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Q8CJ52 (PROM2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Prominin-2

Short name=PROM-2
Alternative name(s):
Prominin-like protein 2
Short name=rPROML2
Testosterone-regulated prominin-related protein
Gene names
Name:Prom2
Synonyms:Proml2, Trprp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length834 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Binds to cholesterol. Ref.4

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein. Cell projectionmicrovillus membrane; Multi-pass membrane protein. Cell projectioncilium membrane; Multi-pass membrane protein. Note: Localizes to the apical and basolateral membranes of epithelial cells. Associates with membrane in a cholesterol-dependent manner. Colocalizes with PROM1. Ref.2 Ref.4

Tissue specificity

In the ventral prostate, expressed in glandular epithelial cells. Ref.1

Induction

Up-regulated by androgen. Ref.1

Post-translational modification

Glycosylated. Ref.4

Sequence similarities

Belongs to the prominin family.

Sequence caution

The sequence AAM03109.1 differs from that shown. Reason: Frameshift at position 775.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 834807Prominin-2
PRO_0000331241

Regions

Topological domain28 – 10679Extracellular Potential
Transmembrane107 – 12721Helical; Potential
Topological domain128 – 15326Cytoplasmic Potential
Transmembrane154 – 17421Helical; Potential
Topological domain175 – 434260Extracellular Potential
Transmembrane435 – 45521Helical; Potential
Topological domain456 – 47217Cytoplasmic Potential
Transmembrane473 – 49321Helical; Potential
Topological domain494 – 779286Extracellular Potential
Transmembrane780 – 80021Helical; Potential
Topological domain801 – 83434Cytoplasmic Potential
Coiled coil637 – 67438 Potential

Amino acid modifications

Glycosylation2701N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2171S → L in AAM03109. Ref.1
Sequence conflict5341L → I in AAM03109. Ref.1
Sequence conflict5801E → K in AAM03109. Ref.1
Sequence conflict6491Q → H in AAM03109. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8CJ52 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: CE1A53DB5CBEF57A

FASTA83492,841
        10         20         30         40         50         60 
MTRTLDLMVP LLGLSLGLAL SLPRAVAADC GSLGRVEHLA FAPVPGTEPT APRVRAPWPL 

        70         80         90        100        110        120 
DSLYGTVRRF LSVVQLNPFP AELIKTLLND PSSVKTDEVV RYEAGYVVCA VIAGLYLLLV 

       130        140        150        160        170        180 
PITGLCFCCC RCRRRCGGRV KTEHKAMACE RGTLMTFLLL TTLMLLIGMV CAFATNQFTH 

       190        200        210        220        230        240 
SQTGPSVEAV PETLLSLRGL VSDVPKKLQA VADQFSSPQK QVSKDLDGVG ENLGNIIHNQ 

       250        260        270        280        290        300 
LKSTVYPVLA SVHGLGQALQ VSIDHLQSVN ATSVELREGQ QHLGPPVQAH RERLLALLQE 

       310        320        330        340        350        360 
SWCHENCKGA LSQASALQLG ADFSQMPPVD DVLHRLQGVP EANFSSMVQE ENATFNNLPI 

       370        380        390        400        410        420 
LVHMQMVSVV KDLKKALAEQ PEGVRMLAQA FPGSEATSRW SQALEGLEQR SRPYLQDVQR 

       430        440        450        460        470        480 
YETYRWILGC VLCSAILLVV ICNLLGLSLG IWGLFAREDP SHSETKGEAG ARFLMAGVAF 

       490        500        510        520        530        540 
SFLFAAPLIL LVFATFLVGG NVQTLVCRSW ESGELYEFVD TPGNLPPSMN LSYLLGLRKN 

       550        560        570        580        590        600 
ISVFQAYRQC KAGTALWKVL QLNDSYDLDK HLDIKQYTHE LQQELQSFKV DLKDLDLLNP 

       610        620        630        640        650        660 
AARQNLEALQ SSGLEKIHYR DFLVQIQKPV VKTDMGQLAK ELEGLAQAQN ESLRRQQLQE 

       670        680        690        700        710        720 
EARELRSLYQ EKVVPQENLV AKLNPSIRVL ESSAPKLQVN TSDLLDIVAR LKGELPAQLN 

       730        740        750        760        770        780 
HILRNATECF LTREMGYFSQ YVTWVREEVT QHIATCQPFS KALDDGHMIL CDMMANPWNA 

       790        800        810        820        830 
FWFCLGWCTF FLIPSIIFAV KTSKYFRPIR KRLSSTSSEE TQLFHIPRVT SLKL 

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References

[1]"Identification and characterization of a novel testosterone-regulated prominin-like gene in the rat ventral prostate."
Zhang Q., Haleem R., Cai X., Wang Z.
Endocrinology 143:4788-4796(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
[2]"Characterization of prominin-2, a new member of the prominin family of pentaspan membrane glycoproteins."
Fargeas C.A., Florek M., Huttner W.B., Corbeil D.
J. Biol. Chem. 278:8586-8596(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Strain: Sprague-Dawley.
Tissue: Kidney.
[3]"AC133 antigen, CD133, prominin-1, prominin-2, etc.: prominin family gene products in need of a rational nomenclature."
Fargeas C.A., Corbeil D., Huttner W.B.
Stem Cells 21:506-508(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Kidney.
[4]"Prominin-2 is a cholesterol-binding protein associated with apical and basolateral plasmalemmal protrusions in polarized epithelial cells and released into urine."
Florek M., Bauer N., Janich P., Wilsch-Braeuninger M., Fargeas C.A., Marzesco A.-M., Ehninger G., Thiele C., Huttner W.B., Corbeil D.
Cell Tissue Res. 328:31-47(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHOLESTEROL, GLYCOSYLATION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF486828 mRNA. Translation: AAM03109.1. Frameshift.
AF508942 mRNA. Translation: AAN63818.1.
RefSeqNP_620212.1. NM_138857.1.
UniGeneRn.82155.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000020354.

Proteomic databases

PaxDbQ8CJ52.
PRIDEQ8CJ52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID192211.
KEGGrno:192211.
UCSCRGD:621435. rat.

Organism-specific databases

CTD150696.
RGD621435. Prom2.

Phylogenomic databases

eggNOGNOG322325.
HOGENOMHOG000115705.
HOVERGENHBG101108.
InParanoidQ8CJ52.
KOK15602.
PhylomeDBQ8CJ52.

Gene expression databases

GenevestigatorQ8CJ52.

Family and domain databases

InterProIPR008795. Prominin.
[Graphical view]
PANTHERPTHR22730. PTHR22730. 1 hit.
PfamPF05478. Prominin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio622797.
PROQ8CJ52.

Entry information

Entry namePROM2_RAT
AccessionPrimary (citable) accession number: Q8CJ52
Secondary accession number(s): Q8R4B6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families