ID PROM1_HUMAN Reviewed; 865 AA. AC O43490; Q6SV49; Q6SV50; Q6SV51; Q6SV52; Q6SV53; Q96EN6; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 198. DE RecName: Full=Prominin-1; DE AltName: Full=Antigen AC133; DE AltName: Full=Prominin-like protein 1; DE AltName: CD_antigen=CD133; DE Flags: Precursor; GN Name=PROM1; Synonyms=PROML1; ORFNames=MSTP061; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 31-42; RP 200-211; 280-291 AND 641-656. RC TISSUE=Fetal liver, and Retinoblastoma; RX PubMed=9389721; RA Miraglia S., Godfrey W., Yin A.H., Atkins K., Warnke R., Holden J.T., RA Bray R.A., Waller E.K., Buck D.W.; RT "A novel five-transmembrane hematopoietic stem cell antigen: isolation, RT characterization, and molecular cloning."; RL Blood 90:5013-5021(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND GLYCOSYLATION. RX PubMed=12042327; DOI=10.1074/jbc.m202349200; RA Yu Y., Flint A., Dvorin E.L., Bischoff J.; RT "AC133-2, a novel isoform of human AC133 stem cell antigen."; RL J. Biol. Chem. 277:20711-20716(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Lin J., Shmelkov S.V., Karajannis M.A., StClair R., Walsh K., Gordon R., RA Shido K., Lam G., Moussazadeh N., Shim W., Rafii S.; RT "Identification and functional analysis of several isoforms of hematopoitic RT stem cell surface maker prominin-1 (AC133)."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Aorta; RA Wang X.Y., Zhao B., Liu B., Xu Y.Y., Liu Y.Q., Cao H.Q., Sheng H., Ye J., RA Song L., Wei Y.J., Liu S., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP CHARACTERIZATION. RC TISSUE=Fetal liver; RX PubMed=9389720; RA Yin A.H., Miraglia S., Zanjani E.D., Almeida-Porada G., Ogawa M., RA Leary A.G., Olweus J., Kearney J., Buck D.W.; RT "AC133, a novel marker for human hematopoietic stem and progenitor cells."; RL Blood 90:5002-5012(1997). RN [10] RP TISSUE SPECIFICITY. RX PubMed=17874118; DOI=10.1007/s00418-007-0334-2; RA Jaszai J., Janich P., Farkas L.M., Fargeas C.A., Huttner W.B., Corbeil D.; RT "Differential expression of prominin-1 (CD133) and prominin-2 in major RT cephalic exocrine glands of adult mice."; RL Histochem. Cell Biol. 128:409-419(2007). RN [11] RP NOMENCLATURE OF ISOFORMS. RX PubMed=17498271; DOI=10.1111/j.1399-0039.2007.00825.x; RA Fargeas C.A., Huttner W.B., Corbeil D.; RT "Nomenclature of prominin-1 (CD133) splice variants - an update."; RL Tissue Antigens 69:602-606(2007). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=18096722; DOI=10.1634/stemcells.2007-0639; RA Huttner H.B., Janich P., Koehrmann M., Jaszai J., Siebzehnrubl F., RA Bluemcke I., Suttorp M., Gahr M., Kuhnt D., Nimsky C., Krex D., RA Schackert G., Loewenbrueck K., Reichmann H., Juettler E., Hacke W., RA Schellinger P.D., Schwab S., Wilsch-Braeuninger M., Marzesco A.M., RA Corbeil D.; RT "The stem cell marker prominin-1/CD133 on membrane particles in human RT cerebrospinal fluid offers novel approaches for studying central nervous RT system disease."; RL Stem Cells 26:698-705(2008). RN [13] RP SUBCELLULAR LOCATION. RX PubMed=19302789; DOI=10.1016/j.febslet.2009.01.048; RA Marzesco A.M., Wilsch-Brauninger M., Dubreuil V., Janich P., Langenfeld K., RA Thiele C., Huttner W.B., Corbeil D.; RT "Release of extracellular membrane vesicles from microvilli of epithelial RT cells is enhanced by depleting membrane