Reviewed, UniProtKB/Swiss-Prot O43490 (PROM1_HUMAN)

Names and origin

Protein names

Recommended name:
    Prominin-1
Alternative name(s):
    Prominin-like protein 1
    Antigen AC133
    CD_antigen=CD133

Gene names

Name:	PROM1
Synonyms:	PROML1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	865 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)

Subunit structure	Interacts with PCDH21 and with actin filaments.
Subcellular location	Apical cell membrane; Multi-pass membrane protein By similarity. Cell projection › microvillus membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Selectively expressed on CD34 hematopoietic stem and progenitor cells in adult and fetal bone marrow, fetal liver, cord blood and adult peripheral blood. Not detected on other blood cells. Also expressed in a number of non-lymphoid tissues including retina, pancreas, placenta, kidney, liver, lung, brain and heart. Found in saliva within small membrane particles. Ref.4
Post-translational modification	Glycosylated.
Involvement in disease	Defects in PROM1 are the cause of retinitis pigmentosa type 41 (RP41) [MIM:612095]; also known as retinal degeneration autosomal recessive prominin-related. RP is a retinal dystrophy belonging to the group of pigmentary retinopathies. RP is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Ref.5 Ref.6 Defects in PROM1 are the cause of cone-rod dystrophy type 12 (CORD12) [MIM:612657]. CORD12 is an inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. Defects in PROM1 are the cause of Stargardt disease type 4 (STGD4) [MIM:603786]. Stargardt disease is the most common hereditary macular degeneration. It is characterized by decreased central vision, atrophy of the macula and underlying retinal pigment epithelium, and frequent presence of prominent flecks in the posterior pole of the retina. Defects in PROM1 are the cause of retinal macular dystrophy type 2 (MCDR2) [MIM:608051]. MCDR2 is a bull's-eye macular dystrophy characterized by bilateral annular atrophy of retinal pigment epithelium at the macula.
Sequence similarities	Belongs to the prominin family.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Cell membrane Cell projection Membrane
Coding sequence diversity	Polymorphism
Disease	Cone-rod dystrophy Disease mutation Retinitis pigmentosa Stargardt disease
Domain	Signal Transmembrane
PTM	Glycoprotein Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apical plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell surface Inferred from direct assay. Source: UniProtKB integral to plasma membrane Ref.2 Traceable author statement. Source: ProtInc microvillus membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 865	846	Prominin-1		PRO_0000025813
Regions
	Topological domain	20 – 108	89	Extracellular Potential
	Transmembrane	109 – 129	21	Potential
	Topological domain	130 – 157	28	Cytoplasmic Potential
	Transmembrane	158 – 178	21	Potential
	Topological domain	179 – 433	255	Extracellular Potential
	Transmembrane	434 – 454	21	Potential
	Topological domain	455 – 486	32	Cytoplasmic Potential
	Transmembrane	487 – 507	21	Potential
	Topological domain	508 – 792	285	Extracellular Potential
	Transmembrane	793 – 813	21	Potential
	Topological domain	814 – 865	52	Cytoplasmic Potential
Amino acid modifications
	Modified residue	266	1	Phosphothreonine Ref.3
	Modified residue	275	1	Phosphoserine Ref.3
	Modified residue	276	1	Phosphothreonine Ref.3
	Glycosylation	220	1	N-linked (GlcNAc...) Potential
	Glycosylation	274	1	N-linked (GlcNAc...) Potential
	Glycosylation	395	1	N-linked (GlcNAc...) Potential
	Glycosylation	414	1	N-linked (GlcNAc...) Potential
	Glycosylation	548	1	N-linked (GlcNAc...) Potential
	Glycosylation	580	1	N-linked (GlcNAc...) Potential
	Glycosylation	729	1	N-linked (GlcNAc...) Potential
	Glycosylation	730	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	31	1	A → G		VAR_010382
	Natural variant	31	1	A → S		VAR_010383
	Natural variant	373	1	R → C in CORD12, STGD4 and MCDR2; affects the interaction with PCDH21 and actin.		VAR_057961
Experimental info
	Sequence conflict	200	1	D → A AA sequence Ref.1
	Sequence conflict	200	1	D → P AA sequence Ref.1
	Sequence conflict	284	1	S → D AA sequence Ref.1
	Sequence conflict	288	1	S → R AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O43490-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: D21CBC05ADB2DEDF	FASTA	865	97,202
	10 20 30 40 50 60 MALVLGSLLL LGLCGNSFSG GQPSSTDAPK AWNYELPATN YETQDSHKAG PIGILFELVH 70 80 90 100 110 120 IFLYVVQPRD FPEDTLRKFL QKAYESKIDY DKPETVILGL KIVYYEAGII LCCVLGLLFI 130 140 150 160 170 180 ILMPLVGYFF CMCRCCNKCG GEMHQRQKEN GPFLRKCFAI SLLVICIIIS IGIFYGFVAN 190 200 210 220 230 240 HQVRTRIKRS RKLADSNFKD LRTLLNETPE QIKYILAQYN TTKDKAFTDL NSINSVLGGG 250 260 270 280 290 300 ILDRLRPNII PVLDEIKSMA TAIKETKEAL ENMNSTLKSL HQQSTQLSSS LTSVKTSLRS 310 320 330 340 350 360 SLNDPLCLVH PSSETCNSIR LSLSQLNSNP ELRQLPPVDA ELDNVNNVLR TDLDGLVQQG 370 380 390 400 410 420 YQSLNDIPDR VQRQTTTVVA GIKRVLNSIG SDIDNVTQRL PIQDILSAFS VYVNNTESYI 430 440 450 460 470 480 HRNLPTLEEY DSYWWLGGLV ICSLLTLIVI FYYLGLLCGV CGYDRHATPT TRGCVSNTGG 490 500 510 520 530 540 VFLMVGVGLS FLFCWILMII VVLTFVFGAN VEKLICEPYT SKELFRVLDT PYLLNEDWEY 550 560 570 580 590 600 YLSGKLFNKS KMKLTFEQVY SDCKKNRGTY GTLHLQNSFN ISEHLNINEH TGSISSELES 610 620 630 640 650 660 LKVNLNIFLL GAAGRKNLQD FAACGIDRMN YDSYLAQTGK SPAGVNLLSF AYDLEAKANS 670 680 690 700 710 720 LPPGNLRNSL KRDAQTIKTI HQQRVLPIEQ SLSTLYQSVK ILQRTGNGLL ERVTRILASL 730 740 750 760 770 780 DFAQNFITNN TSSVIIEETK KYGRTIIGYF EHYLQWIEFS ISEKVASCKP VATALDTAVD 790 800 810 820 830 840 VFLCSYIIDP LNLFWFGIGK ATVFLLPALI FAVKLAKYYR RMDSEDVYDD VETIPMKNME 850 860 NGNNGYHKDH VYGIHNPVMT SPSQH

