Reviewed, UniProtKB/Swiss-Prot P01175 (NEU1_BOVIN)

Names and origin

Protein names

Recommended name:
    Oxytocin-neurophysin 1
      Short name=OT-NPI
Cleaved into the following 2 chains:
    1- Recommended name:
            Oxytocin
        Alternative name(s):
            Ocytocin
    2- Recommended name:
            Neurophysin 1

Gene names

Name:

OXT

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	125 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	Neurophysin 1 specifically binds oxytocin. Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland.
Subcellular location	Secreted.
Sequence similarities	Belongs to the vasopressin/oxytocin family.
Sequence caution	The sequence CAA25194.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hormone
PTM	Amidation Cleavage on pair of basic residues
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	neurohypophyseal hormone activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Peptide

20 – 28

9

Oxytocin

PRO_0000020491

Chain

32 – 125

94

Neurophysin 1

PRO_0000020492

Amino acid modifications

Modified residue

28

1

Glycine amide

Disulfide bond

20 ↔ 25

Disulfide bond

41 ↔ 85

Disulfide bond

44 ↔ 58

Disulfide bond

52 ↔ 75

Disulfide bond

59 ↔ 65

Disulfide bond

92 ↔ 104

Disulfide bond

98 ↔ 116

Disulfide bond

105 ↔ 110

Experimental info

Sequence conflict

124

1

Q → L AA sequence Ref.9

Secondary structure

1

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125

Helix Strand Turn

Details...

Beta strand

36 – 38

3

Beta strand

43 – 45

3

Helix

46 – 48

3

Beta strand

50 – 54

5

Beta strand

57 – 60

4

Turn

61 – 63

3

Beta strand

64 – 69

6

Helix

70 – 80

11

Beta strand

89 – 92

4

Turn

93 – 95

3

Beta strand

96 – 100

5

Beta strand

103 – 106

4

Beta strand

109 – 112

4

Helix

114 – 116

3

Sequences

	Sequence		Length	Mass (Da)
	P01175-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 3B4E4E79A0B7F032	FASTA	125	12,665
	10 20 30 40 50 60 MAGSSLACCL LGLLALTSAC YIQNCPLGGK RAVLDLDVRT CLPCGPGGKG RCFGPSICCG 70 80 90 100 110 120 DELGCFVGTA EALRCQEENY LPSPCQSGQK PCGSGGRCAA AGICCSPDGC HEDPACDPEA AFSQH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deduced amino acid sequence from the bovine oxytocin-neurophysin I precursor cDNA." Land H., Grez M., Ruppert S., Schmale H., Rehbein M., Richter D., Schuetz G. Nature 302:342-344(1983) [PubMed: 6687626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Recent gene conversion involving bovine vasopressin and oxytocin precursor genes suggested by nucleotide sequence." Ruppert S., Scherer G., Schuetz G. Nature 308:554-557(1984) [PubMed: 6709064] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The neurohypophyseal hormones vasopressin and oxytocin. Precursor structure, synthesis and regulation." Rehbein M., Hillers M., Mohr E., Ivell R., Morley S., Schmale H., Richter D. Biol. Chem. Hoppe-Seyler 367:695-704(1986) [PubMed: 3768139] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Hypothalamus.
[5]	"The gene for the hypothalamic peptide hormone oxytocin is highly expressed in the bovine corpus luteum: biosynthesis, structure and sequence analysis." Ivell R., Richter D. EMBO J. 3:2351-2354(1984) [PubMed: 6209133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-125.
[6]	"The sequence of amino acids in oxytocin, with a proposal for the structure of oxytocin." du Vigneaud V., Ressler C., Trippett S. J. Biol. Chem. 205:949-957(1953) [PubMed: 13129273] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-28, DISULFIDE BONDS, AMIDATION AT GLY-28.
[7]	"About the chemical structure of oxytocin." Tuppy H., Michl H. Monatsh. Chem. 84:1011-1020(1953) Cited for: PROTEIN SEQUENCE OF 20-28.
[8]	"Complete amino acid sequence of bovine neurophysin-I. A major secretory product of the posterior pituitary." Schlesinger D.H., Audhya T.K., Walter R. J. Biol. Chem. 253:5019-5024(1978) [PubMed: 670174] [Abstract] Cited for: PROTEIN SEQUENCE OF 32-124.
[9]	"Comparison between MSEL- and VLDV-neurophysins. Complete amino acid sequences of porcine and bovine VLDV-neurophysins." Chauvet M.-T., Codogno P., Chauvet J., Acher R. FEBS Lett. 98:37-40(1979) [PubMed: 428540] [Abstract] Cited for: PROTEIN SEQUENCE OF 32-124.
[10]	"Complete assignment of neurophysin disulfides indicates pairing in two separate domains." Burman S., Wellner D., Chait B., Chaudhary T., Breslow E. Proc. Natl. Acad. Sci. U.S.A. 86:429-433(1989) [PubMed: 2911588] [Abstract] Cited for: DISULFIDE BONDS.
[11]	"Crystal structure analysis of deamino-oxytocin: conformational flexibility and receptor binding." Wood S.P., Tickle I.J., Treharne A.M., Pitts J.E., Mascarenhas Y., Li J.Y., Husain J., Cooper S., Blundell T.L., Hruby V.J. Science 232:633-636(1986) [PubMed: 3008332] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) OF OXYTOCIN, DISULFIDE BOND, AMIDATION AT GLY-28.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X00502 Genomic DNA. Translation: CAA25194.1. Sequence problems.
M25648 mRNA. Translation: AAA30680.1.
BC141997 mRNA. Translation: AAI41998.1.
V00114 mRNA. Translation: CAA23448.1.
V00114 mRNA. Translation: CAA23450.1. Different initiation.
V00114 mRNA. Translation: CAA23449.1. Sequence problems.
X00950 mRNA. Translation: CAA25462.1.

PIR

NFBO1. S07332.

RefSeq

NP_789825.1.

UniGene

Bt.183

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L5C	NMR	-	A	32-123	[»]
1L5D	NMR	-	A	32-123	[»]
1XY1	X-ray	1.04	A/B	21-28	[»]
1XY2	X-ray	1.20	A	21-28	[»]
2HNU	X-ray	2.00	A/B/C/D/E	38-118	[»]
2HNV	X-ray	2.50	A/B/C/D/E	38-118	[»]
2HNW	X-ray	2.90	A/B/C/D/E	38-117	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSBTAG00000008026. Bos taurus. [Contig view]

GeneID

280888.

KEGG

bta:280888.

Phylogenomic databases

HOVERGEN

P01175.

Family and domain databases

InterPro

IPR000981. Neurhyp_horm.
IPR016321. Nonapeptide_hormone_prcur.
[Graphical view]

Gene3D

G3DSA:2.60.9.10. Neurhyp_horm. 1 hit.

Pfam

PF00220. Hormone_4. 1 hit.
PF00184. Hormone_5. 1 hit.
[Graphical view]

PIRSF

PIRSF001815. Nonapeptide_hormone_precursor. 1 hit.

PRINTS

PR00831. NEUROPHYSIN.

ProDom

PD001676. Neurhyp_horm. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00003. NH. 1 hit.
[Graphical view]

PROSITE

PS00264. NEUROHYPOPHYS_HORM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P01175.

Entry information

Entry name

NEU1_BOVIN

Accession

Primary (citable) accession number: P01175
Secondary accession number(s): A5PJ78, P01188

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 1, 1988
Last modified:	November 25, 2008
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)