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O54990 (PROM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prominin-1
Alternative name(s):
Antigen AC133 homolog
Prominin-like protein 1
CD_antigen=CD133
Gene names
Name:Prom1
Synonyms:Prom, Proml1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length867 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds cholesterol in cholesterol-containing plasma membrane microdomains. Proposed to play a role in apical plasma membrane organization of epithelial cells. During early during retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner By similarity. Ref.12

Subunit structure

Interacts with CDHR1 and with actin filaments By similarity.

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Cell projectionmicrovillus membrane; Multi-pass membrane protein. Cell projectionciliumphotoreceptor outer segment. Note: Found in extracellular membrane particles in various body fluids such as ventricular fluid of the developing brain and urine. Ref.5 Ref.6 Ref.8 Ref.10

Tissue specificity

In the submandibular gland, expressed on the apical side of epithelial cells. In the parotid gland, expressed in the intercalated ducts. In the sublingual gland, expressed in intercalated ducts. In the extraorbital lacrimal gland, expressed in the intercalated tubules and larger intralobular ducts. Expressed in the retina. Present in urine within small membrane particles (at protein level). In the embryo, expressed on the apical side of neuroepithelial cells and of other epithelia such as lung buds, gut and ureter buds. In the adult, expressed at the apical side of the kidney tubules and of the ependymal layer of the brain. Not expressed in gut, liver, lung, pituitary, adrenal, heart or spleen. Localized to the nascent disk membranes at the base of the rod outer segment in the retina (at protein level). Ref.6 Ref.9 Ref.11 Ref.12

Developmental stage

At birth, is detected at the interface between the developing neuroretina and the retinal pigment epithelium (RPE) layer. In the postnatal retina (P20) detected in photoreceptors, with particular concentration in the region of plasma membrane evaginations at the basal part of the outer segment (OS). Expressed by rod and cone photoreceptor cells, most abundantly between the OS and inner segment (IS), in close proximity to the connecting cilium. Ref.12

Disruption phenotype

Progressive degeneration and functional deterioration of both cone and rod photoreceptors associated with impaired morphogenesis of the disks and OS. Ref.12

Miscellaneous

Fundus images and light microscopy of retinal sections from transgenic mice expressing mutant PROM1 reveal progressive retinal abnormalities visible as subretinal deposits and photoreceptor atrophy.

Sequence similarities

Belongs to the prominin family.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O54990-1)

Also known as: S2;

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.
Isoform 2 (identifier: O54990-2)

Also known as: S1;

The sequence of this isoform differs from the canonical sequence as follows:
     94-102: Missing.
Isoform 3 (identifier: O54990-3)

Also known as: S3;

The sequence of this isoform differs from the canonical sequence as follows:
     94-102: Missing.
     833-843: VETVPMKNLEI → SSVSGMWHFTL
     844-867: Missing.
Isoform 4 (identifier: O54990-4)

Also known as: S4;

The sequence of this isoform differs from the canonical sequence as follows:
     94-107: Missing.
     335-360: QLPSVDRELNTVTEVDKTDLESLVKR → Q
     833-843: VETVPMKNLEI → SSVSGMWHFTL
     844-867: Missing.
Isoform 5 (identifier: O54990-5)

Also known as: S5;

The sequence of this isoform differs from the canonical sequence as follows:
     94-102: Missing.
     335-360: QLPSVDRELNTVTEVDKTDLESLVKR → Q
     833-843: VETVPMKNLEI → SSVSGMWHFTL
     844-867: Missing.
Isoform 6 (identifier: O54990-6)

Also known as: S6;

The sequence of this isoform differs from the canonical sequence as follows:
     94-102: Missing.
     832-832: D → E
     833-867: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 867848Prominin-1
PRO_0000025814

