Reviewed, UniProtKB/Swiss-Prot P62825 (RAN_CANFA)

Names and origin

Protein names

Recommended name:
    GTP-binding nuclear protein Ran
Alternative name(s):
    GTPase Ran
    Ras-related nuclear protein
    Ras-like protein TC4

Gene names

Name:

RAN

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	216 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	GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle. The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules By similarity.
Subunit structure	Monomer. Also forms a complex with CHC1. Found in a complex with nuclear export signal-cargo peptides, RANBP3 and XPO1. Component of a nuclear export receptor complex composed of KPNB1, Ran, SNUPN and XPO1. Found in a trimeric export complex with SNUPN, Ran and XPO1. Interacts with RANBP10. Interacts in its GTP-bound form with BIRC5/survivin at S and M phases of the cell cycle By similarity.
Subcellular location	Nucleus. Cytoplasm. Melanosome By similarity. Note: Becomes dispersed throughout the cytoplasm during mitosis.
Sequence similarities	Belongs to the small GTPase superfamily. Ran family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Protein transport Transport
Cellular component	Cytoplasm Nucleus
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW intracellular protein transport Inferred from electronic annotation. Source: InterPro mitosis Inferred from electronic annotation. Source: UniProtKB-KW nucleocytoplasmic transport Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase 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

Initiator methionine

1

1

Removed By similarity

Chain

2 – 216

215

GTP-binding nuclear protein Ran

PRO_0000208695

Regions

Nucleotide binding

17 – 24

8

GTP By similarity

Nucleotide binding

65 – 69

5

GTP By similarity

Nucleotide binding

122 – 125

4

GTP By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

60

1

N6-acetyllysine By similarity

Modified residue

71

1

N6-acetyllysine By similarity

Modified residue

99

1

N6-acetyllysine By similarity

Modified residue

147

1

Phosphotyrosine By similarity

Modified residue

155

1

Phosphotyrosine By similarity

Modified residue

159

1

N6-acetyllysine By similarity

Cross-link

71

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

1

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216

Helix Strand Turn

Details...

Turn

3 – 5

3

Beta strand

10 – 17

8

Helix

23 – 27

5

Helix

31 – 35

5

Beta strand

38 – 40

3

Turn

41 – 44

4

Beta strand

45 – 54

10

Beta strand

57 – 66

10

Helix

69 – 71

3

Helix

77 – 80

4

Beta strand

84 – 91

8

Helix

95 – 99

5

Helix

101 – 112

12

Beta strand

117 – 122

6

Beta strand

126 – 128

3

Helix

133 – 136

4

Helix

137 – 141

5

Beta strand

145 – 148

4

Helix

151 – 153

3

Turn

156 – 158

3

Helix

159 – 169

11

Beta strand

176 – 178

3

Helix

191 – 205

15

Sequences

	Sequence		Length	Mass (Da)
	P62825-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D5C9B7275C34BCE0	FASTA	216	24,423
	10 20 30 40 50 60 MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK 70 80 90 100 110 120 FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC 130 140 150 160 170 180 GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP 190 200 210 ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL

References

[1]	"Sequence of a canine cDNA clone encoding a Ran/TC4 GTP-binding protein." Dupree P., Olkkonen V.M., Chavrier P. Gene 120:325-326(1992) [PubMed: 1398150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Cocker spaniel. Tissue: Kidney.
[2]	"Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran." Stewart M., Kent H.M., McCoy A.J. J. Mol. Biol. 277:635-646(1998) [PubMed: 9533885] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH NTF2.
[3]	"The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2)." Stewart M., Kent H.M., McCoy A.J. J. Mol. Biol. 284:1517-1527(1998) [PubMed: 9878368] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF MUTANT LEU-69.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z11922 mRNA. Translation: CAA77980.1.

PIR

JC1455.

RefSeq

NP_001003375.1.

UniGene

Cfa.50

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A2K	X-ray	2.50	C/D/E	1-216	[»]
1BYU	X-ray	2.15	A/B	1-216	[»]
1QG2	X-ray	2.50	A	1-216	[»]
1QG4	X-ray	2.50	A/B	1-216	[»]
1WA5	X-ray	2.00	A	1-176	[»]
2BKU	X-ray	2.70	A/C	1-177	[»]
3RAN	X-ray	2.15	A/B/C/D	1-216	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSCAFT00000010749; ENSCAFP00000009963; ENSCAFG00000006670; Canis familiaris. [Genome view]

GeneID

442976.

KEGG

cfa:442976.

Organism-specific databases

CTD

442976.

Phylogenomic databases

HOVERGEN

P62825.

InParanoid

P62825.

Family and domain databases

InterPro

IPR002041. Ran_GTPase.
IPR013753. Ras.
IPR005225. Small_GTP_bd.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00627. GTPRANTC4.

SMART

SM00176. RAN. 1 hit.
[Graphical view]

PROSITE

PS51418. RAN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RAN_CANFA

Accession

Primary (citable) accession number: P62825
Secondary accession number(s): P17080 , P28746, P28747, Q9CSP3, Q9CWI7, Q9CZA2, Q9UDJ5, Q9UEU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	December 15, 2009
This is version 59 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)