KDF1_RAT
ID KDF1_RAT Reviewed; 397 AA.
AC Q6AY88;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Keratinocyte differentiation factor 1;
GN Name=Kdf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plays a role in the regulation of the epidermis formation
CC during early development. Required both as an inhibitor of basal cell
CC proliferation and a promoter of differentiation of basal progenitor
CC cell progeny (By similarity). {ECO:0000250|UniProtKB:A2A9F4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2A9F4}. Cell
CC junction {ECO:0000250|UniProtKB:A2A9F4}. Note=Localized at cell borders
CC in single layered keratinocytes. Localized at cell borders in the basal
CC and spinous layers but is more diffusely localized in the granular
CC layer. Colocalized with actin near the cell membrane, especially in
CC cellular protrusions (By similarity). {ECO:0000250|UniProtKB:A2A9F4}.
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DR EMBL; BC079148; AAH79148.1; -; mRNA.
DR RefSeq; NP_001004268.1; NM_001004268.1.
DR RefSeq; XP_006239077.1; XM_006239015.3.
DR RefSeq; XP_006239078.1; XM_006239016.1.
DR RefSeq; XP_006239079.1; XM_006239017.3.
DR RefSeq; XP_006239080.1; XM_006239018.3.
DR AlphaFoldDB; Q6AY88; -.
DR PhosphoSitePlus; Q6AY88; -.
DR PaxDb; Q6AY88; -.
DR Ensembl; ENSRNOT00000081318; ENSRNOP00000070982; ENSRNOG00000055933.
DR GeneID; 313018; -.
DR KEGG; rno:313018; -.
DR CTD; 126695; -.
DR RGD; 1303271; Kdf1.
DR eggNOG; ENOG502QQ0M; Eukaryota.
DR GeneTree; ENSGT00390000016565; -.
DR HOGENOM; CLU_058054_2_0_1; -.
DR InParanoid; Q6AY88; -.
DR OMA; ALCFRRC; -.
DR OrthoDB; 896286at2759; -.
DR PhylomeDB; Q6AY88; -.
DR TreeFam; TF336538; -.
DR PRO; PR:Q6AY88; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000055933; Expressed in duodenum and 12 other tissues.
DR Genevisible; Q6AY88; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0048589; P:developmental growth; ISS:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR GO; GO:0003334; P:keratinocyte development; ISO:RGD.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0060887; P:limb epidermis development; ISS:UniProtKB.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; ISS:UniProtKB.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:RGD.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; ISS:UniProtKB.
DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; ISS:UniProtKB.
DR GO; GO:0010482; P:regulation of epidermal cell division; ISS:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR InterPro; IPR028003; KDF1.
DR PANTHER; PTHR35085; PTHR35085; 1.
DR Pfam; PF15551; DUF4656; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cytoplasm; Developmental protein; Differentiation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..397
FT /note="Keratinocyte differentiation factor 1"
FT /id="PRO_0000289050"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2A9F4"
SQ SEQUENCE 397 AA; 43445 MW; 0AD13E1FAF33D8D4 CRC64;
MPRPGQPRPS SGPPRLGPWE RPTELCLETN DERSQPPPGR RTRRPDPKDP GHHGPESITF
ISGSAEPANE PPTCCLLWRP WGWDWCRAAF CFRRCRDCLQ RCGACVRSCS PCLSAGDPIE
GSSEAAWAKE HNGVPPSPDR APPSRRDGQK LKTSMGSSFS YPDVKLKGIP VYPYRHATSP
VPDADSCCKE PLADPPPTRH SLPSTFTSSP RGSEEYYSFH ESDLDLPEMG SGSMSSREID
VLIFKKLTEL FSVHQIDELA KCTSDTVFLE KTSKISDLIS SITQDYHLDE QDAEGRLVRG
IIRISTRKSR SRPQTSEGRS ARSTAPAAAP DSGHETMVGS GLSQDELTVQ ISQETTADAI
ARKLRPYGAP GYPASQDSSF QGTDTDSSGA PLLQVYC