cholesterol."; RL FEBS Lett. 583:897-902(2009). RN [14] RP FUNCTION. RX PubMed=20818439; DOI=10.1038/onc.2010.383; RA Takenobu H., Shimozato O., Nakamura T., Ochiai H., Yamaguchi Y., Ohira M., RA Nakagawara A., Kamijo T.; RT "CD133 suppresses neuroblastoma cell differentiation via signal pathway RT modification."; RL Oncogene 30:97-105(2011). RN [15] RP INVOLVEMENT IN RP41. RX PubMed=10587575; DOI=10.1093/hmg/9.1.27; RA Maw M.A., Corbeil D., Koch J., Hellwig A., Wilson-Wheeler J.C., RA Bridges R.J., Kumaramanickavel G., John S., Nancarrow D., Roeper K., RA Weigmann A., Huttner W.B., Denton M.J.; RT "A frameshift mutation in prominin (mouse)-like 1 causes human retinal RT degeneration."; RL Hum. Mol. Genet. 9:27-34(2000). RN [16] RP INVOLVEMENT IN RP41. RX PubMed=17605048; DOI=10.1007/s00439-007-0395-2; RA Zhang Q., Zulfiqar F., Xiao X., Riazuddin S.A., Ahmad Z., Caruso R., RA MacDonald I., Sieving P., Riazuddin S., Hejtmancik J.F.; RT "Severe retinitis pigmentosa mapped to 4p15 and associated with a novel RT mutation in the PROM1 gene."; RL Hum. Genet. 122:293-299(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, RP ACETYLATION AT LYS-225; LYS-257 AND LYS-264 BY NAT8 AND NAT8B, MUTAGENESIS RP OF LYS-225; LYS-257 AND LYS-264, AND INTERACTION WITH NAT8 AND NAT8B. RX PubMed=24556617; DOI=10.1016/j.jmb.2014.02.012; RA Mak A.B., Pehar M., Nixon A.M., Williams R.A., Uetrecht A.C., Puglielli L., RA Moffat J.; RT "Post-translational regulation of CD133 by ATase1/ATase2-mediated lysine RT acetylation."; RL J. Mol. Biol. 426:2175-2182(2014). RN [19] RP INVOLVEMENT IN CORD12, INVOLVEMENT IN STGD4, INVOLVEMENT IN MCDR2, VARIANT RP CORD12/STGD4/MCDR2 CYS-373, INTERACTION WITH CDHR1 AND ACTIN, AND RP CHARACTERIZATION OF VARIANT CORD12/STGD4/MCDR2 CYS-373. RX PubMed=18654668; DOI=10.1172/jci35891; RA Yang Z., Chen Y., Lillo C., Chien J., Yu Z., Michaelides M., Klein M., RA Howes K.A., Li Y., Kaminoh Y., Chen H., Zhao C., Chen Y., Al-Sheikh Y.T., RA Karan G., Corbeil D., Escher P., Kamaya S., Li C., Johnson S., RA Frederick J.M., Zhao Y., Wang C., Cameron D.J., Huttner W.B., RA Schorderet D.F., Munier F.L., Moore A.T., Birch D.G., Baehr W., Hunt D.M., RA Williams D.S., Zhang K.; RT "Mutant prominin 1 found in patients with macular degeneration disrupts RT photoreceptor disk morphogenesis in mice."; RL J. Clin. Invest. 118:2908-2916(2008). RN [20] RP VARIANT CORD12 CYS-373. RX PubMed=35947379; DOI=10.1167/iovs.63.9.14; RG Genomics England Research Consortium; RA Martin-Gutierrez M.P., Schiff E.R., Wright G., Waseem N., Mahroo O.A., RA Michaelides M., Moore A.T., Webster A.R., Arno G.; RT "Dominant Cone Rod Dystrophy, Previously Assigned to a Missense Variant in RT RIMS1, Is Fully Explained by Co-Inheritance of a Dominant Allele of RT PROM1."; RL Invest. Ophthalmol. Vis. Sci. 63:14-14(2022). CC -!- FUNCTION: May play a role in cell differentiation, proliferation and CC apoptosis (PubMed:24556617). Binds cholesterol in cholesterol- CC containing plasma membrane microdomains and may play a role in the CC organization of the apical plasma membrane in epithelial cells. During CC early retinal development acts as a key regulator of disk CC morphogenesis. Involved in regulation of MAPK and Akt signaling CC pathways. In neuroblastoma cells suppresses cell differentiation such CC as neurite outgrowth in a RET-dependent manner (PubMed:20818439). CC {ECO:0000269|PubMed:20818439, ECO:0000269|PubMed:24556617}. CC -!