ID   SKI_XENLA               Reviewed;         717 AA.
AC   Q02225;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Ski oncogene;
DE   AltName: Full=Proto-oncogene c-Ski;
GN   Name=ski;
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].
RC   TISSUE=Oocyte;
RX   PubMed=8423997;
RA   Sleeman J.P., Laskey R.A.;
RT   "Xenopus c-ski contains a novel coiled-coil protein domain, and is
RT   maternally expressed during development.";
RL   Oncogene 8:67-77(1993).
CC   -!- FUNCTION: May play a role in terminal differentiation of skeletal
CC       muscle cells but not in the determination of cells to the myogenic
CC       lineage. May function in TGF-beta signaling (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: High levels of the protein are found in the lungs
CC       and ovary with intermediate levels of expression in the heart, spleen
CC       and brain. Low expression levels are found in the liver, kidney,
CC       testis, intestine and blood while no expression is found in muscle,
CC       skin, stomach, eyes or nerves.
CC   -!- DEVELOPMENTAL STAGE: The protein is expressed in oocytes as they
CC       develop. After fertilization, the level of expression remains high over
CC       the rapid cleavage stages, then decreases during the mid-blastula
CC       transition to a low level which is maintained throughout the later
CC       developmental stages.
CC   -!- SIMILARITY: Belongs to the SKI family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X68683; CAA48642.1; -; mRNA.
DR   PIR; I51644; S29923.
DR   RefSeq; NP_001080930.1; NM_001087461.1.
DR   AlphaFoldDB; Q02225; -.
DR   SMR; Q02225; -.
DR   DNASU; 394271; -.
DR   GeneID; 394271; -.
DR   KEGG; xla:394271; -.
DR   CTD; 394271; -.
DR   Xenbase; XB-GENE-6254672; ski.S.
DR   OrthoDB; 1148296at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 394271; Expressed in internal ear and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046332; F:SMAD binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.10.260.20; -; 1.
DR   Gene3D; 3.10.390.10; -; 1.
DR   InterPro; IPR014890; c-SKI_SMAD4-bd_dom.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR010919; SAND-like_dom_sf.
DR   InterPro; IPR028760; Ski.
DR   InterPro; IPR003380; SKI/SNO/DAC.
DR   InterPro; IPR037000; Ski_DNA-bd_sf.
DR   InterPro; IPR023216; Tscrpt_reg_SKI_SnoN.
DR   PANTHER; PTHR10005; PTHR10005; 1.
DR   PANTHER; PTHR10005:SF15; PTHR10005:SF15; 1.
DR   Pfam; PF08782; c-SKI_SMAD_bind; 1.
DR   Pfam; PF02437; Ski_Sno; 1.
DR   SMART; SM01046; c-SKI_SMAD_bind; 1.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF63763; SSF63763; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Nucleus; Proto-oncogene; Reference proteome; Repeat.
FT   CHAIN           1..717
FT                   /note="Ski oncogene"
FT                   /id="PRO_0000129385"
FT   REPEAT          527..550
FT                   /note="1"
FT   REPEAT          551..575
FT                   /note="2"
FT   REPEAT          576..600
FT                   /note="3"
FT   REPEAT          601..625
FT                   /note="4"
FT   REGION          415..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..625
FT                   /note="4 X 25 AA approximate tandem repeats"
FT   REGION          698..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          524..700
FT   COMPBIAS        420..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   717 AA;  80740 MW;  0B2248C79380E55F CRC64;
     METVSRSSFQ PHAGLQKTLE QFHLSSMSSL GGPAAFSARW TQDLYKKECG KEPPEPILHL
     PSQPPPVIPG GPLFMPSDRS TERCETILEG ETISCFVVGG EKRLCLPQIL NSVLRDFSLQ
     QINAVCDELH VYCSRCTADQ LEILKVMGIL PFSAPSCGLI TKTDAERLCN ALMYGGSYPP
     RCAKKSDFPP GPLELELTEG SFKVYHECFG KCRGLFVPEL YGHPSAPCIQ CLDCRLMYPP
     HKFVVHSHKA LENRTCHWGF DSANWRAYIL LARDGVGGDD ELARLGRLLE EIKEKFDYSN
     KYKRKAARLS SEPVAKKAKA DDSIIHSPSS AEKDKSSSWL RNLSNINKNA GYVHPRQRLS
     AFRPWSPAIS ANDKELSTHL PALIRDSFYN YKSFENLVAP NVALTPPVQQ KVITSPPCVP
     AVPRSTQSSG SPPQSRKRRP TAELPIVPEA PAPPVPIREE EKESETEIEV ESREECTFTS
     SLSSLSSPSF TSSSSAKELS SPGMLAPTVI NTSYEVASHN DQHCSGLEAE LEHLKQALDS
     GLDSKEAKEK FLHEVVKMRV KQEEKLNAAL QAKRSLQQEL EFLRVAKKEK LREATEAKRN
     LRKEIERLRA EHEKKMKEAN ESRLRLKREL EQARQIRVCD KGCEAGRIRV KYSAQIEELQ
     SKLQHAENDR EQLRTDLVHE REAREHLEKV VKDLQEQLWS KTSHLPSSEH TRKDIEN