INSM1_XENTR
ID INSM1_XENTR Reviewed; 441 AA.
AC A4IHR5; Q0VA44;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Insulinoma-associated protein 1;
DE AltName: Full=Zinc finger protein IA-1;
GN Name=insm1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as a transcriptional regulator. Plays a role in
CC noradrenergic neuron, pancreatic and gastrointestinal endocrine cells
CC differentiation during embryonic development (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q63ZV0}.
CC -!- SIMILARITY: Belongs to the INSM1 family. {ECO:0000305}.
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DR EMBL; AAMC01092729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC121257; AAI21258.1; -; mRNA.
DR EMBL; BC135650; AAI35651.1; -; mRNA.
DR RefSeq; NP_001076827.1; NM_001083358.1.
DR AlphaFoldDB; A4IHR5; -.
DR DNASU; 779614; -.
DR GeneID; 779614; -.
DR KEGG; xtr:779614; -.
DR CTD; 3642; -.
DR Xenbase; XB-GENE-993149; insm1.
DR OrthoDB; 1306883at2759; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000040150; Expressed in neurula embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0031018; P:endocrine pancreas development; ISS:UniProtKB.
DR GO; GO:0035987; P:endodermal cell differentiation; ISS:UniProtKB.
DR GO; GO:0048732; P:gland development; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0003310; P:pancreatic A cell differentiation; ISS:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; IBA:GO_Central.
DR GO; GO:0060290; P:transdifferentiation; ISS:UniProtKB.
DR GO; GO:0003309; P:type B pancreatic cell differentiation; ISS:UniProtKB.
DR InterPro; IPR042972; INSM1/2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15065; PTHR15065; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; DNA-binding; Metal-binding;
KW Neurogenesis; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..441
FT /note="Insulinoma-associated protein 1"
FT /id="PRO_0000425457"
FT ZN_FING 258..280
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 317..339
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 372..395
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..423
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..20
FT /note="SNAG domain"
FT /evidence="ECO:0000250|UniProtKB:Q63ZV0"
FT REGION 43..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 307
FT /note="A -> V (in Ref. 2; AAI35651/AAI21258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 47965 MW; B673C7D2B3368693 CRC64;
MPKGFLVKRS RKSPPVSYRV REEEEPRGES LPGWMLLATM CPTGGAPPPC SPDRATQAPC
CSSPRPPPAG QFGNPDTVQQ ALYSPTRPVS REQRERKYLG SPVSAESFPG LGTSSEALLY
PPTGTANGHH GLALLPPVSS SSSVSRSQGK RPAPEPDSKP AAMPGTGPGA TSSSAPSKPP
AAKKTKAIRK LTFEDEVTTS PVLGLKIKEG PVEPPRPRAA SSGPRPLGEF ICQLCKEEYS
DPFSLAQHKC SRIVRVEYRC PECHKVFSCP ANLASHRRWH KPRPPVASTA QAKEEPLSDR
DTPSPGASES GSEDGLYECP RCARKFRRQA YLRKHLLSHQ AAKEPEEPGV MMFPGEEQRA
KSPPSLNAQE CHPCPVCGET FPGKSSQERH IRLLHSSQLY PCKYCPATFY SSPGLTRHIN
KCHPSENRQV ILLQVPVRPA C