- SUBUNIT: Interacts with CDHR1 and with actin filaments. Interacts with CC NAT8 and NAT8B. {ECO:0000269|PubMed:18654668, CC ECO:0000269|PubMed:24556617}. CC -!- INTERACTION: CC O43490; Q9UBN7: HDAC6; NbExp=4; IntAct=EBI-3447549, EBI-301697; CC O43490; Q8VHP6: Cdhr1; Xeno; NbExp=3; IntAct=EBI-3447549, EBI-4395045; CC O43490-2; Q9UBN7: HDAC6; NbExp=2; IntAct=EBI-21452032, EBI-301697; CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. Cell projection, microvillus membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell CC projection, cilium, photoreceptor outer segment {ECO:0000250}. CC Endoplasmic reticulum. Endoplasmic reticulum-Golgi intermediate CC compartment. Note=Found in extracellular membrane particles in various CC body fluids such as cerebrospinal fluid, saliva, seminal fluid and CC urine. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=AC133-1, S2; CC IsoId=O43490-1; Sequence=Displayed; CC Name=2; Synonyms=AC133-2, S1; CC IsoId=O43490-2; Sequence=VSP_039069; CC Name=3; Synonyms=S3; CC IsoId=O43490-3; Sequence=VSP_040000, VSP_040002, VSP_040004; CC Name=4; Synonyms=S10; CC IsoId=O43490-4; Sequence=VSP_040000, VSP_040003; CC Name=5; Synonyms=S7; CC IsoId=O43490-5; Sequence=VSP_040000, VSP_040001; CC Name=6; Synonyms=S11; CC IsoId=O43490-6; Sequence=VSP_040001; CC Name=7; Synonyms=S12; CC IsoId=O43490-7; Sequence=VSP_040003; CC -!- TISSUE SPECIFICITY: Isoform 1 is selectively expressed on CD34 CC hematopoietic stem and progenitor cells in adult and fetal bone marrow, CC fetal liver, cord blood and adult peripheral blood. Isoform 1 is not CC detected on other blood cells. Isoform 1 is also expressed in a number CC of non-lymphoid tissues including retina, pancreas, placenta, kidney, CC liver, lung, brain and heart. Found in saliva within small membrane CC particles. Isoform 2 is predominantly expressed in fetal liver, CC skeletal muscle, kidney, and heart as well as adult pancreas, kidney, CC liver, lung, and placenta. Isoform 2 is highly expressed in fetal CC liver, low in bone marrow, and barely detectable in peripheral blood. CC Isoform 2 is expressed on hematopoietic stem cells and in epidermal CC basal cells (at protein level). Expressed in adult retina by rod and CC cone photoreceptor cells (at protein level). CC {ECO:0000269|PubMed:12042327, ECO:0000269|PubMed:17874118}. CC -!- PTM: Isoform 1 and isoform 2 are glycosylated. CC {ECO:0000269|PubMed:12042327}. CC -!- PTM: Acetylation at Lys-225, Lys-257 and Lys-264 by NAT8 and NAT8B may CC control PROM1 protein expression and its function in cell apoptosis. CC {ECO:0000269|PubMed:24556617}. CC -!- DISEASE: Retinitis pigmentosa 41 (RP41) [MIM:612095]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis CC pigmentosa is characterized by retinal pigment deposits visible on CC fundus examination and primary loss of rod photoreceptor cells followed CC by secondary loss of cone photoreceptors. Patients typically have night CC vision blindness and loss of midperipheral visual field. As their CC condition progresses, they lose their far peripheral visual field and CC eventually central vision as well. {ECO:0000269|PubMed:10587575, CC ECO:0000269|PubMed:17605048}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Cone-rod