ABCB5_HUMAN
ID ABCB5_HUMAN Reviewed; 1257 AA.
AC Q2M3G0; A4D131; A7BKA4; B5MD19; B7WPL1; F8QQP8; F8QQP9; J3KQ04; Q2M3I5;
AC Q5I5Q7; Q5I5Q8; Q6KG50; Q6XFQ5; Q8IXA1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 4.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP-binding cassette sub-family B member 5 {ECO:0000305};
DE AltName: Full=ABCB5 P-gp;
DE AltName: Full=P-glycoprotein ABCB5;
DE EC=7.6.2.2 {ECO:0000269|PubMed:22306008};
GN Name=ABCB5 {ECO:0000312|HGNC:HGNC:46};
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), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANT LYS-970.
RC TISSUE=Melanocyte, and Melanoma;
RX PubMed=12960149; DOI=10.1074/jbc.m308700200;
RA Frank N.Y., Pendse S.S., Lapchak P.H., Margaryan A., Shlain D., Doeing C.,
RA Sayegh M.H., Frank M.H.;
RT "Regulation of progenitor cell fusion by ABCB5 P-glycoprotein, a novel
RT human ATP-binding cassette transporter.";
RL J. Biol. Chem. 278:47156-47165(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS GLU-560 AND
RP LYS-970, AND TISSUE SPECIFICITY.
RC TISSUE=Melanoma;
RX PubMed=15760339; DOI=10.1111/j.1600-0749.2005.00214.x;
RA Chen K.G., Szakacs G., Annereau J.-P., Rouzaud F., Liang X.-J.,
RA Valencia J.C., Nagineni C.N., Hooks J.J., Hearing V.J., Gottesman M.M.;
RT "Principal expression of two mRNA isoforms (ABCB 5alpha and ABCB 5beta) of
RT the ATP-binding cassette transporter gene ABCB 5 in melanoma cells and
RT melanocytes.";
RL Pigment Cell Res. 18:102-112(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RX PubMed=21652540; DOI=10.1158/0008-5472.can-11-0221;
RA Wilson B.J., Schatton T., Zhan Q., Gasser M., Ma J., Saab K.R.,
RA Schanche R., Waaga-Gasser A.M., Gold J.S., Huang Q., Murphy G.F.,
RA Frank M.H., Frank N.Y.;
RT "ABCB5 identifies a therapy-refractory tumor cell population in colorectal
RT cancer patients.";
RL Cancer Res. 71:5307-5316(2011).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, VARIANT LYS-970, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Prostate, and Testis;
RX PubMed=22306008; DOI=10.1016/j.bbrc.2012.01.090;
RA Kawanobe T., Kogure S., Nakamura S., Sato M., Katayama K., Mitsuhashi J.,
RA Noguchi K., Sugimoto Y.;
RT "Expression of human ABCB5 confers resistance to taxanes and
RT anthracyclines.";
RL Biochem. Biophys. Res. Commun. 418:736-741(2012).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT LYS-970.
RA Meij I.C., van Aubel R., Tammur J., Dean M., Russel F.G., Allikmets R.,
RA Cremers F.P.M.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-970.
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Melanoma;
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 [10]
RP FUNCTION.
RX PubMed=15205344; DOI=10.1158/0008-5472.can-03-3884;
RA Huang Y., Anderle P., Bussey K.J., Barbacioru C., Shankavaram U., Dai Z.,
RA Reinhold W.C., Papp A., Weinstein J.N., Sadee W.;
RT "Membrane transporters and channels: role of the transportome in cancer
RT chemosensitivity and chemoresistance.";
RL Cancer Res. 64:4294-4301(2004).
RN [11]
RP FUNCTION.