References

	« Hide 'large scale' referencesShow '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: 9389721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-42; 200-211; 280-291 AND 641-656. Tissue: Fetal liver and Retinoblastoma.
[2]	"AC133, a novel marker for human hematopoietic stem and progenitor cells." Yin A.H., Miraglia S., Zanjani E.D., Almeida-Porada G., Ogawa M., Leary A.G., Olweus J., Kearney J., Buck D.W. Blood 90:5002-5012(1997) [PubMed: 9389720] [Abstract] Cited for: CHARACTERIZATION. Tissue: Fetal liver.
[3]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266; SER-275 AND THR-276, MASS SPECTROMETRY. Tissue: Epithelium.
[4]	"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: 17874118] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"A frameshift mutation in prominin (mouse)-like 1 causes human retinal degeneration." Maw M.A., Corbeil D., Koch J., Hellwig A., Wilson-Wheeler J.C., Bridges R.J., Kumaramanickavel G., John S., Nancarrow D., Roeper K., Weigmann A., Huttner W.B., Denton M.J. Hum. Mol. Genet. 9:27-34(2000) [PubMed: 10587575] [Abstract] Cited for: INVOLVEMENT IN RP41.
[6]	"Severe retinitis pigmentosa mapped to 4p15 and associated with a novel mutation in the PROM1 gene." Zhang Q., Zulfiqar F., Xiao X., Riazuddin S.A., Ahmad Z., Caruso R., MacDonald I., Sieving P., Riazuddin S., Hejtmancik J.F. Hum. Genet. 122:293-299(2007) [PubMed: 17605048] [Abstract] Cited for: INVOLVEMENT IN RP41.
[7]	"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. , 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: 18654668] [Abstract] Cited for: VARIANT CORD12/STGD4/MCDR2 CYS-373, INTERACTION WITH PCDH21 AND ACTIN, CHARACTERIZATION OF VARIANT CORD12/STGD4/MCDR2 CYS-373.
+	Additional computationally mapped references.

Web resources

Mutations of the PROM1 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF027208 mRNA. Translation: AAB92514.1.
IPI	IPI00012540.
PIR	T09050.
RefSeq	NP_006008.1.
UniGene	Hs.614734
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	O43490.
Proteomic databases
PRIDE	O43490.
Genome annotation databases
Ensembl	ENSG00000007062. Homo sapiens. [Contig view]
GeneID	8842.
KEGG	hsa:8842.
Organism-specific databases
GeneCards	GC04M015578.
H-InvDB	HIX0004116.
HGNC	HGNC:9454. PROM1.
HPA	CAB011525.
MIM	603786. phenotype. 604365. gene. 608051. phenotype. 612095. phenotype. 612657. phenotype.
Orphanet	791. Retinitis pigmentosa. 827. Stargardt disease.
PharmGKB	PA33807.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O43490.
HOVERGEN	O43490.
Gene expression databases
CleanEx	HS_PROM1.
GermOnline	ENSG00000007062. Homo sapiens.
Family and domain databases
InterPro	IPR008795. Prominin. [Graphical view]
PANTHER	PTHR22730. Prominin. 1 hit.
Pfam	PF05478. Prominin. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	33194.
SOURCE	Search...

Entry information

Entry name

PROM1_HUMAN

Accession

Primary (citable) accession number: O43490

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	June 1, 1998
Last modified:	June 16, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)