dystrophy 12 (CORD12) [MIM:612657]: An inherited CC retinal dystrophy characterized by retinal pigment deposits visible on CC fundus examination, predominantly in the macular region, and initial CC loss of cone photoreceptors followed by rod degeneration. This leads to CC decreased visual acuity and sensitivity in the central visual field, CC followed by loss of peripheral vision. Severe loss of vision occurs CC earlier than in retinitis pigmentosa, due to cone photoreceptors CC degenerating at a higher rate than rod photoreceptors. CC {ECO:0000269|PubMed:18654668, ECO:0000269|PubMed:35947379}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Stargardt disease 4 (STGD4) [MIM:603786]: A common hereditary CC macular degeneration. It is characterized by decreased central vision, CC atrophy of the macula and underlying retinal pigment epithelium, and CC frequent presence of prominent flecks in the posterior pole of the CC retina. {ECO:0000269|PubMed:18654668}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Macular dystrophy, retinal, 2 (MCDR2) [MIM:608051]: An CC autosomal dominant retinal disease characterized by dyschromatopsia, CC gradual progressive loss of central visual acuity, and bilateral CC annular atrophy of retinal pigment epithelium at the macula. CC {ECO:0000269|PubMed:18654668}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Is used as marker for hematopoietic stem and progenitor CC cells (HSPC) for somatic stem cell isolation. CC -!- SIMILARITY: Belongs to the prominin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Mutations of the PROM1 gene; Note=Retina CC International's Scientific Newsletter; CC URL="https://www.retina-international.org/files/sci-news/promlmut.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF027208; AAB92514.1; -; mRNA. DR EMBL; AF507034; AAM33415.1; -; mRNA. DR EMBL; AY449689; AAS19705.1; -; mRNA. DR EMBL; AY449690; AAS19706.1; -; mRNA. DR EMBL; AY449691; AAS19707.1; -; mRNA. DR EMBL; AY449692; AAS19708.1; -; mRNA. DR EMBL; AY449693; AAS19709.1; -; mRNA. DR EMBL; AF117225; AAO15307.1; -; mRNA. DR EMBL; AK027422; BAG51317.1; -; mRNA. DR EMBL; AC005598; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108063; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471069; EAW92750.1; -; Genomic_DNA. DR EMBL; BC012089; AAH12089.1; -; mRNA. DR CCDS; CCDS47029.1; -. [O43490-1] DR CCDS; CCDS54746.1; -. [O43490-2] DR CCDS; CCDS54747.1; -. [O43490-6] DR CCDS; CCDS54748.1; -. [O43490-7] DR CCDS; CCDS93482.1; -. [O43490-5] DR CCDS; CCDS93483.1; -. [O43490-4] DR PIR; T09050; T09050. DR RefSeq; NP_001139319.1; NM_001145847.1. [O43490-2] DR RefSeq; NP_001139320.1; NM_001145848.1. [O43490-2] DR RefSeq; NP_001139321.1; NM_001145849.1. [O43490-7] DR RefSeq; NP_001139322.1; NM_001145850.1. [O43490-6] DR RefSeq; NP_001139323.1; NM_001145851.1. [O43490-4] DR RefSeq; NP_001139324.1; NM_001145852.1. [O43490-5] DR RefSeq; NP_006008.1; NM_006017.2. [O43490-1] DR RefSeq; XP_005248252.1; XM_005248195.4. [O43490-4] DR RefSeq; XP_005248253.1; XM_005248196.4. [O43490-5] DR RefSeq; XP_011512192.1; XM_011513890.1. DR RefSeq; XP_011512194.1; XM_011513892.2. DR RefSeq; XP_011512195.1; XM_011513893.2. [O43490-1] DR RefSeq; XP_011512196.1; XM_011513894.2. [O43490-1] DR RefSeq; XP_011512197.1; XM_011513895.2. [O43490-1] DR