ID A0A2Y9J3Z4_ENHLU Unreviewed; 397 AA.
AC A0A2Y9J3Z4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=CST complex subunit STN1 {ECO:0000256|ARBA:ARBA00017411, ECO:0000256|PIRNR:PIRNR036950};
DE AltName: Full=Oligonucleotide/oligosaccharide-binding fold-containing protein 1 {ECO:0000256|ARBA:ARBA00030852, ECO:0000256|PIRNR:PIRNR036950};
DE AltName: Full=Suppressor of cdc thirteen homolog {ECO:0000256|ARBA:ARBA00030039, ECO:0000256|PIRNR:PIRNR036950};
GN Name=LOC111145169 {ECO:0000313|RefSeq:XP_022355582.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022355582.1};
RN [1] {ECO:0000313|RefSeq:XP_022355582.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022355582.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the CST complex proposed to act as a specialized
CC replication factor promoting DNA replication under conditions of
CC replication stress or natural replication barriers such as the telomere
CC duplex. The CST complex binds single-stranded DNA with high affinity in
CC a sequence-independent manner, while isolated subunits bind DNA with
CC low affinity by themselves. Initially the CST complex has been proposed
CC to protect telomeres from DNA degradation. However, the CST complex has
CC been shown to be involved in several aspects of telomere replication.
CC {ECO:0000256|PIRNR:PIRNR036950}.
CC -!- SUBUNIT: Component of the CST complex. {ECO:0000256|PIRNR:PIRNR036950}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR036950}.
CC -!- SIMILARITY: Belongs to the STN1 family.
CC {ECO:0000256|ARBA:ARBA00009698}.
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DR RefSeq; XP_022355582.1; XM_022499874.1.
DR AlphaFoldDB; A0A2Y9J3Z4; -.
DR STRING; 391180.A0A2Y9J3Z4; -.
DR KEGG; elk:111145169; -.
DR OrthoDB; 593927at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:1990879; C:CST complex; IEA:InterPro.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016233; P:telomere capping; IEA:InterPro.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IEA:UniProtKB-UniRule.
DR CDD; cd04483; hOBFC1_like; 1.
DR Gene3D; 1.10.10.980; CST, Suppressor of Cdc13 homolog, complex subunit STN1, N-terminal domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR015253; CST_STN1_C.
DR InterPro; IPR042082; CST_Stn1_wHTH1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR040260; RFA2-like.
DR InterPro; IPR014647; Stn1.
DR InterPro; IPR018856; Stn1_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13989:SF33; CST COMPLEX SUBUNIT STN1; 1.
DR PANTHER; PTHR13989; REPLICATION PROTEIN A-RELATED; 1.
DR Pfam; PF10451; Stn1; 1.
DR Pfam; PF09170; STN1_2; 1.
DR PIRSF; PIRSF036950; UCP036950; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|PIRNR:PIRNR036950};
KW DNA-binding {ECO:0000256|PIRNR:PIRNR036950};
KW Nucleus {ECO:0000256|PIRNR:PIRNR036950};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|PIRNR:PIRNR036950}.
FT DOMAIN 71..134
FT /note="CST complex subunit Stn1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10451"
FT DOMAIN 231..397
FT /note="Stn1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09170"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 44988 MW; 096B586683CC3893 CRC64;
MDTAPQDPPL SDAEPFRVGC EPNPGFPMQP ESSQYEEETP SLLWGLDPVF VAFAKLYIGD
ILDLKESRQV PGVFFYKGHP IKQVEILGTV IGRREKDAFY SYGVDDSTGV INCICWKKSN
NNEASSATTA TATLGALNLT SQLKKLQDTI EQKTKIEIGD IVQIRGYVHT YREEREIRVT
TYYKVDDPVC NIQISRMLEL PRIYRKVYDQ PFRSPALEQE SSDPGALDLA NLTCLLSERA
KEFLVENKVQ TFYQQELEIV ESLMSLANQP VIHSAGPEQG DAKNDSTSKA IHSIFKNAIQ
LLQEKGFVFQ KDDGFDKLYY VTREDKELHR KIHHIIQEDC QKPNPDAEKG CHFQHILACA
RLSVSPDLSE GVLQQVLELL EDQSDIISTT EHYYTAF
//