Regions

Topological domain20 – 10788Extracellular Potential
Transmembrane108 – 12821Helical; Potential
Topological domain129 – 15830Cytoplasmic Potential
Transmembrane159 – 17921Helical; Potential
Topological domain180 – 434255Extracellular Potential
Transmembrane435 – 45521Helical; Potential
Topological domain456 – 48732Cytoplasmic Potential
Transmembrane488 – 50821Helical; Potential
Topological domain509 – 794286Extracellular Potential
Transmembrane795 – 81521Helical; Potential
Topological domain816 – 86752Cytoplasmic Potential

Amino acid modifications

Modified residue8651Phosphoserine By similarity
Glycosylation2731N-linked (GlcNAc...) Ref.13
Glycosylation2911N-linked (GlcNAc...) Ref.13
Glycosylation3321N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Ref.13
Glycosylation4151N-linked (GlcNAc...) Potential
Glycosylation5541N-linked (GlcNAc...) Potential
Glycosylation5811N-linked (GlcNAc...) Potential
Glycosylation7321N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence94 – 10714Missing in isoform 4.
VSP_040005
Alternative sequence94 – 1029Missing in isoform 2, isoform 3, isoform 5 and isoform 6.
VSP_040006
Alternative sequence335 – 36026QLPSV…SLVKR → Q in isoform 4 and isoform 5.
VSP_040007
Alternative sequence8321D → E in isoform 6.
VSP_040008
Alternative sequence833 – 86735Missing in isoform 6.
VSP_040009
Alternative sequence833 – 84311VETVPMKNLEI → SSVSGMWHFTL in isoform 3, isoform 4 and isoform 5.
VSP_040010
Alternative sequence844 – 86724Missing in isoform 3, isoform 4 and isoform 5.
VSP_040011

Experimental info

Sequence conflict641S → N in AAB86715. Ref.2
Sequence conflict641S → N in AAM28245. Ref.3
Sequence conflict641S → N in AAO11840. Ref.3
Sequence conflict641S → N in AAO72429. Ref.3
Sequence conflict641S → N in AAO72430. Ref.3
Sequence conflict641S → N in BAC26745. Ref.4
Sequence conflict841K → N in AAB86715. Ref.2
Sequence conflict841K → N in AAM28245. Ref.3
Sequence conflict841K → N in AAO11840. Ref.3
Sequence conflict841K → N in AAO72429. Ref.3
Sequence conflict841K → N in AAO72430. Ref.3
Sequence conflict841K → N in BAC26745. Ref.4
Sequence conflict6681P → L in AAB86715. Ref.2
Sequence conflict6681P → L in AAM28245. Ref.3
Sequence conflict6681P → L in AAO72429. Ref.3
Sequence conflict6681P → L in AAO72430. Ref.3
Sequence conflict6681P → L in BAC26745. Ref.4
Sequence conflict8441G → D in AAB86715. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (S2) [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: D442F6372552B3C8

FASTA86797,113
        10         20         30         40         50         60 
MALVFSALLL LGLCGKISSE GQPAFHNTPG AMNYELPTTK YETQDTFNAG IVGPLYKMVH 

        70         80         90        100        110        120 
IFLSVVQPND FPLDLIKKLI QNKKFDISVD SKEPEIIVLA LKIALYEIGV LICAILGLLF 

       130        140        150        160        170        180 
IILMPLVGCF FCMCRCCNKC GGEMHQRQKQ NAPCRRKCLG LSLLVICLLM SLGIIYGFVA 

       190        200        210        220        230        240 
NQQTRTRIKG TQKLAKSNFR DFQTLLTETP KQIDYVVEQY TNTKNKAFSD LDGIGSVLGG 

       250        260        270        280        290        300 
RIKDQLKPKV TPVLEEIKAM ATAIKQTKDA LQNMSSSLKS LQDAATQLNT NLSSVRNSIE 

       310        320        330        340        350        360 
NSLSSSDCTS DPASKICDSI RPSLSSLGSS LNSSQLPSVD RELNTVTEVD KTDLESLVKR 

