NHRF3_MOUSE
ID NHRF3_MOUSE Reviewed; 519 AA.
AC Q9JIL4; Q8CDP5; Q8R4G2; Q9CQ72;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 171.
DE RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF3;
DE Short=NHERF-3;
DE AltName: Full=CFTR-associated protein of 70 kDa;
DE AltName: Full=Na(+)/H(+) exchanger regulatory factor 3;
DE AltName: Full=Na/Pi cotransporter C-terminal-associated protein 1;
DE Short=NaPi-Cap1;
DE AltName: Full=PDZ domain-containing protein 1;
DE AltName: Full=Sodium-hydrogen exchanger regulatory factor 3;
GN Name=Pdzk1; Synonyms=Cap70, Nherf3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 351-376 AND 467-485,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP CFTR.
RX PubMed=11051556; DOI=10.1016/s0092-8674(00)00096-9;
RA Wang S., Yue H., Derin R.B., Guggino W.B., Li M.;
RT "Accessory protein facilitated CFTR-CFTR interaction, a molecular mechanism
RT to potentiate the chloride channel activity.";
RL Cell 103:169-179(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12556478; DOI=10.1128/mcb.23.4.1175-1180.2003;
RA Kocher O., Pal R., Roberts M., Cirovic C., Gilchrist A.;
RT "Targeted disruption of the PDZK1 gene by homologous recombination.";
RL Mol. Cell. Biol. 23:1175-1180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP INTERACTION WITH SLC17A1.
RX PubMed=11099500; DOI=10.1074/jbc.m008745200;
RA Gisler S.M., Stagljar I., Traebert M., Bacic D., Biber J., Murer H.;
RT "Interaction of the type IIa Na/Pi-cotransporter with PDZ proteins.";
RL J. Biol. Chem. 276:9206-9213(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH AKAP2; SLC22A12; SLC22A4; SLC26A6; SLC9A3R1;
RP SLC9A3R2 AND PDZK1IP1.
RX PubMed=14531806; DOI=10.1046/j.1523-1755.2003.00266.x;
RA Gisler S.M., Pribanic S., Bacic D., Forrer P., Gantenbein A.,
RA Sabourin L.A., Tsuji A., Zhao Z.-S., Manser E., Biber J., Murer H.;
RT "PDZK1: I. a major scaffolder in brush borders of proximal tubular cells.";
RL Kidney Int. 64:1733-1745(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH SLC22A5.
RX PubMed=15523054; DOI=10.1124/mol.104.002212;
RA Kato Y., Sai Y., Yoshida K., Watanabe C., Hirata T., Tsuji A.;
RT "PDZK1 directly regulates the function of organic cation/carnitine
RT transporter OCTN2.";
RL Mol. Pharmacol. 67:734-743(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16141316; DOI=10.1073/pnas.0506578102;
RA Thomson R.B., Wang T., Thomson B.R., Tarrats L., Girardi A., Mentone S.,
RA Soleimani M., Kocher O., Aronson P.S.;
RT "Role of PDZK1 in membrane expression of renal brush border ion
RT exchangers.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13331-13336(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-488; SER-489; SER-492 AND
RP SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-192; SER-250;
RP SER-334; SER-348; THR-451; SER-489; SER-492; THR-503; SER-508; SER-510;
RP SER-511; SER-512 AND SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP STRUCTURE BY NMR OF 242-331.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the third PDZ domain of PDZ domain containing
RT protein 1.";
RL Submitted (DEC-2006) to the PDB data bank.
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 7-106, INTERACTION WITH SCARB1,
RP FUNCTION, AND MUTAGENESIS OF LYS-14 AND TYR-20.
RX PubMed=20739281; DOI=10.1074/jbc.m110.164418;
RA Kocher O., Birrane G., Tsukamoto K., Fenske S., Yesilaltay A., Pal R.,
RA Daniels K., Ladias J.A., Krieger M.;
RT "In vitro and in vivo analysis of the binding of the C terminus of the HDL
RT receptor scavenger receptor class B, type I (SR-BI), to the PDZ1 domain of
RT its adaptor protein PDZK1.";
RL J. Biol. Chem. 285:34999-35010(2010).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 238-323 IN COMPLEX WITH SCARB1,
RP INTERACTION WITH SCARB1, MUTAGENESIS OF TYR-20 AND TYR-253, AND FUNCTION.
RX PubMed=21602281; DOI=10.1074/jbc.m111.242362;
RA Kocher O., Birrane G., Yesilaltay A., Shechter S., Pal R., Daniels K.,
RA Krieger M.;
RT "Identification of the PDZ3 domain of the adaptor protein PDZK1 as a
RT second, physiologically functional binding site for the C terminus of the
RT high density lipoprotein receptor scavenger receptor class B type I.";
RL J. Biol. Chem. 286:25171-25186(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 7-106 IN COMPLEX WITH PTGIR, AND
RP INTERACTION WITH PTGIR.
RX PubMed=23457445; DOI=10.1371/journal.pone.0053819;
RA Birrane G., Mulvaney E.P., Pal R., Kinsella B.T., Kocher O.;
RT "Molecular analysis of the prostacyclin receptor's interaction with the
RT PDZ1 domain of its adaptor protein PDZK1.";
RL PLoS ONE 8:E53819-E53819(2013).
CC -!- FUNCTION: A scaffold protein that connects plasma membrane proteins and
CC regulatory components, regulating their surface expression in
CC epithelial cells apical domains. May be involved in the coordination of
CC a diverse range of regulatory processes for ion transport and second
CC messenger cascades. In complex with SLC9A3R1, may cluster proteins that
CC are functionally dependent in a mutual fashion and modulate the
CC trafficking and the activity of the associated membrane proteins. May
CC play a role in the cellular mechanisms associated with multidrug
CC resistance through its interaction with ABCC2 and PDZK1IP1. May
CC potentiate the CFTR chloride channel activity (By similarity). Required
CC for normal cell-surface expression of SCARB1. Plays a role in
CC maintaining normal plasma cholesterol levels via its effects on SCARB1.
CC Plays a role in the normal localization and function of the chloride-
CC anion exchanger SLC26A6 to the plasma membrane in the brush border of
CC the proximal tubule of the kidney. May be involved in the regulation of
CC proximal tubular Na(+)-dependent inorganic phosphate cotransport
CC therefore playing an important role in tubule function. {ECO:0000250,
CC ECO:0000269|PubMed:11051556, ECO:0000269|PubMed:12556478,
CC ECO:0000269|PubMed:14531806, ECO:0000269|PubMed:15523054,
CC ECO:0000269|PubMed:16141316, ECO:0000269|PubMed:20739281,
CC ECO:0000269|PubMed:21602281}.
CC -!- SUBUNIT: Interacts with PDZK1IP1 and ABCC2. Binds to the C-terminal
CC region of SLC26A3. Interacts (via C-terminal PDZ domain) with SLC26A6
CC (via C-terminal domain). Interacts (via C-terminal PDZ domain) with
CC SLC9A3 (via C-terminal domain) (By similarity). Component of a complex,
CC composed of PDZK1, SYNGAP1, KLHL17 and NMDA receptors. Interacts (via
CC PDZ1 domain) directly with KLHL17; the interaction is important for
CC integrity of actin cytoskeleton structures in neurons (By similarity).
CC Forms a heterodimeric complex with SLC9A3R1. Interacts with AKAP2, BCR,
CC CFTR, SLCO1A1, SLC22A12, SLC22A4, SLC22A5, SLC26A6, SLC9A3R2 and
CC SLC17A1. Interacts (via the first PDZ domain) with PTGIR (via non-
CC isoprenylated C-terminus). Interacts (via PDZ domains 1 and 3) with
CC SCARB1 (C-terminal domain). {ECO:0000250, ECO:0000269|PubMed:11051556,
CC ECO:0000269|PubMed:11099500, ECO:0000269|PubMed:14531806,
CC ECO:0000269|PubMed:15523054, ECO:0000269|PubMed:20739281,
CC ECO:0000269|PubMed:21602281, ECO:0000269|PubMed:23457445}.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9JJ40}. Cell membrane
CC {ECO:0000269|PubMed:11051556, ECO:0000269|PubMed:16141316}.
CC Note=Localized in the brush border membrane of renal proximal tubule
CC cells (PubMed:11051556, PubMed:16141316). Associated with peripheral
CC membranes (By similarity). Localizes to the apical compartment of
CC proximal cells and to sinusoidal liver membranes (By similarity).