RX PubMed=15899824; DOI=10.1158/0008-5472.can-04-3327;
RA Frank N.Y., Margaryan A., Huang Y., Schatton T., Waaga-Gasser A.M.,
RA Gasser M., Sayegh M.H., Sadee W., Frank M.H.;
RT "ABCB5-mediated doxorubicin transport and chemoresistance in human
RT malignant melanoma.";
RL Cancer Res. 65:4320-4333(2005).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=22784549; DOI=10.1016/j.ejca.2012.05.027;
RA Grimm M., Krimmel M., Polligkeit J., Alexander D., Munz A., Kluba S.,
RA Keutel C., Hoffmann J., Reinert S., Hoefert S.;
RT "ABCB5 expression and cancer stem cell hypothesis in oral squamous cell
RT carcinoma.";
RL Eur. J. Cancer 48:3186-3197(2012).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=22044138; DOI=10.3109/10428194.2011.637214;
RA Yang M., Li W., Fan D., Yan Y., Zhang X., Zhang Y., Xiong D.;
RT "Expression of ABCB5 gene in hematological malignances and its
RT significance.";
RL Leuk. Lymphoma 53:1211-1215(2012).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=22675422; DOI=10.1371/journal.pone.0036762;
RA Chartrain M., Riond J., Stennevin A., Vandenberghe I., Gomes B., Lamant L.,
RA Meyer N., Gairin J.E., Guilbaud N., Annereau J.P.;
RT "Melanoma chemotherapy leads to the selection of ABCB5-expressing cells.";
RL PLoS ONE 7:E36762-E36762(2012).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=23770371; DOI=10.1016/j.bbrc.2013.06.006;
RA Lin J.Y., Zhang M., Schatton T., Wilson B.J., Alloo A., Ma J.,
RA Qureshi A.A., Frank N.Y., Han J., Frank M.H.;
RT "Genetically determined ABCB5 functionality correlates with pigmentation
RT phenotype and melanoma risk.";
RL Biochem. Biophys. Res. Commun. 436:536-542(2013).
RN [16]
RP TISSUE SPECIFICITY.
RX PubMed=24934811; DOI=10.1158/0008-5472.can-14-0582;
RA Wilson B.J., Saab K.R., Ma J., Schatton T., Putz P., Zhan Q., Murphy G.F.,
RA Gasser M., Waaga-Gasser A.M., Frank N.Y., Frank M.H.;
RT "ABCB5 maintains melanoma-initiating cells through a pro-inflammatory
RT cytokine signaling circuit.";
RL Cancer Res. 74:4196-4207(2014).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-675.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] THR-880.
RX PubMed=18772397; DOI=10.1126/science.1164368;
RA Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P.,
RA Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T.,
RA Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y.,
RA Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M.,
RA Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E.,
RA Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B.,
RA Velculescu V.E., Kinzler K.W.;
RT "Core signaling pathways in human pancreatic cancers revealed by global
RT genomic analyses.";
RL Science 321:1801-1806(2008).
RN [19]
RP TISSUE SPECIFICITY.
RX PubMed=25030174; DOI=10.1038/nature13426;
RA Ksander B.R., Kolovou P.E., Wilson B.J., Saab K.R., Guo Q., Ma J.,
RA McGuire S.P., Gregory M.S., Vincent W.J., Perez V.L., Cruz-Guilloty F.,
RA Kao W.W., Call M.K., Tucker B.A., Zhan Q., Murphy G.F., Lathrop K.L.,
RA Alt C., Mortensen L.J., Lin C.P., Zieske J.D., Frank M.H., Frank N.Y.;
RT "ABCB5 is a limbal stem cell gene required for corneal development and
RT repair.";
RL Nature 511:353-357(2014).
CC -!- FUNCTION: Energy-dependent efflux transporter responsible for decreased
CC drug accumulation in multidrug-resistant cells (PubMed:12960149,
CC PubMed:22306008, PubMed:15899824, PubMed:15205344). Specifically
CC present in limbal stem cells, where it plays a key role in corneal
CC development and repair (By similarity). {ECO:0000250|UniProtKB:B5X0E4,
CC ECO:0000269|PubMed:12960149, ECO:0000269|PubMed:15205344,
CC ECO:0000269|PubMed:15899824, ECO:0000269|PubMed:22306008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + daunorubicin(in) + H2O = ADP + daunorubicin(out) + H(+)
CC + phosphate; Xref=Rhea:RHEA:33147, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64677, ChEBI:CHEBI:456216; EC=7.6.2.2;
CC Evidence={ECO:0000269|PubMed:22306008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33148;
CC Evidence={ECO:0000269|PubMed:22306008};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12960149};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:12960149}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=Q2M3G0-4; Sequence=Displayed;
CC Name=2; Synonyms=ABCB5alpha;
CC IsoId=Q2M3G0-2; Sequence=VSP_056752, VSP_056753, VSP_056756;
CC Name=3;
CC IsoId=Q2M3G0-3; Sequence=VSP_056752, VSP_056754, VSP_056755;
CC Name=1; Synonyms=ABCB5beta;
CC IsoId=Q2M3G0-1; Sequence=VSP_056752;
CC -!- TISSUE SPECIFICITY: Expressed by CD133-expressing progenitor cells
CC among epidermal melanocytes (at protein level). Widely expressed with
CC specific expression in pigment cells. Highly expressed in several
CC malignant tissues: highly expressed in clinical melanomas, with low
CC expression in normal skin. In melanoma, marks malignant melanoma-
CC initiating cells (MMIC), in which clinical virulence resides as a
CC consequence of unlimited self-renewal capacity, resulting in inexorable
CC tumor progression and metastasis. Also highly expressed in a number of
CC leukemia cells. Expressed in basal limbal epithelium.
