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P47872 (SCTR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Secretin receptor

Short name=SCT-R
Gene names
Name:SCTR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This is a receptor for secretin. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the G-protein coupled receptor 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 440418Secretin receptor
PRO_0000012852

Regions

Topological domain23 – 143121Extracellular Potential
Transmembrane144 – 16724Helical; Name=1; Potential
Topological domain168 – 1747Cytoplasmic Potential
Transmembrane175 – 19420Helical; Name=2; Potential
Topological domain195 – 21622Extracellular Potential
Transmembrane217 – 24024Helical; Name=3; Potential
Topological domain241 – 25414Cytoplasmic Potential
Transmembrane255 – 27622Helical; Name=4; Potential
Topological domain277 – 29418Extracellular Potential
Transmembrane295 – 31723Helical; Name=5; Potential
Topological domain318 – 34326Cytoplasmic Potential
Transmembrane344 – 36219Helical; Name=6; Potential
Topological domain363 – 3697Extracellular Potential
Transmembrane370 – 39223Helical; Name=7; Potential
Topological domain393 – 44048Cytoplasmic Potential

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1061N-linked (GlcNAc...) Potential
Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential

Natural variations

Natural variant1101D → N.
Corresponds to variant rs6726491 [ dbSNP | Ensembl ].
VAR_049456
Natural variant1221A → P.
Corresponds to variant rs3731600 [ dbSNP | Ensembl ].
VAR_033970

Experimental info

Sequence conflict1241G → A in AAC50106. Ref.1
Sequence conflict2101A → P in AAA87556. Ref.2
Sequence conflict3081I → F in AAA64949. Ref.3
Sequence conflict3331E → Q in AAA64949. Ref.3
Sequence conflict3771G → A in AAC50106. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47872 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: E22CDD0EE7C0ACC1

FASTA44050,207
        10         20         30         40         50         60 
MRPHLSPPLQ QLLLPVLLAC AAHSTGALPR LCDVLQVLWE EQDQCLQELS REQTGDLGTE 

        70         80         90        100        110        120 
QPVPGCEGMW DNISCWPSSV PGRMVEVECP RFLRMLTSRN GSLFRNCTQD GWSETFPRPN 

       130        140        150        160        170        180 
LACGVNVNDS SNEKRHSYLL KLKVMYTVGY SSSLVMLLVA LGILCAFRRL HCTRNYIHMH 

       190        200        210        220        230        240 
LFVSFILRAL SNFIKDAVLF SSDDVTYCDA HRAGCKLVMV LFQYCIMANY SWLLVEGLYL 

       250        260        270        280        290        300 
HTLLAISFFS ERKYLQGFVA FGWGSPAIFV ALWAIARHFL EDVGCWDINA NASIWWIIRG 

       310        320        330        340        350        360 
PVILSILINF ILFINILRIL MRKLRTQETR GNEVSHYKRL ARSTLLLIPL FGIHYIVFAF 

       370        380        390        400        410        420 
SPEDAMEIQL FFELALGSFQ GLVVAVLYCF LNGEVQLEVQ KKWQQWHLRE FPLHPVASFS 

       430        440 
NSTKASHLEQ SQGTCRTSII 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and functional expression of a human pancreatic secretin receptor."
Jiang S., Ulrich C.D.
Biochem. Biophys. Res. Commun. 207:883-890(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[2]"Molecular cloning and functional characterization of a human secretin receptor."
Chow B.K.-C.
Biochem. Biophys. Res. Commun. 212:204-211(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreas.
[3]"Molecular cloning and expression of a human secretin receptor."
Patel D.R., Kong Y., Sreedharan S.P.
Mol. Pharmacol. 47:467-473(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[4]"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].
[5]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
King M.M., Aronstam R.S., Sharma S.V.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20178 mRNA. Translation: AAC50106.1.
U28281 mRNA. Translation: AAA87556.1.
U13989 mRNA. Translation: AAA64949.1.
AB065660 Genomic DNA. Translation: BAC05886.1.
AY462218 mRNA. Translation: AAR25625.1.
AC013275 Genomic DNA. Translation: AAY14741.1.
CH471103 Genomic DNA. Translation: EAW95219.1.
PIRJC2532.
RefSeqNP_002971.2. NM_002980.2.
UniGeneHs.42091.

3D structure databases

ProteinModelPortalP47872.
SMRP47872. Positions 40-126, 142-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112248. 6 interactions.
IntActP47872. 2 interactions.
MINTMINT-1217464.
STRING9606.ENSP00000019103.

Chemistry

BindingDBP47872.
ChEMBLCHEMBL1925.
DrugBankDB00021. Secretin.
GuidetoPHARMACOLOGY252.

Protein family/group databases

TCDB9.A.14.4.10. the g-protein-coupled receptor (gpcr) family.
GPCRDBSearch...

Polymorphism databases

DMDM2506489.

Proteomic databases

PaxDbP47872.
PRIDEP47872.

Protocols and materials databases

DNASU6344.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000019103; ENSP00000019103; ENSG00000080293.
GeneID6344.
KEGGhsa:6344.
UCSCuc002tlz.3. human.

Organism-specific databases

CTD6344.
GeneCardsGC02M120292.
HGNCHGNC:10608. SCTR.
HPAHPA007269.
MIM182098. gene.
neXtProtNX_P47872.
PharmGKBPA35018.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG244152.
HOGENOMHOG000008249.
HOVERGENHBG008318.
InParanoidP47872.
KOK04588.
OMANDSSNEK.
OrthoDBEOG7TF78W.
PhylomeDBP47872.
TreeFamTF315710.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP47872.

Gene expression databases

BgeeP47872.
CleanExHS_SCTR.
GenevestigatorP47872.

Family and domain databases

InterProIPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR002144. GPCR_2_secretin_rcpt.
[Graphical view]
PANTHERPTHR12011:SF29. PTHR12011:SF29. 1 hit.
PfamPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSPR00249. GPCRSECRETIN.
PR00490. SECRETINR.
SMARTSM00008. HormR. 1 hit.
[Graphical view]
PROSITEPS00649. 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]
ProtoNetSearch...

Other

GeneWikiSecretin_receptor.
GenomeRNAi6344.
NextBio24644.
PROP47872.
SOURCESearch...

Entry information

Entry nameSCTR_HUMAN
AccessionPrimary (citable) accession number: P47872
Secondary accession number(s): Q12961, Q13213, Q53T00
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries