LOCUS       NP_003733               1321 aa            linear   PRI 04-OCT-2024
DEFINITION  bile salt export pump [Homo sapiens].
ACCESSION   NP_003733
VERSION     NP_003733.2
DBSOURCE    REFSEQ: accession NM_003742.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1321)
  AUTHORS   Khabou,B., Kallabi,F., Abdelaziz,R.B., Maaloul,I., Aloulou,H.,
            Chehida,A.B., Kammoun,T., Barbu,V., Boudawara,T.S., Fakhfakh,F.,
            Khemakhem,B. and Sahnoun,O.S.
  TITLE     Molecular and computational characterization of ABCB11 and ABCG5
            variants in Tunisian patients with neonatal/infantile low-GGT
            intrahepatic cholestasis: Genetic diagnosis and genotype-phenotype
            correlation assessment
  JOURNAL   Ann Hum Genet 88 (3), 194-211 (2024)
   PUBMED   38108658
  REMARK    GeneRIF: Molecular and computational characterization of ABCB11 and
            ABCG5 variants in Tunisian patients with neonatal/infantile low-GGT
            intrahepatic cholestasis: Genetic diagnosis and genotype-phenotype
            correlation assessment.
REFERENCE   2  (residues 1 to 1321)
  AUTHORS   Pang,L., Cui,M., Wu,S. and Kong,J.
  TITLE     Cav-1 regulates the bile salt export pump on the canalicular
            membrane of hepatocytes by PKCalpha-associated signalling under
            cholesterol stimulation
  JOURNAL   J Cell Mol Med 28 (3), e18110 (2024)
   PUBMED   38164042
  REMARK    GeneRIF: Cav-1 regulates the bile salt export pump on the
            canalicular membrane of hepatocytes by PKCalpha-associated
            signalling under cholesterol stimulation.
REFERENCE   3  (residues 1 to 1321)
  AUTHORS   Liu,H., Irobalieva,R.N., Kowal,J., Ni,D., Nosol,K.,
            Bang-Sorensen,R., Lancien,L., Stahlberg,H., Stieger,B. and
            Locher,K.P.
  TITLE     Structural basis of bile salt extrusion and small-molecule
            inhibition in human BSEP
  JOURNAL   Nat Commun 14 (1), 7296 (2023)
   PUBMED   37949847
  REMARK    GeneRIF: Structural basis of bile salt extrusion and small-molecule
            inhibition in human BSEP.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1321)
  AUTHORS   Pfister,E.D., Jaeger,V.K., Karch,A., Shay,D., Schukfeh,N.,
            Ohlendorf,J., Junge,N., Goldschmidt,I., Stalke,A.,
            Keitel-Anselmino,V. and Baumann,U.
  TITLE     Native liver survival in bile salt export pump deficiency: results
            of a retrospective cohort study
  JOURNAL   Hepatol Commun 7 (4), e0092 (2023)
   PUBMED   36995996
  REMARK    GeneRIF: Native liver survival in bile salt export pump deficiency:
            results of a retrospective cohort study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1321)
  AUTHORS   Wang,R., Salem,M., Yousef,I.M., Tuchweber,B., Lam,P., Childs,S.J.,
            Helgason,C.D., Ackerley,C., Phillips,M.J. and Ling,V.
  TITLE     Targeted inactivation of sister of P-glycoprotein gene (spgp) in
            mice results in nonprogressive but persistent intrahepatic
            cholestasis
  JOURNAL   Proc Natl Acad Sci U S A 98 (4), 2011-2016 (2001)
   PUBMED   11172067
REFERENCE   6  (residues 1 to 1321)
  AUTHORS   Jansen,P.L., Strautnieks,S.S., Jacquemin,E., Hadchouel,M.,
            Sokal,E.M., Hooiveld,G.J., Koning,J.H., De Jager-Krikken,A.,
            Kuipers,F., Stellaard,F., Bijleveld,C.M., Gouw,A., Van Goor,H.,
            Thompson,R.J. and Muller,M.
  TITLE     Hepatocanalicular bile salt export pump deficiency in patients with
            progressive familial intrahepatic cholestasis
  JOURNAL   Gastroenterology 117 (6), 1370-1379 (1999)
   PUBMED   10579978
REFERENCE   7  (residues 1 to 1321)
  AUTHORS   Strautnieks,S.S., Bull,L.N., Knisely,A.S., Kocoshis,S.A., Dahl,N.,
            Arnell,H., Sokal,E., Dahan,K., Childs,S., Ling,V., Tanner,M.S.,
            Kagalwalla,A.F., Nemeth,A., Pawlowska,J., Baker,A.,
            Mieli-Vergani,G., Freimer,N.B., Gardiner,R.M. and Thompson,R.J.
  TITLE     A gene encoding a liver-specific ABC transporter is mutated in
            progressive familial intrahepatic cholestasis
  JOURNAL   Nat Genet 20 (3), 233-238 (1998)
   PUBMED   9806540
REFERENCE   8  (residues 1 to 1321)
  AUTHORS   Gerloff,T., Stieger,B., Hagenbuch,B., Madon,J., Landmann,L.,
            Roth,J., Hofmann,A.F. and Meier,P.J.
