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UBXN1_CAEEL
ID   UBXN1_CAEEL             Reviewed;         299 AA.
AC   Q9TXH9;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=UBX domain-containing protein 1 {ECO:0000305};
GN   Name=ubxn-1 {ECO:0000312|WormBase:F23C8.4};
GN   ORFNames=F23C8.4 {ECO:0000312|WormBase:F23C8.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17498661; DOI=10.1016/j.bbrc.2007.04.163;
RA   Yamauchi S., Sasagawa Y., Ogura T., Yamanaka K.;
RT   "Differential expression pattern of UBX family genes in Caenorhabditis
RT   elegans.";
RL   Biochem. Biophys. Res. Commun. 358:545-552(2007).
RN   [3] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH CDC-48.1 AND CDC-48.2, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=20977550; DOI=10.1111/j.1365-2443.2010.01454.x;
RA   Sasagawa Y., Yamanaka K., Saito-Sasagawa Y., Ogura T.;
RT   "Caenorhabditis elegans UBX cofactors for CDC-48/p97 control
RT   spermatogenesis.";
RL   Genes Cells 15:1201-1215(2010).
CC   -!- FUNCTION: Ubiquitin-binding protein which acts as an adapter for ATPase
CC       cdc-48.1 and/or cdc-48.2, conferring substrate specificity
CC       (PubMed:20977550). Together with ubxn-2 and ubxn-3, plays a role in
CC       hermaphrodite spermatogenesis probably by promoting the degradation of
CC       sex determination terminal factor tra-1. {ECO:0000269|PubMed:20977550}.
CC   -!- SUBUNIT: Interacts with cdc-48.1 (via N-terminus) and cdc-48.2 (via N-
CC       terminus) in vitro; the interaction with cdc-48.1 is not detected in
CC       vivo. {ECO:0000269|PubMed:20977550}.
CC   -!- INTERACTION:
CC       Q9TXH9; P54811: cdc-48.1; NbExp=3; IntAct=EBI-320236, EBI-320245;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:20977550}. Note=Colocalizes with cdc-48.1 to the
CC       perinuclear region in spermatocytes. {ECO:0000269|PubMed:20977550}.
CC   -!- TISSUE SPECIFICITY: Expressed in the germline (at protein level)
CC       (PubMed:17498661, PubMed:20977550). Expressed in spermatocytes but not
CC       in mature sperm (at protein level) (PubMed:20977550). Ubiquitously
CC       expressed (PubMed:17498661). Predominantly expressed in the spermatheca
CC       (PubMed:17498661). {ECO:0000269|PubMed:17498661,
CC       ECO:0000269|PubMed:20977550}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos, L4 larvae and adults.
CC       Expressed to a lesser extent between L1 and L3 larval stages.
CC       {ECO:0000269|PubMed:17498661}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown does not cause any
CC       visible phenotype. Simultaneous RNAi-mediated knockdown of ubxn-2 and
CC       ubxn-3, causes 50 percent embryonic lethality. The surviving
CC       hermaphrodite progeny are sterile due to a lack of sperm. Abnormal
CC       accumulation of sex determination terminal factor tra-1. Germline
CC       development is normal. In males, sperm production is normal.
CC       {ECO:0000269|PubMed:20977550}.
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DR   EMBL; BX284601; CCD69888.1; -; Genomic_DNA.
DR   PIR; T33830; T33830.
DR   RefSeq; NP_490978.1; NM_058577.4.
DR   AlphaFoldDB; Q9TXH9; -.
DR   SMR; Q9TXH9; -.
DR   DIP; DIP-27462N; -.
DR   IntAct; Q9TXH9; 8.
DR   STRING; 6239.F23C8.4; -.
DR   EPD; Q9TXH9; -.
DR   PaxDb; Q9TXH9; -.
DR   PeptideAtlas; Q9TXH9; -.
DR   EnsemblMetazoa; F23C8.4.1; F23C8.4.1; WBGene00017733.
DR   GeneID; 171804; -.
DR   KEGG; cel:CELE_F23C8.4; -.
DR   UCSC; F23C8.4; c. elegans.
DR   CTD; 171804; -.
DR   WormBase; F23C8.4; CE20713; WBGene00017733; ubxn-1.
DR   eggNOG; KOG2689; Eukaryota.
DR   GeneTree; ENSGT00940000156457; -.
DR   HOGENOM; CLU_047594_1_0_1; -.
DR   InParanoid; Q9TXH9; -.
DR   OMA; TNHANGV; -.
DR   OrthoDB; 1297214at2759; -.
DR   PhylomeDB; Q9TXH9; -.
DR   Reactome; R-CEL-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   PRO; PR:Q9TXH9; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00017733; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR   GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0042006; P:masculinization of hermaphroditic germ-line; IGI:UniProtKB.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; IBA:GO_Central.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IGI:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IGI:UniProtKB.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR001012; UBX_dom.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00166; UBX; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50033; UBX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Differentiation; Reference proteome;
KW   Spermatogenesis.
FT   CHAIN           1..299
FT                   /note="UBX domain-containing protein 1"
FT                   /id="PRO_0000444373"
FT   DOMAIN          218..295
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          39..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          127..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          111..179
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   299 AA;  32909 MW;  40ECE8DD414B6B5E CRC64;
     MSIAQQLMDM GFPADKAEAA AGNNRNLDQA LDWIEKDGAG VPMETDAPAQ AAPGAADSGA
     PPVAASFKCD DCGKLLANDD AIMFHASKTK HENFSESSEA IKPLTAEEKA AKVLEIREKI
     KVHQAKKAKL EAEENREKEK KRREDGKAMI SHKEAARDRE IREAAQDRRR EKNEDEIARK
     RVLEQIRLDK EARKAKASGQ PVPEAKPAPS AAPVAPPKDY STTTLQFRLL DGQTVRQQFE
     ANEPLAMVRA WVETNHANGV PFTLMTPFPR KVFTEDDMGT PLKVLNLVPS ANVILNRAA
 
 
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