CC {ECO:0000269|PubMed:12960149, ECO:0000269|PubMed:15760339,
CC ECO:0000269|PubMed:22044138, ECO:0000269|PubMed:22675422,
CC ECO:0000269|PubMed:22784549, ECO:0000269|PubMed:23770371,
CC ECO:0000269|PubMed:24934811, ECO:0000269|PubMed:25030174}.
CC -!- MISCELLANEOUS: Acts as a marker of stem-like cells (CSC) in a number of
CC malignancies (PubMed:24934811). Associated with clinical drug
CC resistance, tumor progression and disease recurrence in malignant
CC melanoma and acute leukemias. Responsible for the resistance to
CC doxorubicin of a subset of malignant melanomas. ABCB5-expressing cells
CC selectively survive when exposed to dacarbazine drug, the reference
CC treatment of metastatic melanoma, vemurafenib and other various
CC chemotherapeutic drugs, suggesting that anti-melanoma chemotherapy
CC participates in the chemoresistance acquisition by selecting tumor cell
CC subpopulations expressing ABCB5 (PubMed:22784549, PubMed:22044138,
CC PubMed:22675422, PubMed:23770371, PubMed:24934811). Present in
CC melanoma-initiating cells that acts as an enhancer of tumor growth by
CC promoting CSC maintenance and tumor growth by controlling IL-1beta
CC (IL1B) secretion to maintain slow-cycling, chemoresistant cells through
CC an IL-1beta (IL1B)/IL8/CXCR1 cytokine signaling circuit
CC (PubMed:24934811). {ECO:0000305|PubMed:22044138,
CC ECO:0000305|PubMed:22675422, ECO:0000305|PubMed:22784549,
CC ECO:0000305|PubMed:23770371, ECO:0000305|PubMed:24934811}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC -!- CAUTION: Was named ABCB1 by some authors. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN76500.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ03033.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ABCB5ID44305ch7p15.html";
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DR EMBL; AF319622; AAN76500.1; ALT_INIT; mRNA.
DR EMBL; AF399931; AAQ03033.1; ALT_INIT; mRNA.
DR EMBL; AY090613; AAM09027.1; -; mRNA.
DR EMBL; AY234788; AAO73470.1; -; mRNA.
DR EMBL; AY851364; AAW31629.1; -; mRNA.
DR EMBL; AY851365; AAW31630.1; -; mRNA.
DR EMBL; GU437216; ADV32636.1; -; mRNA.
DR EMBL; GU437217; ADV32637.1; -; mRNA.
DR EMBL; AB353947; BAF75364.1; -; mRNA.
DR EMBL; AY230001; AAP55848.1; -; mRNA.
DR EMBL; AC002486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236948; EAL24273.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93726.1; -; Genomic_DNA.
DR EMBL; BC104894; AAI04895.2; -; mRNA.
DR EMBL; BC104920; AAI04921.1; -; mRNA.
DR EMBL; BC110370; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS5371.1; -. [Q2M3G0-1]
DR CCDS; CCDS55090.1; -. [Q2M3G0-4]
DR CCDS; CCDS55091.1; -. [Q2M3G0-2]
DR CCDS; CCDS55092.1; -. [Q2M3G0-3]
DR RefSeq; NP_001157413.1; NM_001163941.1. [Q2M3G0-4]
DR RefSeq; NP_001157414.1; NM_001163942.1. [Q2M3G0-2]
DR RefSeq; NP_001157465.1; NM_001163993.2. [Q2M3G0-3]
DR RefSeq; NP_848654.3; NM_178559.5. [Q2M3G0-1]
DR RefSeq; XP_011513669.1; XM_011515367.2. [Q2M3G0-1]
DR AlphaFoldDB; Q2M3G0; -.
DR SMR; Q2M3G0; -.
DR BioGRID; 131028; 11.
DR IntAct; Q2M3G0; 2.
DR STRING; 9606.ENSP00000384881; -.
DR ChEMBL; CHEMBL1772928; -.
DR DrugBank; DB06263; Amrubicin.
DR DrugBank; DB13997; Baloxavir marboxil.
DR DrugBank; DB11591; Bilastine.
DR DrugBank; DB04851; Biricodar.
DR DrugBank; DB08870; Brentuximab vedotin.
DR DrugBank; DB12267; Brigatinib.