CC {ECO:0000250|UniProtKB:Q9JJ40, ECO:0000269|PubMed:11051556,
CC ECO:0000269|PubMed:16141316}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, small intestine. brain,
CC lung, and testis (at protein level). {ECO:0000269|PubMed:11051556,
CC ECO:0000269|PubMed:12556478}.
CC -!- DOMAIN: The PDZ 2 and 3 domains seem to be involved in the interaction
CC with SLC26A3. {ECO:0000250}.
CC -!- DOMAIN: Interaction with the C-terminus of CFTR could be mediated
CC through independent binding of PDZ 1, 3 and 4 domains.
CC -!- DOMAIN: The PDZ 1 and 3 domains seem to be involved in the interaction
CC with SLCO1A1. {ECO:0000250}.
CC -!- DOMAIN: The PDZ 1 domain interacts with BCR. {ECO:0000250}.
CC -!- DOMAIN: The PDZ 2 and 4 domains do not interact with the C-terminal
CC region of SCARB1.
CC -!- MISCELLANEOUS: Disruption of the gene was not associated with abnormal
CC growth and development or redistribution of interacting proteins.
CC However, a modulation of expression of selective ion channels in the
CC kidney, as well as increased serum cholesterol levels were observed.
CC -!- SIMILARITY: Belongs to the NHER family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL84634.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC26605.1; Type=Frameshift; Note=The frameshift causes a read through of the stop codon.; Evidence={ECO:0000305};
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DR EMBL; AF474247; AAL84634.1; ALT_FRAME; mRNA.
DR EMBL; AF220100; AAF73863.1; -; mRNA.
DR EMBL; AK006269; BAB24493.1; -; mRNA.
DR EMBL; AK029752; BAC26598.1; -; mRNA.
DR EMBL; AK029764; BAC26605.1; ALT_FRAME; mRNA.
DR EMBL; AK012070; BAB28007.1; -; mRNA.
DR EMBL; AK014879; BAB29600.1; -; mRNA.
DR EMBL; BC013512; AAH13512.1; -; mRNA.
DR CCDS; CCDS17649.1; -.
DR RefSeq; NP_001139473.1; NM_001146001.1.
DR RefSeq; NP_067492.2; NM_021517.2.
DR RefSeq; XP_006501896.1; XM_006501833.2.
DR RefSeq; XP_011238480.1; XM_011240178.2.
DR RefSeq; XP_017175164.1; XM_017319675.1.
DR PDB; 2D90; NMR; -; A=242-330.
DR PDB; 2EDZ; NMR; -; A=1-107.
DR PDB; 3NGH; X-ray; 1.80 A; A/B=7-106.
DR PDB; 3R68; X-ray; 1.30 A; A=238-323.
DR PDB; 3R69; X-ray; 1.50 A; A/B=241-322.
DR PDB; 4F8K; X-ray; 1.70 A; A/B=7-106.
DR PDB; 4R2Z; X-ray; 1.70 A; A/B=375-459.
DR PDBsum; 2D90; -.
DR PDBsum; 2EDZ; -.
DR PDBsum; 3NGH; -.
DR PDBsum; 3R68; -.
DR PDBsum; 3R69; -.
DR PDBsum; 4F8K; -.
DR PDBsum; 4R2Z; -.
DR AlphaFoldDB; Q9JIL4; -.
DR SMR; Q9JIL4; -.
DR BioGRID; 208488; 7.
DR CORUM; Q9JIL4; -.
DR IntAct; Q9JIL4; 5.
DR MINT; Q9JIL4; -.
DR STRING; 10090.ENSMUSP00000102685; -.
DR iPTMnet; Q9JIL4; -.
DR PhosphoSitePlus; Q9JIL4; -.
DR SwissPalm; Q9JIL4; -.
DR jPOST; Q9JIL4; -.
DR MaxQB; Q9JIL4; -.
DR PaxDb; Q9JIL4; -.
DR PeptideAtlas; Q9JIL4; -.
DR PRIDE; Q9JIL4; -.
DR ProteomicsDB; 252891; -.
DR DNASU; 59020; -.
DR GeneID; 59020; -.
DR KEGG; mmu:59020; -.
DR UCSC; uc008qoi.2; mouse.
DR CTD; 5174; -.
DR MGI; MGI:1928901; Pdzk1.
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; Q9JIL4; -.
DR OrthoDB; 880632at2759; -.
DR PhylomeDB; Q9JIL4; -.
DR TreeFam; TF350449; -.
DR BioGRID-ORCS; 59020; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Pdzk1; mouse.
DR EvolutionaryTrace; Q9JIL4; -.
DR PRO; PR:Q9JIL4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JIL4; protein.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005903; C:brush border; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR GO; GO:0005124; F:scavenger receptor binding; ISO:MGI.
DR GO; GO:0015879; P:carnitine transport; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:1904064; P:positive regulation of cation transmembrane transport; ISO:MGI.
DR GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:1905477; P:positive regulation of protein localization to membrane; ISO:MGI.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0044070; P:regulation of anion transport; IMP:UniProtKB.
DR Gene3D; 2.30.42.10; -; 4.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 4.
DR SMART; SM00228; PDZ; 4.
DR SUPFAM; SSF50156; SSF50156; 4.
DR PROSITE; PS50106; PDZ; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..519
FT /note="Na(+)/H(+) exchange regulatory cofactor NHE-RF3"
FT /id="PRO_0000058288"
FT DOMAIN 9..90
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 128..215
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 243..323
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 378..458
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 348..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JJ40"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 451
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 503
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MUTAGEN 14
FT /note="K->A: Impairs interaction of the first PDZ domain
FT with SCARB1."
FT /evidence="ECO:0000269|PubMed:20739281"
FT MUTAGEN 20
FT /note="Y->A: Disrupts interaction of the first PDZ domain
FT with SCARB1. Abolishes interaction with SCARB1; when
FT associated with A-253."
FT /evidence="ECO:0000269|PubMed:20739281,
FT ECO:0000269|PubMed:21602281"
FT MUTAGEN 253
FT /note="Y->A: Disrupts interaction of the third PDZ domain
FT with SCARB1. Abolishes interaction with SCARB1; when
FT associated with A-20."
FT /evidence="ECO:0000269|PubMed:21602281"
FT CONFLICT 24
FT /note="L -> R (in Ref. 1; AAL84634)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="L -> S (in Ref. 1; AAL84634)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="D -> N (in Ref. 3; BAB24493/BAC26598/BAC26605/
FT BAB28007/BAB29600)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="D -> S (in Ref. 1; AAL84634)"
FT /evidence="ECO:0000305"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:4F8K"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:4F8K"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4F8K"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:4F8K"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4F8K"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2EDZ"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:4F8K"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:4F8K"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:4F8K"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:4F8K"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4F8K"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3NGH"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:3R68"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3R69"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:3R68"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:3R68"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:3R68"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:3R68"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:3R68"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:3R68"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:3R68"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:4R2Z"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:4R2Z"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:4R2Z"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:4R2Z"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:4R2Z"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:4R2Z"
FT STRAND 448..455
FT /evidence="ECO:0007829|PDB:4R2Z"
SQ SEQUENCE 519 AA; 56499 MW; 681B57F4E237BC28 CRC64;
MASTFNPREC KLSKQEGQNY GFFLRIEKDT DGHLIRVIEE GSPAEKAGLL DGDRVLRING
VFVDKEEHAQ VVELVRKSGN SVTLLVLDGD SYEKAVKNQV DLKELDQSQR EAALNDKKPG
PGMNGAVEPC AQPRLCYLVK EGNSFGFSLK TIQGKKGVYL TDIMPQGVAM KAGVLADDHL
IEVNGENVEN ASHEEVVEKV TKSGSRIMFL LVDKETARCH SEQKTQFKRE TASLKLLPHQ
PRVVVIKKGS NGYGFYLRAG PEQKGQIIKD IEPGSPAEAA GLKNNDLVVA VNGKSVEALD
HDGVVEMIRK GGDQTTLLVL DKEAESIYSL ARFSPLLYCQ SQELPNGSVK EGPAPIPAPL
EATGSEPTED AEGHKPKLCR LLKEDDSYGF HLNAIRGQPG SFVKEVQQGG PADKAGLENE
DVIIEVNGEN VQEEPYDRVV ERIKSSGKHV TLLVCGKMAY SYFQAKKIPI VSSMAEPLVA
GPDEKGETSA ESEHDAHPAK DRTLSTASHS SSNSEDTEM
