INSM1_XENLA
ID INSM1_XENLA Reviewed; 433 AA.
AC A7UKY7;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Insulinoma-associated protein 1;
DE AltName: Full=Zinc finger protein IA-1;
GN Name=insm1;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18627098; DOI=10.1002/dvdy.21621;
RA Parlier D., Ariza A., Christulia F., Genco F., Vanhomwegen J., Kricha S.,
RA Souopgui J., Bellefroid E.J.;
RT "Xenopus zinc finger transcription factor IA1 (Insm1) expression marks
RT anteroventral noradrenergic neuron progenitors in Xenopus embryos.";
RL Dev. Dyn. 237:2147-2157(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19705447; DOI=10.1002/dvdy.22071;
RA Horb L.D., Jarkji Z.H., Horb M.E.;
RT "Xenopus insm1 is essential for gastrointestinal and pancreatic endocrine
RT cell development.";
RL Dev. Dyn. 238:2505-2510(2009).
CC -!- FUNCTION: May act as a transcriptional regulator (By similarity). Plays
CC a role in noradrenergic neuron, pancreatic and gastrointestinal
CC endocrine cells differentiation during embryonic development.
CC {ECO:0000250, ECO:0000269|PubMed:18627098,
CC ECO:0000269|PubMed:19705447}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q63ZV0}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed during neurogenesis in neural plate primary neurons and in
CC the anteroventral noradrenergic neurons. Expressed in the dorsal
CC endoderm, throughout the gastrointestinal tract and in the ventral and
CC dorsal pancreas from tail bud through tadpole stages.
CC {ECO:0000269|PubMed:18627098, ECO:0000269|PubMed:19705447}.
CC -!- SIMILARITY: Belongs to the INSM1 family. {ECO:0000305}.
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DR EMBL; EU076904; ABU50799.1; -; mRNA.
DR RefSeq; NP_001104189.1; NM_001110719.1.
DR AlphaFoldDB; A7UKY7; -.
DR GeneID; 100126605; -.
DR KEGG; xla:100126605; -.
DR CTD; 100126605; -.
DR Xenbase; XB-GENE-1030672; insm1.L.
DR OrthoDB; 1306883at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 100126605; Expressed in pancreas and 16 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: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; IMP:UniProtKB.
DR GO; GO:0035987; P:endodermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0048732; P:gland development; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0003310; P:pancreatic A cell differentiation; ISS:UniProtKB.
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..433
FT /note="Insulinoma-associated protein 1"
FT /id="PRO_0000425456"
FT ZN_FING 250..272
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 364..387
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..415
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..111
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 131..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..305
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"
SQ SEQUENCE 433 AA; 47581 MW; EBF2FC109FE0CF4E CRC64;
MPKGFLVKRN RKSPPVSYRV REDEENRGES LPGWMLLATM CPTGGAPPPS SPERLASAAP
SCNNPRPPPA GQFGNPEAVP QTLYSPTRPV SREQRERKYL GSPVSAESFP GLGSSSEALL
FPPTSTANGH HGLALLPPVS SSSSISRTHG KRPAPEPDVK AGAAPGTACK PPAAKKTKAI
RKLTFEDEVT TSPVLGLKIK EGPVEPPRPR APSSGPRPLG EFICQLCKEE YSDPFSLAQH
KCSRIVRVEY RCPECHKVFS CPANLASHRR WHKPRPPAVP AVQPKEEALS DRDTPSPESG
SEDGLYECPR CARKFRRQAY LRKHLLSHQV TKEPEEAGHM MYQSDEQRPQ AKSPPSLNVP
QECHPCPVCG ETFPGKSSQE RHIRLLHSSQ LYPCKYCPAT FYSSPGLTRH INKCHPSENR
QVILLQVPVR PAC
