9924D367A
GO
Isoform S (identifier: P41586-3) [UniParc]FASTAAdd to basket

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

Show »
Length:447
Mass (Da):51,030
Checksum:i71C127C1056CA6AD
GO
Isoform S-HOP1 (identifier: P41586-4) [UniParc]FASTAAdd to basket

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

Show »
Length:475
Mass (Da):54,248
Checksum:i11ECA8F276CE00B9
GO
Isoform VS (identifier: P41586-5) [UniParc]FASTAAdd to basket

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

Show »
Length:411
Mass (Da):46,957
Checksum:i614BB6FB467ABD2A
GO

Sequence cautioni

The sequence BAA04466.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform N-HOP1 (identifier: P41586-2)
Sequence conflicti350 – 3501Missing in AAI43680 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei53 – 8836Missing in isoform VS. CuratedVSP_042669Add
BLAST
Alternative sequencei89 – 10921Missing in isoform S, isoform S-HOP1 and isoform VS. CuratedVSP_042670Add
BLAST
Alternative sequencei348 – 3481Y → YFSCVQKCYCKPQRAQQHSC KMSELSTIT in isoform N-HOP1 and isoform S-HOP1. 1 PublicationVSP_042671

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5433.1. [P41586-1]
CCDS56480.1. [P41586-2]
CCDS56481.1. [P41586-3]
PIRiJN0902.
RefSeqiNP_001109.2. NM_001118.4. [P41586-1]
NP_001186564.1. NM_001199635.1. [P41586-2]
NP_001186565.1. NM_001199636.1.
NP_001186566.1. NM_001199637.1. [P41586-3]
XP_005249675.1. XM_005249618.3. [P41586-5]
UniGeneiHs.377783.

Genome annotation databases

EnsembliENST00000304166; ENSP00000306620; ENSG00000078549.
ENST00000396211; ENSP00000379514; ENSG00000078549. [P41586-2]
ENST00000409363; ENSP00000387335; ENSG00000078549. [P41586-3]
ENST00000614107; ENSP00000483721; ENSG00000078549. [P41586-2]
GeneIDi117.
KEGGihsa:117.
UCSCiuc003tca.2. human. [P41586-1]
uc003tcb.2. human. [P41586-3]
uc003tce.2. human. [P41586-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5433.1. [P41586-1]
CCDS56480.1. [P41586-2]
CCDS56481.1. [P41586-3]
PIRiJN0902.
RefSeqiNP_001109.2. NM_001118.4. [P41586-1]
NP_001186564.1. NM_001199635.1. [P41586-2]
NP_001186565.1. NM_001199636.1.
NP_001186566.1. NM_001199637.1. [P41586-3]
XP_005249675.1. XM_005249618.3. [P41586-5]
UniGeneiHs.377783.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JODNMR-A22-143[»]
3N94X-ray1.80A26-140[»]
ProteinModelPortaliP41586.
SMRiP41586. Positions 26-140, 150-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42467N.
MINTiMINT-1217291.

Chemistry

BindingDBiP41586.
ChEMBLiCHEMBL5399.
GuidetoPHARMACOLOGYi370.

Protein family/group databases

TCDBi9.A.14.4.8. the g-protein-coupled receptor (gpcr) family.
GPCRDBiSearch...

PTM databases

PhosphoSiteiP41586.

Polymorphism and mutation databases

BioMutaiADCYAP1R1.
DMDMi1171986.

Proteomic databases

MaxQBiP41586.
PaxDbiP41586.
PRIDEiP41586.

Protocols and materials databases

DNASUi117.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304166; ENSP00000306620; ENSG00000078549.
ENST00000396211; ENSP00000379514; ENSG00000078549. [P41586-2]
ENST00000409363; ENSP00000387335; ENSG00000078549. [P41586-3]
ENST00000614107; ENSP00000483721; ENSG00000078549. [P41586-2]
GeneIDi117.
KEGGihsa:117.
UCSCiuc003tca.2. human. [P41586-1]
uc003tcb.2. human. [P41586-3]
uc003tce.2. human. [P41586-2]

Organism-specific databases

CTDi117.
GeneCardsiGC07P031058.
HGNCiHGNC:242. ADCYAP1R1.
HPAiHPA049877.
MIMi102981. gene.
neXtProtiNX_P41586.
PharmGKBiPA24565.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG330024.
GeneTreeiENSGT00760000118800.
HOGENOMiHOG000008249.
HOVERGENiHBG008318.
InParanoidiP41586.
KOiK04587.
OrthoDBiEOG7TF78W.
PhylomeDBiP41586.
TreeFamiTF315710.

Enzyme and pathway databases

ReactomeiREACT_11046. NGF-independant TRKA activation.
REACT_18377. Glucagon-type ligand receptors.
REACT_19327. G alpha (s) signalling events.

Miscellaneous databases

ChiTaRSiADCYAP1R1. human.
EvolutionaryTraceiP41586.
GeneWikiiADCYAP1R1.
GenomeRNAii117.
NextBioi455.
PROiP41586.
SOURCEiSearch...

Gene expression databases

BgeeiP41586.
CleanExiHS_ADCYAP1R1.
ExpressionAtlasiP41586. baseline and differential.
GenevisibleiP41586. HS.

Family and domain databases

InterProiIPR017981. 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]
PfamiPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01156. PACAPRECEPTR.
SMARTiSM00008. HormR. 1 hit.
[Graphical view]
PROSITEiPS00649. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiPACR_HUMAN
AccessioniPrimary (citable) accession number: P41586
Secondary accession number(s): A8K1Y1
, B7ZLA7, B8ZZK3, Q17S10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.