DR DrugBank; DB09183; Dasabuvir.
DR DrugBank; DB11943; Delafloxacin.
DR DrugBank; DB14067; Dofequidar.
DR DrugBank; DB00254; Doxycycline.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB00598; Labetalol.
DR DrugBank; DB04948; Lofexidine.
DR DrugBank; DB11691; Naldemedine.
DR DrugBank; DB11641; Vinflunine.
DR TCDB; 3.A.1.201.13; the atp-binding cassette (abc) superfamily.
DR TCDB; 3.A.1.209.4; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q2M3G0; 11 sites.
DR iPTMnet; Q2M3G0; -.
DR PhosphoSitePlus; Q2M3G0; -.
DR BioMuta; ABCB5; -.
DR DMDM; 308153645; -.
DR EPD; Q2M3G0; -.
DR jPOST; Q2M3G0; -.
DR MassIVE; Q2M3G0; -.
DR MaxQB; Q2M3G0; -.
DR PaxDb; Q2M3G0; -.
DR PeptideAtlas; Q2M3G0; -.
DR PRIDE; Q2M3G0; -.
DR ProteomicsDB; 61374; -. [Q2M3G0-4]
DR ProteomicsDB; 61375; -. [Q2M3G0-2]
DR ProteomicsDB; 6148; -.
DR Antibodypedia; 11940; 423 antibodies from 38 providers.
DR DNASU; 340273; -.
DR Ensembl; ENST00000258738.10; ENSP00000258738.6; ENSG00000004846.17. [Q2M3G0-1]
DR Ensembl; ENST00000404938.7; ENSP00000384881.2; ENSG00000004846.17. [Q2M3G0-4]
DR Ensembl; ENST00000406935.5; ENSP00000383899.1; ENSG00000004846.17. [Q2M3G0-3]
DR Ensembl; ENST00000443026.6; ENSP00000406730.2; ENSG00000004846.17. [Q2M3G0-2]
DR GeneID; 340273; -.
DR KEGG; hsa:340273; -.
DR MANE-Select; ENST00000404938.7; ENSP00000384881.2; NM_001163941.2; NP_001157413.1.
DR UCSC; uc003suv.4; human. [Q2M3G0-4]
DR CTD; 340273; -.
DR DisGeNET; 340273; -.
DR GeneCards; ABCB5; -.
DR HGNC; HGNC:46; ABCB5.
DR HPA; ENSG00000004846; Tissue enriched (epididymis).
DR MIM; 611785; gene.
DR neXtProt; NX_Q2M3G0; -.
DR OpenTargets; ENSG00000004846; -.
DR PharmGKB; PA24387; -.
DR VEuPathDB; HostDB:ENSG00000004846; -.
DR eggNOG; KOG0055; Eukaryota.
DR GeneTree; ENSGT00940000161340; -.
DR HOGENOM; CLU_000604_1_9_1; -.
DR InParanoid; Q2M3G0; -.
DR OMA; FGYMQIS; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q2M3G0; -.
DR TreeFam; TF105193; -.
DR BRENDA; 7.6.2.2; 2681.
DR PathwayCommons; Q2M3G0; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR SignaLink; Q2M3G0; -.
DR BioGRID-ORCS; 340273; 13 hits in 1062 CRISPR screens.
DR ChiTaRS; ABCB5; human.
DR GeneWiki; ABCB5; -.
DR GenomeRNAi; 340273; -.
DR Pharos; Q2M3G0; Tbio.
DR PRO; PR:Q2M3G0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q2M3G0; protein.
DR Bgee; ENSG00000004846; Expressed in cauda epididymis and 80 other tissues.
DR ExpressionAtlas; Q2M3G0; baseline and differential.