RefSeq; XP_011512198.1; XM_011513896.2. DR RefSeq; XP_011512199.1; XM_011513897.2. [O43490-1] DR RefSeq; XP_011512201.2; XM_011513899.2. DR RefSeq; XP_011512202.1; XM_011513900.2. [O43490-7] DR RefSeq; XP_011512204.1; XM_011513902.2. [O43490-6] DR RefSeq; XP_016864288.1; XM_017008799.1. DR RefSeq; XP_016864291.1; XM_017008802.1. DR RefSeq; XP_016864292.1; XM_017008803.1. DR RefSeq; XP_016864293.1; XM_017008804.1. DR RefSeq; XP_016864294.1; XM_017008805.1. DR AlphaFoldDB; O43490; -. DR SMR; O43490; -. DR BioGRID; 114369; 21. DR IntAct; O43490; 34. DR STRING; 9606.ENSP00000426809; -. DR TCDB; 9.B.411.1.1; the prominin (prominin) family. DR GlyConnect; 1642; 16 N-Linked glycans (2 sites). DR GlyCosmos; O43490; 8 sites, 15 glycans. DR GlyGen; O43490; 8 sites, 15 N-linked glycans (2 sites). DR iPTMnet; O43490; -. DR PhosphoSitePlus; O43490; -. DR SwissPalm; O43490; -. DR BioMuta; PROM1; -. DR EPD; O43490; -. DR jPOST; O43490; -. DR MassIVE; O43490; -. DR MaxQB; O43490; -. DR PaxDb; 9606-ENSP00000426809; -. DR PeptideAtlas; O43490; -. DR ProteomicsDB; 48967; -. [O43490-1] DR ProteomicsDB; 48968; -. [O43490-2] DR ProteomicsDB; 48969; -. [O43490-3] DR ProteomicsDB; 48970; -. [O43490-4] DR ProteomicsDB; 48971; -. [O43490-5] DR ProteomicsDB; 48972; -. [O43490-6] DR ProteomicsDB; 48973; -. [O43490-7] DR Pumba; O43490; -. DR ABCD; O43490; 12 sequenced antibodies. DR Antibodypedia; 1554; 892 antibodies from 42 providers. DR CPTC; O43490; 2 antibodies. DR DNASU; 8842; -. DR Ensembl; ENST00000447510.7; ENSP00000415481.2; ENSG00000007062.12. [O43490-1] DR Ensembl; ENST00000505450.5; ENSP00000426090.1; ENSG00000007062.12. [O43490-2] DR Ensembl; ENST00000508167.5; ENSP00000427346.1; ENSG00000007062.12. [O43490-2] DR Ensembl; ENST00000510224.5; ENSP00000426809.1; ENSG00000007062.12. [O43490-1] DR Ensembl; ENST00000539194.6; ENSP00000443620.1; ENSG00000007062.12. [O43490-6] DR Ensembl; ENST00000540805.6; ENSP00000438045.2; ENSG00000007062.12. [O43490-4] DR Ensembl; ENST00000675377.1; ENSP00000502545.1; ENSG00000007062.12. [O43490-7] DR Ensembl; ENST00000675613.1; ENSP00000501741.1; ENSG00000007062.12. [O43490-5] DR GeneID; 8842; -. DR KEGG; hsa:8842; -. DR MANE-Select; ENST00000447510.7; ENSP00000415481.2; NM_006017.3; NP_006008.1. DR UCSC; uc003goo.2; human. [O43490-1] DR AGR; HGNC:9454; -. DR CTD; 8842; -. DR DisGeNET; 8842; -. DR GeneCards; PROM1; -. DR GeneReviews; PROM1; -. DR HGNC; HGNC:9454; PROM1. DR HPA; ENSG00000007062; Tissue enriched (retina). DR MalaCards; PROM1; -. DR MIM; 603786; phenotype. DR MIM; 604365; gene. DR MIM; 608051; phenotype. DR MIM; 612095; phenotype. DR MIM; 612657; phenotype. DR neXtProt; NX_O43490; -. DR OpenTargets; ENSG00000007062; -. DR Orphanet; 1872; Cone rod dystrophy. DR Orphanet; 319640; Retinal macular dystrophy type 2. DR Orphanet; 791; Retinitis pigmentosa. DR Orphanet; 827; Stargardt disease. DR PharmGKB; PA33807; -. DR VEuPathDB; HostDB:ENSG00000007062; -. DR eggNOG; KOG4331; Eukaryota. DR GeneTree; ENSGT00530000063586; -. DR HOGENOM; CLU_008293_0_0_1; -. DR InParanoid; O43490; -. DR OMA; VYHLMMY; -. DR OrthoDB; 3538424at2759; -. DR PhylomeDB; O43490; -. DR TreeFam; TF324631; -. DR PathwayCommons; O43490; -. DR SignaLink; O43490; -. DR SIGNOR; O43490; -. DR BioGRID-ORCS; 8842; 17 hits in 1149 CRISPR screens. DR ChiTaRS; PROM1; human. DR