ARHA_XENLA
ID ARHA_XENLA Reviewed; 309 AA.
AC Q801G1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Low density lipoprotein receptor adapter protein 1-A {ECO:0000305};
DE AltName: Full=Autosomal recessive hypercholesterolemia protein homolog alpha {ECO:0000303|PubMed:15327785};
DE Short=ARH alpha {ECO:0000303|PubMed:15327785};
DE Short=xARH alpha {ECO:0000303|PubMed:15327785};
DE AltName: Full=Phosphotyrosine-binding protein {ECO:0000312|EMBL:AAN78447.1};
DE AltName: Full=Xcat4 {ECO:0000303|PubMed:15327785};
GN Name=ldlrap1-a {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].
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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH LDLR AND THE VITELLOGENIN RECEPTOR.
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).
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:15327785}.
CC -!- SUBUNIT: Interacts (via PID domain) with ldlr (via NPXY motif)
CC (PubMed:15327785). 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:15327785). {ECO:0000250|UniProtKB:Q5SW96,
CC ECO:0000269|PubMed:15327785}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5SW96}.
CC -!- TISSUE SPECIFICITY: Expressed at high level during oogenesis and
CC embryogenesis. Found in the oocyte vegetal cortex. Found at low level
CC in the adult liver and spleen. Found at very low level in testis and
CC heart. {ECO:0000269|PubMed:15327785}.
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; AY183756; AAN78447.1; -; mRNA.
DR EMBL; AY344472; AAR05662.1; -; mRNA.
DR RefSeq; NP_001082560.1; NM_001089091.1.
DR RefSeq; XP_018103634.1; XM_018248145.1.
DR AlphaFoldDB; Q801G1; -.
DR SMR; Q801G1; -.
DR GeneID; 398568; -.
DR KEGG; xla:398568; -.
DR CTD; 398568; -.
DR Xenbase; XB-GENE-6256035; ldlrap1.S.
DR OMA; NATHIDE; -.
DR OrthoDB; 1531411at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 398568; Expressed in oocyte 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 A"
FT /id="PRO_0000064673"
FT DOMAIN 41..195
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 179..199
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"
SQ SEQUENCE 309 AA; 34121 MW; 9805F10240D5BA5E CRC64;
MDALKSAGRA IIRSPSIAKQ SWGGGKHKKL PENWTDTRET LLEGMLFHLK YLGMTLVEQP
KGEELSATAV KRIVATAKAS GKKLQKVILK VSPRGIILYD STSNQLIENV SIYRISYCTA
DKMHDKVFAY IAQSQQNETL ECHAFLCTKR KMAQAVTLTV AQAFKVAFEF WQVSRDKTEK
REKSGSGGEG ASSSQSDGSS SITSLKASAS ANLLDLEDCT KAFDVLNASD NHIEDLFRQN
ASNENNNIVW ELDDGLDEAF ARLAESRTNP QVLDIGLTAN DLQSEECLSP SSWDKLELNP
AEADELFMF