  TITLE     The sister of P-glycoprotein represents the canalicular bile salt
            export pump of mammalian liver
  JOURNAL   J Biol Chem 273 (16), 10046-10050 (1998)
   PUBMED   9545351
REFERENCE   9  (residues 1 to 1321)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
REFERENCE   10 (residues 1 to 1321)
  AUTHORS   Bull,L.N., Morotti,R. and Squires,J.E.
  TITLE     ATP8B1 Deficiency
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301474
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008177.3, AF091582.1,
            AC069137.6 and CB161524.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 21, 2002 this sequence version replaced NP_003733.1.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intra-cellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White). This protein is a member of the MDR/TAP subfamily. Members
            of the MDR/TAP subfamily are involved in multidrug resistance. The
            protein encoded by this gene is the major canalicular bile salt
            export pump in man. Mutations in this gene cause a form of
            progressive familial intrahepatic cholestases which are a group of
            inherited disorders with severe cholestatic liver disease from
            early infancy. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF091582.1, AF136523.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000650372.1/ ENSP00000497931.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..1321
                     /product="bile salt export pump"
                     /note="progressive familial intrahepatic cholestasis 2;
                     ABC member 16, MDR/TAP subfamily; sister p-glycoprotein;
                     ATP-binding cassette sub-family B member 11; ATP-binding
                     cassette, sub-family B (MDR/TAP), member 11"
                     /calculated_mol_wt=146277
     Region          16..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Region          21..1314
                     /region_name="PTZ00265"
                     /note="multidrug resistance protein (mdr1); Provisional"
                     /db_xref="CDD:240339"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17082223; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17082223; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Site            122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17082223; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17082223; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            216..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            320..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            354..374
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            586
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Region          651..672
                     /region_name="Interaction with HAX1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QY30; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Site            701
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70127; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Site            704
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Region          739..1316
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
     Site            756..776
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            795..815
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            870..890
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            891..911
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            980..1000
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            1012..1032
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            1214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     Region          1311..1314
                     /region_name="Mediates internalization from the plasma
                     membrane. /evidence=ECO:0000269|PubMed:22262466"
                     /note="propagated from UniProtKB/Swiss-Prot (O95342.2)"
     Site            1321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70127; propagated from
                     UniProtKB/Swiss-Prot (O95342.2)"
     CDS             1..1321
                     /gene="ABCB11"
                     /gene_synonym="ABC16; BRIC2; BSEP; PFIC-2; PFIC2; PGY4;
                     SPGP"
                     /coded_by="NM_003742.4:128..4093"
                     /db_xref="CCDS:CCDS46444.1"
                     /db_xref="GeneID:8647"
                     /db_xref="HGNC:HGNC:42"
                     /db_xref="MIM:603201"
ORIGIN      
        1 msdsvilrsi kkfgeendgf esdksynndk ksrlqdekkg dgvrvgffql frfssstdiw
       61 lmfvgslcaf lhgiaqpgvl lifgtmtdvf idydvelqel qipgkacvnn tivwtnssln
      121 qnmtngtrcg llniesemik fasyyagiav avlitgyiqi cfwviaaarq iqkmrkfyfr
      181 rimrmeigwf dcnsvgelnt rfsddinkin daiadqmalf iqrmtsticg fllgffrgwk
      241 ltlviisvsp ligigaatig lsvskftdye lkayakagvv adevissmrt vaafggekre
      301 veryeknlvf aqrwgirkgi vmgfftgfvw cliflcyala fwygstlvld egeytpgtlv
      361 qiflsvivga lnlgnaspcl eafatgraaa tsifetidrk piidcmsedg ykldrikgei
      421 efhnvtfhyp srpevkilnd lnmvikpgem talvgpsgag kstalqliqr fydpcegmvt
      481 vdghdirsln iqwlrdqigi veqepvlfst tiaenirygr edatmedivq aakeanaynf
      541 imdlpqqfdt lvgegggqms ggqkqrvaia ralirnpkil lldmatsald neseamvqev
      601 lskiqhghti isvahrlstv raadtiigfe hgtavergth eellerkgvy ftlvtlqsqg
      661 nqalneedik dateddmlar tfsrgsyqds lrasirqrsk sqlsylvhep plavvdhkst
      721 yeedrkdkdi pvqeevepap vrrilkfsap ewpymlvgsv gaavngtvtp lyaflfsqil
      781 gtfsipdkee qrsqingvcl lfvamgcvsl ftqflqgyaf aksgelltkr lrkfgframl
      841 gqdiawfddl rnspgalttr latdasqvqg aagsqigmiv nsftnvtvam iiafsfswkl
      901 slvilcffpf lalsgatqtr mltgfasrdk qalemvgqit nealsnirtv agigkerrfi
      961 ealetelekp fktaiqkani ygfcfafaqc imfiansasy ryggylisne glhfsyvfrv
     1021 isavvlsata lgrafsytps yakakisaar ffqlldrqpp isvyntagek wdnfqgkidf
     1081 vdckftypsr pdsqvlngls vsispgqtla fvgssgcgks tsiqllerfy dpdqgkvmid
     1141 ghdskkvnvq flrsnigivs qepvlfacsi mdnikygdnt keipmervia aakqaqlhdf
     1201 vmslpekyet nvgsqgsqls rgekqriaia raivrdpkil lldeatsald tesektvqva
     1261 ldkaregrtc iviahrlsti qnadiiavma qgvviekgth eelmaqkgay yklvttgspi
     1321 s
//