GeneWiki; CD133; -. DR GenomeRNAi; 8842; -. DR Pharos; O43490; Tbio. DR PRO; PR:O43490; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; O43490; Protein. DR Bgee; ENSG00000007062; Expressed in bronchial epithelial cell and 182 other cell types or tissues. DR ExpressionAtlas; O43490; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005929; C:cilium; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005902; C:microvillus; IBA:GO_Central. DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell. DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB. DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0071914; C:prominosome; IBA:GO_Central. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0042805; F:actinin binding; IDA:BHF-UCL. DR GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL. DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central. DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IMP:BHF-UCL. DR GO; GO:0072139; P:glomerular parietal epithelial cell differentiation; IMP:UniProtKB. DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:BHF-UCL. DR GO; GO:0072112; P:podocyte differentiation; IMP:UniProtKB. DR GO; GO:2000768; P:positive regulation of nephron tubule epithelial cell differentiation; IMP:UniProtKB. DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB. DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:BHF-UCL. DR InterPro; IPR008795; Prominin. DR PANTHER; PTHR22730; PROMININ PROM PROTEIN; 1. DR PANTHER; PTHR22730:SF3; PROMININ-1; 1. DR Pfam; PF05478; Prominin; 1. DR Genevisible; O43490; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell membrane; Cell projection; Cilium; KW Cone-rod dystrophy; Direct protein sequencing; Disease variant; KW Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein; KW Reference proteome; Retinitis pigmentosa; Signal; Stargardt disease; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..865 FT /note="Prominin-1" FT /id="PRO_0000025813" FT TOPO_DOM 20..108 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 109..129 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 130..157 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 158..178 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 179..433 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 434..454 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 455..486 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 487..507 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 508..792 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 793..813 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 814..865 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOD_RES 225 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:24556617" FT MOD_RES 257 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:24556617" FT MOD_RES 264 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:24556617" FT MOD_RES 863 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 274 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 395 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 414 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 548 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 580 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 729 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 730 