DSL1_CHICK
ID DSL1_CHICK Reviewed; 427 AA.
AC P34822;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Dorsalin-1;
DE Short=DSL-1;
DE Flags: Precursor;
GN Name=DSL1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 319-322.
RC TISSUE=Spinal cord;
RX PubMed=7916656; DOI=10.1016/0092-8674(93)90249-p;
RA Basler K., Edlund T., Jessell T.M., Yamada T.;
RT "Control of cell pattern in the neural tube: regulation of cell
RT differentiation by dorsalin-1, a novel TGF beta family member.";
RL Cell 73:687-702(1993).
CC -!- FUNCTION: Appears to regulate cell differentiation within the neural
CC tube. May regulate the differentiation of cell types along the
CC dorsoventral axis of the neural tube, acting in conjunction with
CC distinct ventralizing signals from the notochord and floor plate.
CC Controls the cell differentiation in the neural tube in several ways:
CC (1) promotes the differentiation of cell types that derive from the
CC dorsal neural tube. (2) ensures that the dorsal neural tube is
CC refractory to ventralizing species from the notochord. (3) can diffuse
CC and influence the fate of cells in more ventral regions of the neural
CC tube.
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed selectively in the dorsal neural tube.
CC Lower levels seen in kidney and myotomal cells.
CC -!- DEVELOPMENTAL STAGE: Is not expressed in neural cells at stages before
CC neural tube closure. Is expressed at high levels in the dorsal third of
CC the neural tube, beginning at the time of neural tube closure, but not
CC by ventral neural cells or by nonneural cells. Dorsal restriction
CC persists in the spinal cord at stages after the onset of neuronal
CC differentiation. At later stages of spinal development, is restricted
CC to the dorsomedial region of the spinal cord, including but not
CC confined to the roof plate.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; L12032; AAA48752.1; -; mRNA.
DR PIR; A40735; A40735.
DR RefSeq; NP_990763.1; NM_205432.1.
DR AlphaFoldDB; P34822; -.
DR SMR; P34822; -.
DR STRING; 9031.ENSGALP00000009606; -.
DR PaxDb; P34822; -.
DR Ensembl; ENSGALT00000009620; ENSGALP00000009606; ENSGALG00000005981.
DR GeneID; 396412; -.
DR KEGG; gga:396412; -.
DR CTD; 2658; -.
DR VEuPathDB; HostDB:geneid_396412; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000159802; -.
DR HOGENOM; CLU_020515_2_0_1; -.
DR InParanoid; P34822; -.
DR OMA; GTFDLRM; -.
DR OrthoDB; 749511at2759; -.
DR PhylomeDB; P34822; -.
DR TreeFam; TF316134; -.
DR Reactome; R-GGA-201451; Signaling by BMP.
DR PRO; PR:P34822; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000005981; Expressed in colon and 4 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Growth factor; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..318
FT /evidence="ECO:0000269|PubMed:7916656"
FT /id="PRO_0000033906"
FT CHAIN 319..427
FT /note="Dorsalin-1"
FT /id="PRO_0000033907"
FT REGION 288..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 325..391
FT /evidence="ECO:0000250"
FT DISULFID 354..424
FT /evidence="ECO:0000250"
FT DISULFID 358..426
FT /evidence="ECO:0000250"
FT DISULFID 390
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 48626 MW; 23AA42DC7085FABC CRC64;
MHYFGVLAAL SVFNIIACLT RGKPLENWKK LPVMEESDAF FHDPGEVEHD THFDFKSFLE
NMKTDLLRSL NLSRVPSQVK TKEEPPQFMI DLYNRYTADK SSIPASNIVR SFSTEDVVSL
ISPEEHSFQK HILLFNISIP RYEEVTRAEL RIFISCHKEV GSPSRLEGNM VIYDVLDGDH
WENKESTKSL LVSHSIQDCG WEMFEVSSAV KRWVKADKMK TKNKLEVVIE SKDLSGFPCG
KLDITVTHDT KNLPLLIVFS NDRSNGTKET KVELREMIVH EQESVLNKLG KNDSSSEEEQ
REEKAIARPR QHSSRSKRSI GANHCRRTSL HVNFKEIGWD SWIIAPKDYE AFECKGGCFF
PLTDNVTPTK HAIVQTLVHL QNPKKASKAC CVPTKLDAIS ILYKDDAGVP TLIYNYEGMK
VAECGCR
