ID   TF2L1_PONAB             Reviewed;         457 AA.
AC   Q5RB16;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Transcription factor CP2-like protein 1;
GN   Name=TFCP2L1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that facilitates establishment and
CC       maintenance of pluripotency in embryonic stem cells (ESCs) (By
CC       similarity). With KLF2, acts as the major effector of self-renewal that
CC       mediates induction of pluripotency downstream of LIF/STAT3 and
CC       Wnt/beta-catenin signaling (By similarity). Required for normal duct
CC       development in the salivary gland and kidney (By similarity).
CC       Coordinates the development of the kidney collecting ducts intercalated
CC       (IC) and principal (PC) cells, which regulate acid-base and salt-water
CC       homeostasis, respectively (By similarity). Regulates the expression of
CC       IC genes including subunits B1 and D2 of the V-ATPase complex, OXGR1,
CC       CA12, SLC4A1, AQP6 and IC-specific transcription factor FOXI1 (By
CC       similarity). Regulates also the expression of JAG1 and subsequent notch
CC       signaling in the collecting duct (By similarity). JAG1 initiates notch
CC       signaling in PCs but inhibits notch signaling in ICs (By similarity).
CC       Acts as a transcriptional suppressor that may suppress UBP1-mediated
CC       transcriptional activation (By similarity). Modulates the placental
CC       expression of CYP11A1 (By similarity). {ECO:0000250|UniProtKB:Q3UNW5}.
CC   -!- SUBUNIT: Forms homohexamers via its SAM-like domain (By similarity).
CC       Interacts with MTA1; which is indispensable for TFCP2L1-mediated self-
CC       renewal-promoting effect and endoderm-inhibiting action (By
CC       similarity). {ECO:0000250|UniProtKB:Q3UNW5,
CC       ECO:0000250|UniProtKB:Q9NZI6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NZI6}.
CC   -!- DOMAIN: The Grh/CP2 DB domain is required for direct DNA-binding (By
CC       similarity). The Grh/CP2 DB domain is essential to maintain the
CC       undifferentiated state of embryonic stem cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q3UNW5, ECO:0000250|UniProtKB:Q9NZI6}.
CC   -!- DOMAIN: The SAM-like domain is required for homohexamerization (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NZI6}.
CC   -!- SIMILARITY: Belongs to the grh/CP2 family. CP2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR858843; CAH91044.1; -; mRNA.
DR   RefSeq; NP_001125604.1; NM_001132132.1.
DR   AlphaFoldDB; Q5RB16; -.
DR   SMR; Q5RB16; -.
DR   STRING; 9601.ENSPPYP00000014259; -.
DR   GeneID; 100172521; -.
DR   KEGG; pon:100172521; -.
DR   CTD; 29842; -.
DR   eggNOG; KOG4091; Eukaryota.
DR   InParanoid; Q5RB16; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd09590; SAM_LBP9; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR007604; CP2.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041418; SAM_3.
DR   InterPro; IPR037598; TFCP2L1_SAM.
DR   Pfam; PF04516; CP2; 1.
DR   Pfam; PF18016; SAM_3; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS51968; GRH_CP2_DB; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..457
FT                   /note="Transcription factor CP2-like protein 1"
FT                   /id="PRO_0000228008"
FT   DOMAIN          43..280
FT                   /note="Grh/CP2 DB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01313"
FT   REGION          1..52
FT                   /note="Mediate transcriptional repression"
FT   REGION          219..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..365
FT                   /note="SAM2-like domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZI6"
FT   REGION          271..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  52041 MW;  E1D6D42462C2F57A CRC64;
     MLFWHTQPEH YNQHNSGSYL RDVLALPIFK QEEPQLSPEN EARLPPLQYV LCAATSPAVK
     LHEETLTYLN QGQSYEIRLL ENRKLGDFQD LNTKYVKSII RVVFNDRRLQ YTEHQQLEGW
     RWSRPGDRIL DIDIPLSVGI LDPRASPTQL NAVEFLWDPA KRASAFIQVH CISTEFTPRK
     HGGEKGVPFR VQIDTFKQNE NGEYTEHLHS ASCQIKVFKP KGADRKQETD REKMEKRTAQ
     EKEKYQPSYE TTILTECSPW PDVAYQVNSA PSPSYNGSPN SFGLGEGNAS PTHPVEALPV
     GSDHLLPSAS IQDAQQWLHR NRFSQFCRLF ASFSGADLLK MSRDDLVQIC GPADGIRLFN
     AIKGRNVRPK MTIYVCQELE QNRVPLQQKR DGSGDSNLCV YHAIFLEELT TLDLIEKIAN
     LYSISPQHIH RVYRQGPTGI HVVVSNELRA MTATTSS