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 92..100 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12042327, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.4" FT /id="VSP_039069" FT VAR_SEQ 93..101 FT /note="Missing (in isoform 3, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_040000" FT VAR_SEQ 831..861 FT /note="Missing (in isoform 5 and isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_040001" FT VAR_SEQ 831..839 FT /note="VETIPMKNM -> SSWVTSVQC (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_040002" FT VAR_SEQ 839..861 FT /note="Missing (in isoform 4 and isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_040003" FT VAR_SEQ 840..865 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_040004" FT VARIANT 31 FT /note="A -> G" FT /id="VAR_010382" FT VARIANT 31 FT /note="A -> S" FT /id="VAR_010383" FT VARIANT 373 FT /note="R -> C (in CORD12, STGD4 and MCDR2; affects the FT interaction with actin; dbSNP:rs137853006)" FT /evidence="ECO:0000269|PubMed:18654668, FT ECO:0000269|PubMed:35947379" FT /id="VAR_057961" FT MUTAGEN 225 FT /note="K->Q: Loss of acetylation; when associated with FT Q-257 and Q-264." FT /evidence="ECO:0000269|PubMed:24556617" FT MUTAGEN 225 FT /note="K->R: Loss of expression of the protein in part due FT to proteasomal degradation; when associated with Q-257 and FT Q-264." FT /evidence="ECO:0000269|PubMed:24556617" FT MUTAGEN 257 FT /note="K->Q: Loss of acetylation; when associated with FT Q-225 and Q-264." FT /evidence="ECO:0000269|PubMed:24556617" FT MUTAGEN 257 FT /note="K->R: Loss of expression of the protein in part due FT to proteasomal degradation; when associated with Q-225 and FT Q-264." FT /evidence="ECO:0000269|PubMed:24556617" FT MUTAGEN 264 FT /note="K->Q: Loss of acetylation; when associated with FT Q-225 and Q-257." FT /evidence="ECO:0000269|PubMed:24556617" FT MUTAGEN 264 FT /note="K->R: Loss of expression of the protein in part due FT to proteasomal degradation; when associated with Q-225 and FT Q-257." FT /evidence="ECO:0000269|PubMed:24556617" FT CONFLICT 200 FT /note="D -> A (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 200 FT /note="D -> P (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 284 FT /note="S -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="S -> R (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 865 AA; 97202 MW; D21CBC05ADB2DEDF CRC64; MALVLGSLLL LGLCGNSFSG GQPSSTDAPK AWNYELPATN YETQDSHKAG PIGILFELVH IFLYVVQPRD FPEDTLRKFL QKAYESKIDY DKPETVILGL KIVYYEAGII LCCVLGLLFI ILMPLVGYFF CMCRCCNKCG GEMHQRQKEN GPFLRKCFAI SLLVICIIIS IGIFYGFVAN HQVRTRIKRS RKLADSNFKD LRTLLNETPE QIKYILAQYN TTKDKAFTDL NSINSVLGGG ILDRLRPNII PVLDEIKSMA TAIKETKEAL ENMNSTLKSL HQQSTQLSSS LTSVKTSLRS SLNDPLCLVH PSSETCNSIR LSLSQLNSNP ELRQLPPVDA ELDNVNNVLR TDLDGLVQQG YQSLNDIPDR VQRQTTTVVA GIKRVLNSIG SDIDNVTQRL PIQDILSAFS VYVNNTESYI HRNLPTLEEY DSYWWLGGLV ICSLLTLIVI FYYLGLLCGV CGYDRHATPT TRGCVSNTGG VFLMVGVGLS FLFCWILMII VVLTFVFGAN VEKLICEPYT SKELFRVLDT PYLLNEDWEY YLSGKLFNKS KMKLTFEQVY SDCKKNRGTY GTLHLQNSFN ISEHLNINEH TGSISSELES LKVNLNIFLL GAAGRKNLQD FAACGIDRMN YDSYLAQTGK SPAGVNLLSF AYDLEAKANS LPPGNLRNSL KRDAQTIKTI HQQRVLPIEQ SLSTLYQSVK ILQRTGNGLL ERVTRILASL DFAQNFITNN TSSVIIEETK KYGRTIIGYF EHYLQWIEFS ISEKVASCKP VATALDTAVD VFLCSYIIDP LNLFWFGIGK ATVFLLPALI FAVKLAKYYR RMDSEDVYDD VETIPMKNME NGNNGYHKDH VYGIHNPVMT SPSQH //