       370        380        390        400        410        420 
GYTTIDEIPN TIQNQTVDVI KDVKNTLDSI SSNIKDMSQS IPIEDMLLQV SHYLNNSNRY 

       430        440        450        460        470        480 
LNQELPKLEE YDSYWWLGGL IVCFLLTLIV TFFFLGLLCG VFGYDKHATP TRRGCVSNTG 

       490        500        510        520        530        540 
GIFLMAGVGF GFLFCWILMI LVVLTFVVGA NVEKLLCEPY ENKKLLQVLD TPYLLKEQWQ 

       550        560        570        580        590        600 
FYLSGMLFNN PDINMTFEQV YRDCKRGRGI YAAFQLENVV NVSDHFNIDQ ISENINTELE 

       610        620        630        640        650        660 
NLNVNIDSIE LLDNTGRKSL EDFAHSGIDT IDYSTYLKET EKSPTEVNLL TFASTLEAKA 

       670        680        690        700        710        720 
NQLPEGKPKQ AFLLDVQNIR AIHQHLLPPV QQSLNTLRQS VWTLQQTSNK LPEKVKKILA 

       730        740        750        760        770        780 
SLDSVQHFLT NNVSLIVIGE TKKFGKTILG YFEHYLHWVF YAITEKMTSC KPMATAMDSA 

       790        800        810        820        830        840 
VNGILCGYVA DPLNLFWFGI GKATVLLLPA VIIAIKLAKY YRRMDSEDVY DDVETVPMKN 

       850        860 
LEIGSNGYHK DHLYGVHNPV MTSPSRY 

« Hide

Isoform 2 (S1) [UniParc].

Checksum: CAFCAD4C3039848D
Show »

FASTA85896,136
Isoform 3 (S3) [UniParc].

Checksum: CAFC85B2596BAB9C
Show »

FASTA83493,416
Isoform 4 (S4) [UniParc].

Checksum: A8C6925524AE94D5
Show »

FASTA80489,987
Isoform 5 (S5) [UniParc].

Checksum: 1FF6FB4EF6CB7095
Show »

FASTA80990,577
Isoform 6 (S6) [UniParc].

Checksum: E8425D90B970938A
Show »

