ID   UBAP1_RAT               Reviewed;         502 AA.
AC   Q5XIS7;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Ubiquitin-associated protein 1;
DE            Short=UBAP-1;
GN   Name=Ubap1 {ECO:0000312|RGD:1305186};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
CC   -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular
CC       trafficking process. Binds to ubiquitinated cargo proteins and is
CC       required for the sorting of endocytic ubiquitinated cargos into
CC       multivesicular bodies (MVBs). Plays a role in the proteasomal
CC       degradation of ubiquitinated cell-surface proteins, such as EGFR and
CC       BST2. {ECO:0000250|UniProtKB:Q9NZ09}.
CC   -!- SUBUNIT: Component of an ESCRT-I complex (endosomal sorting complex
CC       required for transport I) which consists of TSG101, VPS28, VPS37A and
CC       UBAP1 in a 1:1:1:1 stoichiometry. Interacts with PTPN23. Interacts (via
CC       UBA domains) with ubiquitinated proteins.
CC       {ECO:0000250|UniProtKB:Q9NZ09}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9NZ09}. Endosome
CC       {ECO:0000250|UniProtKB:Q9NZ09}. Note=Predominantly cytosolic. Recruited
CC       to endosomes as part of the ESCRT-I complex.
CC       {ECO:0000250|UniProtKB:Q9NZ09}.
CC   -!- DOMAIN: The UMA domain mediates association with the ESCRT-I complex.
CC       {ECO:0000250|UniProtKB:Q9NZ09}.
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DR   EMBL; BC083594; AAH83594.1; -; mRNA.
DR   RefSeq; NP_001012190.1; NM_001012190.1.
DR   AlphaFoldDB; Q5XIS7; -.
DR   SMR; Q5XIS7; -.
DR   STRING; 10116.ENSRNOP00000062034; -.
DR   PhosphoSitePlus; Q5XIS7; -.
DR   PaxDb; Q5XIS7; -.
DR   PRIDE; Q5XIS7; -.
DR   Ensembl; ENSRNOT00000063849; ENSRNOP00000062034; ENSRNOG00000012004.
DR   GeneID; 362502; -.
DR   KEGG; rno:362502; -.
DR   UCSC; RGD:1305186; rat.
DR   CTD; 51271; -.
DR   RGD; 1305186; Ubap1.
DR   eggNOG; ENOG502QTJC; Eukaryota.
DR   GeneTree; ENSGT00390000008092; -.
DR   HOGENOM; CLU_041679_0_0_1; -.
DR   InParanoid; Q5XIS7; -.
DR   OMA; ETQYDFS; -.
DR   OrthoDB; 683409at2759; -.
DR   PhylomeDB; Q5XIS7; -.
DR   Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   PRO; PR:Q5XIS7; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000012004; Expressed in adult mammalian kidney and 19 other tissues.
DR   Genevisible; Q5XIS7; RN.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0000813; C:ESCRT I complex; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
DR   Gene3D; 1.20.120.1920; -; 1.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR038870; UBAP1.
DR   InterPro; IPR042575; UBAP1_C.
DR   InterPro; IPR023340; UMA.
DR   PANTHER; PTHR15960; PTHR15960; 1.
DR   SUPFAM; SSF46934; SSF46934; 2.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS51497; UMA; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endosome; Phosphoprotein; Protein transport; Reference proteome;
KW   Repeat; Transport.
FT   CHAIN           1..502
FT                   /note="Ubiquitin-associated protein 1"
FT                   /id="PRO_0000211019"
FT   DOMAIN          17..63
FT                   /note="UMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00830"
FT   DOMAIN          389..430
FT                   /note="UBA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          451..498
FT                   /note="UBA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          1..95
FT                   /note="Interaction with ESCRT-I"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ09"
FT   REGION          77..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..290
FT                   /note="Interaction with PTPN23"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ09"
FT   COMPBIAS        77..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ09"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ09"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZ09"
SQ   SEQUENCE   502 AA;  55140 MW;  B2E04C7E8C36A37F CRC64;
     MASKKLGTDF HGTFSYLDDV PFKIGDKFKT PAKVGLPIGF SLPDCLQVVR EMQYDFSLEK
     KAIEWAEDIR LIQEAQQEAE RKSEEAEAKV NSKSGPEGDS KVSFSKTHSP ATMPPPINPI
     LASLQHNNIL TPTRVSSSAT KQKVLSPPHT KADFNPADFE CEEDPFDNLE LKTIDEKEEL
     RNILVGTTGP IMAQLLDSNT PRGNSGSVLQ DEEVLASLEQ ATLDFKPLHK PNGFITLPQL
     GNCEKMSLSS KVSLPPIPTV SNIKSLSFPK LDSDDSSQKT VRLASTFHST SCLRSGASRN
     FLKPSTQSSA SELNGDHALG LSALNLNSGT EVPALTSSQM PSLSILSVCT EESSPPSTCP
     TVTPLNFSVS QVPTMPSCPQ AYLELQALSP SERQCVETVV NMGYSYDCVL RAMKKKGENI
     EQILDYLFAH GQLCEKGFDP LLVEEALEMH QCSEEKMMEF LQLMSKFKEM GFELKDIKEV
     LLLHNNDQDN ALEDLMARAE AS