DR Genevisible; Q2M3G0; HS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IDA:UniProtKB.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Differentiation;
KW Glycoprotein; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1257
FT /note="ATP-binding cassette sub-family B member 5"
FT /id="PRO_0000253575"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 917..937
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 954..974
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 49..350
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 386..622
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 693..980
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1015..1253
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 421..428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1050..1057
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..445
FT /note="Missing (in isoform 1, isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12960149,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15760339,
FT ECO:0000303|PubMed:21652540"
FT /id="VSP_056752"
FT VAR_SEQ 570..576
FT /note="ASKGRTT -> DTPRYSF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15760339"
FT /id="VSP_056753"
FT VAR_SEQ 570..571
FT /note="AS -> KK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056754"
FT VAR_SEQ 572..1257
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056755"
FT VAR_SEQ 577..1257
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15760339"
FT /id="VSP_056756"
FT VARIANT 560
FT /note="K -> E (in dbSNP:rs2301641)"
FT /evidence="ECO:0000269|PubMed:15760339"
FT /id="VAR_028387"
FT VARIANT 669
FT /note="K -> R (in dbSNP:rs13222448)"
FT /id="VAR_028388"
FT VARIANT 675
FT /note="E -> V (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035731"
FT VARIANT 880
FT /note="A -> T (in a pancreatic ductal adenocarcinoma
FT sample; somatic mutation; dbSNP:rs1187237313)"
FT /evidence="ECO:0000269|PubMed:18772397"
FT /id="VAR_062662"
FT VARIANT 905
FT /note="Q -> H (in dbSNP:rs35885925)"
FT /id="VAR_033456"
FT VARIANT 915
FT /note="A -> T (in dbSNP:rs17143304)"
FT /id="VAR_028389"
FT VARIANT 970
FT /note="E -> K (in dbSNP:rs6461515)"
FT /evidence="ECO:0000269|PubMed:12960149,
FT ECO:0000269|PubMed:15760339, ECO:0000269|PubMed:22306008,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.8"
FT /id="VAR_028390"
FT CONFLICT 577
FT /note="I -> M (in Ref. 1; AAN76500)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141
FT /note="L -> P (in Ref. 2; AAW31630)"
FT /evidence="ECO:0000305"
FT CONFLICT 1186
FT /note="L -> I (in Ref. 3; ADV32637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1257 AA; 138641 MW; A4521B83E0D234CF CRC64;
MENSERAEEM QENYQRNGTA EEQPKLRKEA VGSIEIFRFA DGLDITLMIL GILASLVNGA
CLPLMPLVLG EMSDNLISGC LVQTNTTNYQ NCTQSQEKLN EDMTLLTLYY VGIGVAALIF
GYIQISLWII TAARQTKRIR KQFFHSVLAQ DIGWFDSCDI GELNTRMTDD IDKISDGIGD
KIALLFQNMS TFSIGLAVGL VKGWKLTLVT LSTSPLIMAS AAACSRMVIS LTSKELSAYS
KAGAVAEEVL SSIRTVIAFR AQEKELQRYT QNLKDAKDFG IKRTIASKVS LGAVYFFMNG
TYGLAFWYGT SLILNGEPGY TIGTVLAVFF SVIHSSYCIG AAVPHFETFA IARGAAFHIF
QVIDKKPSID NFSTAGYKPE SIEGTVEFKN VSFNYPSRPS IKILKGLNLR IKSGETVALV
GLNGSGKSTV VQLLQRLYDP DDGFIMVDEN DIRALNVRHY RDHIGVVSQE PVLFGTTISN
NIKYGRDDVT DEEMERAARE ANAYDFIMEF PNKFNTLVGE KGAQMSGGQK QRIAIARALV
RNPKILILDE ATSALDSESK SAVQAALEKA SKGRTTIVVA HRLSTIRSAD LIVTLKDGML
AEKGAHAELM AKRGLYYSLV MSQDIKKADE QMESMTYSTE RKTNSLPLHS VKSIKSDFID
KAEESTQSKE ISLPEVSLLK ILKLNKPEWP FVVLGTLASV LNGTVHPVFS IIFAKIITMF
GNNDKTTLKH DAEIYSMIFV ILGVICFVSY FMQGLFYGRA GEILTMRLRH LAFKAMLYQD
IAWFDEKENS TGGLTTILAI DIAQIQGATG SRIGVLTQNA TNMGLSVIIS FIYGWEMTFL
ILSIAPVLAV TGMIETAAMT GFANKDKQEL KHAGKIATEA LENIRTIVSL TREKAFEQMY
EEMLQTQHRN TSKKAQIIGS CYAFSHAFIY FAYAAGFRFG AYLIQAGRMT PEGMFIVFTA
IAYGAMAIGE TLVLAPEYSK AKSGAAHLFA LLEKKPNIDS RSQEGKKPDT CEGNLEFREV
SFFYPCRPDV FILRGLSLSI ERGKTVAFVG SSGCGKSTSV QLLQRLYDPV QGQVLFDGVD
AKELNVQWLR SQIAIVPQEP VLFNCSIAEN IAYGDNSRVV PLDEIKEAAN AANIHSFIEG
LPEKYNTQVG LKGAQLSGGQ KQRLAIARAL LQKPKILLLD EATSALDNDS EKVVQHALDK
ARTGRTCLVV THRLSAIQNA DLIVVLHNGK IKEQGTHQEL LRNRDIYFKL VNAQSVQ