FASTA82392,197

References

« Hide 'large scale' references
[1]"A novel five-transmembrane hematopoietic stem cell antigen: isolation, characterization, and molecular cloning."
Miraglia S., Godfrey W., Yin A.H., Atkins K., Warnke R., Holden J.T., Bray R.A., Waller E.K., Buck D.W.
Blood 90:5013-5021(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Prominin, a novel microvilli-specific polytopic membrane protein of the apical surface of epithelial cells, is targeted to plasmalemmal protrusions of non-epithelial cells."
Weigmann A., Corbeil D., Hellwig A., Huttner W.B.
Proc. Natl. Acad. Sci. U.S.A. 94:12425-12430(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Kidney.
[3]"Identification of novel Prominin-1/CD133 splice variants with alternative C-termini and their expression in epididymis and testis."
Fargeas C.A., Joester A., Missol-Kolka E., Hellwig A., Huttner W.B., Corbeil D.
J. Cell Sci. 117:4301-4311(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5 AND 6).
Strain: BALB/c.
Tissue: Testis.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Strain: C57BL/6J.
Tissue: Testis.
[5]"Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane."
Roeper K., Corbeil D., Huttner W.B.
Nat. Cell Biol. 2:582-592(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CHOLESTEROL BINDING.
[6]"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: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[7]"Nomenclature of prominin-1 (CD133) splice variants - an update."
Fargeas C.A., Huttner W.B., Corbeil D.
Tissue Antigens 69:602-606(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE OF ISOFORMS.
[8]"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: SUBCELLULAR LOCATION.
[9]"Differential expression of prominin-1 (CD133) and prominin-2 in major cephalic exocrine glands of adult mice."
Jaszai J., Janich P., Farkas L.M., Fargeas C.A., Huttner W.B., Corbeil D.
Histochem. Cell Biol. 128:409-419(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Midbody and primary cilium of neural progenitors release extracellular membrane particles enriched in the stem cell marker prominin-1."
Dubreuil V., Marzesco A.M., Corbeil D., Huttner W.B., Wilsch-Braeuninger M.
J. Cell Biol. 176:483-495(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Mutant prominin 1 found in patients with macular degeneration disrupts photoreceptor disk morphogenesis in mice."
Yang Z., Chen Y., Lillo C., Chien J., Yu Z., Michaelides M., Klein M., Howes K.A., Li Y., Kaminoh Y., Chen H., Zhao C., Chen Y., Al-Sheikh Y.T., Karan G., Corbeil D., Escher P., Kamaya S. expand/collapse author list , Li C., Johnson S., Frederick J.M., Zhao Y., Wang C., Cameron D.J., Huttner W.B., Schorderet D.F., Munier F.L., Moore A.T., Birch D.G., Baehr W., Hunt D.M., Williams D.S., Zhang K.
J. Clin. Invest. 118:2908-2916(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"Loss of the cholesterol-binding protein prominin-1/CD133 causes disk dysmorphogenesis and photoreceptor degeneration."
Zacchigna S., Oh H., Wilsch-Brauninger M., Missol-Kolka E., Jaszai J., Jansen S., Tanimoto N., Tonagel F., Seeliger M., Huttner W.B., Corbeil D., Dewerchin M., Vinckier S., Moons L., Carmeliet P.
J. Neurosci. 29:2297-2308(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[13]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-273; ASN-291 AND ASN-374.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039663 mRNA. Translation: AAB96916.1.
AF026269 mRNA. Translation: AAB86715.1.
AF305215 mRNA. Translation: AAO11840.1.
AY099088 mRNA. Translation: AAM28245.1.
AY223521 mRNA. Translation: AAO72429.1.
AY223522 mRNA. Translation: AAO72430.1.
AK030027 mRNA. Translation: BAC26745.1.
CCDSCCDS39082.1. [O54990-2]
CCDS51491.1. [O54990-5]
CCDS51493.1. [O54990-3]
CCDS51494.1. [O54990-1]
PIRT08881.
RefSeqNP_001157050.1. NM_001163578.1.
NP_001157053.1. NM_001163581.1.
NP_001157054.1. NM_001163582.1.
NP_001157055.1. NM_001163583.1.
UniGeneMm.6250.

3D structure databases

ProteinModelPortalO54990.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202393. 1 interaction.
IntActO54990. 1 interaction.
MINTMINT-4108629.
STRING10090.ENSMUSP00000073751.

PTM databases

PhosphoSiteO54990.

Proteomic databases

MaxQBO54990.
PaxDbO54990.
PRIDEO54990.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030973; ENSMUSP00000030973; ENSMUSG00000029086.
ENSMUST00000087442; ENSMUSP00000084709; ENSMUSG00000029086.
GeneID19126.
KEGGmmu:19126.
UCSCuc008xii.1. mouse. [O54990-4]

Organism-specific databases

CTD8842.
MGIMGI:1100886. Prom1.

Phylogenomic databases

eggNOGNOG322325.
GeneTreeENSGT00530000063586.
HOGENOMHOG000115704.
HOVERGENHBG053690.
InParanoidO54990.
KOK06532.
OrthoDBEOG7TQV02.
PhylomeDBO54990.

Gene expression databases

ArrayExpressO54990.
BgeeO54990.
CleanExMM_PROM1.
GenevestigatorO54990.

Family and domain databases

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

Other

NextBio295734.
PROO54990.
SOURCESearch...

Entry information

Entry namePROM1_MOUSE
AccessionPrimary (citable) accession number: O54990
Secondary accession number(s): O35408 expand/collapse secondary AC list , Q80XB2, Q80XB3, Q80XB6, Q8BH12
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 108 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot