ARHB_XENLA
ID ARHB_XENLA Reviewed; 309 AA.
AC Q67FQ3; Q6NTZ2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Low density lipoprotein receptor adapter protein 1-B {ECO:0000305};
DE AltName: Full=Autosomal recessive hypercholesterolemia protein homolog beta {ECO:0000303|PubMed:15327785};
DE Short=ARH beta {ECO:0000303|PubMed:15327785};
DE Short=xARH beta {ECO:0000303|PubMed:15327785};
GN Name=ldlrap1-b {ECO:0000305};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH LDLR AND THE
RP VITELLOGENIN RECEPTOR.
RX PubMed=12591597; DOI=10.1016/s0925-4773(02)00460-4;
RA Chen Y., Jurgens K., Hollemann T., Claussen M., Ramadori G., Pieler T.;
RT "Cell-autonomous and signal-dependent expression of liver and intestine
RT marker genes in pluripotent precursor cells from Xenopus embryos.";
RL Mech. Dev. 120:277-288(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=15327785; DOI=10.1016/j.mod.2004.05.008;
RA Zhou Y., Zhang J., King M.L.;
RT "Polarized distribution of mRNAs encoding a putative LDL receptor adaptor
RT protein, xARH (autosomal recessive hypercholesterolemia) in Xenopus
RT oocytes.";
RL Mech. Dev. 121:1249-1258(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adapter protein (clathrin-associated sorting protein (CLASP))
CC required for efficient endocytosis of the LDL receptor (LDLR). Also
CC involved in the vitellogenin receptor mediated endocytosis of nutrients
CC during oogenesis. {ECO:0000269|PubMed:12591597}.
CC -!- SUBUNIT: Interacts (via PID domain) with ldlr (via NPXY motif)
CC (PubMed:12591597). Binds to soluble clathrin trimers and to the adapter
CC protein complex 2 (AP-2, beta 2 subunit). Binds to phosphoinositides,
CC which regulate clathrin bud assembly at the cell surface. Interacts
CC with the VLDL receptor (vldlr) (By similarity). Interacts with the
CC vitellogenin receptor (PubMed:12591597). {ECO:0000250|UniProtKB:Q8C142,
CC ECO:0000269|PubMed:12591597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5SW96}.
CC -!- TISSUE SPECIFICITY: Expressed at high level during oogenesis and
CC embryogenesis. Found at low level in the adult liver and spleen. Found
CC at very low level in testis and heart. Not found in the oocyte vegetal
CC cortex.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout oogenesis. Homogeneously
CC distributed in stages I and II oocytes and only later localized
CC primarily to the vegetal cortex. Expressed in early stage embryos, but
CC expression decreases during gastrulation, reaching barely detectable
CC levels by tailbud stages.
CC -!- DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction
CC the AP-2 complex subunit AP2B1. {ECO:0000250|UniProtKB:Q5SW96}.
CC -!- DOMAIN: The PID domain mediates interaction with the NPXY
CC internalization motif of LDLR. {ECO:0000250|UniProtKB:D3ZAR1}.
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DR EMBL; AY344473; AAR05663.1; -; mRNA.
DR EMBL; BC068810; AAH68810.1; -; mRNA.
DR RefSeq; NP_001084567.1; NM_001091098.1.
DR AlphaFoldDB; Q67FQ3; -.
DR SMR; Q67FQ3; -.
DR MaxQB; Q67FQ3; -.
DR DNASU; 414519; -.
DR GeneID; 414519; -.
DR KEGG; xla:414519; -.
DR CTD; 414519; -.
DR Xenbase; XB-GENE-954266; ldlrap1.L.
DR OMA; NNSVVWE; -.
DR OrthoDB; 1531411at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 414519; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW Atherosclerosis; Cholesterol metabolism; Cytoplasm; Endocytosis;
KW Hyperlipidemia; Lipid metabolism; Reference proteome; Steroid metabolism;
KW Sterol metabolism.
FT CHAIN 1..309
FT /note="Low density lipoprotein receptor adapter protein 1-
FT B"
FT /id="PRO_0000064674"
FT DOMAIN 41..195
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 179..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..277
FT /note="AP-2 complex binding"
FT /evidence="ECO:0000250|UniProtKB:Q5SW96"
FT MOTIF 213..217
FT /note="Clathrin box"
FT /evidence="ECO:0000250|UniProtKB:Q5SW96"
FT MOTIF 258..267
FT /note="[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif"
FT /evidence="ECO:0000250|UniProtKB:Q5SW96"
FT CONFLICT 138
FT /note="E -> K (in Ref. 3; AAH68810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34241 MW; 7F0F3CB5C3B59F24 CRC64;
MDALKSAGRA IIRSPSIAKQ SWGGGKHKKL PENWTDTRET LLEGMLFHLK YLGMTLVEQP
KGEELSATAV KRIVATAKAS GKKLQKVLLK VSPRGIILYD SASNQLIENV SIYRISYCTA
DKMHDKVFAY IAQSQQNETL ECHAFLCTKR KMAQAVTLTV AQAFKVAFEF WQVSRENKDK
REKSGSDGEG ASSSQSDGSS SITSLKASAS ANLLDFEDCT KAFDVLNASD NHIEDLFRQN
STNENNNIVW ELDDGLDEAF ARLAESRTNP QVLDIGLTAN DLQSEECLSP TSWDKLELNP
AEADELFMF
