PROM1_HUMAN
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 03-AUG-2022, entry version 189.
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).
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}. Note=The disease is caused by variants
CC affecting the gene represented in this 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: Retinal macular dystrophy 2 (MCDR2) [MIM:608051]: A bull's-eye
CC macular dystrophy characterized by bilateral annular atrophy of retinal
CC pigment epithelium at the macula. {ECO:0000269|PubMed:18654668}.
CC Note=The disease is caused by variants affecting the gene represented
CC 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";
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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 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. [O43490-1]
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. [O43490-1]
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; 18.
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 GlyGen; O43490; 8 sites, 15 N-linked glycans (2 sites).
DR iPTMnet; O43490; -.
DR PhosphoSitePlus; O43490; -.
DR BioMuta; PROM1; -.
DR EPD; O43490; -.
DR jPOST; O43490; -.
DR MassIVE; O43490; -.
DR MaxQB; O43490; -.
DR PaxDb; O43490; -.
DR PeptideAtlas; O43490; -.
DR PRIDE; 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 ABCD; O43490; 12 sequenced antibodies.
DR Antibodypedia; 1554; 746 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 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; TIFREQA; -.
DR OrthoDB; 1129032at2759; -.
DR PhylomeDB; O43490; -.
DR TreeFam; TF324631; -.
DR PathwayCommons; O43490; -.
DR SignaLink; O43490; -.
DR SIGNOR; O43490; -.
DR BioGRID-ORCS; 8842; 12 hits in 1067 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 180 other tissues.
DR ExpressionAtlas; O43490; baseline and differential.
DR Genevisible; O43490; HS.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; PTHR22730; 1.
DR Pfam; PF05478; Prominin; 1.
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 /id="VAR_057961"
FT MUTAGEN 225
FT /note="K->Q: Loss of acetylation; when associated with Q-
FT 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 Q-
FT 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 Q-
FT 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
