ID   LIF_NEOVI               Reviewed;         202 AA.
AC   O62728;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Leukemia inhibitory factor;
DE            Short=LIF;
DE   Flags: Precursor;
GN   Name=LIF;
OS   Neovison vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC   Neogale.
OX   NCBI_TaxID=452646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Endometrium;
RX   PubMed=9712313;
RX   DOI=10.1002/(sici)1098-2795(199809)51:1<13::aid-mrd2>3.0.co;2-z;
RA   Song J.H., Houde A., Murphy B.D.;
RT   "Cloning of leukemia inhibitory factor (LIF) and its expression in the
RT   uterus during embryonic diapause and implantation in the mink (Mustela
RT   vison).";
RL   Mol. Reprod. Dev. 51:13-21(1998).
CC   -!- FUNCTION: LIF has the capacity to induce terminal differentiation in
CC       leukemic cells. Its activities include the induction of hematopoietic
CC       differentiation in normal and myeloid leukemia cells, the induction of
CC       neuronal cell differentiation, and the stimulation of acute-phase
CC       protein synthesis in hepatocytes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the LIF/OSM family. {ECO:0000305}.
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DR   EMBL; AF048827; AAC05638.1; -; mRNA.
DR   AlphaFoldDB; O62728; -.
DR   SMR; O62728; -.
DR   Proteomes; UP000694425; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005146; F:leukemia inhibitory factor receptor binding; IEA:InterPro.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0010646; P:regulation of cell communication; IEA:UniProt.
DR   GO; GO:0023051; P:regulation of signaling; IEA:UniProt.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR003624; Leukemia_IF.
DR   InterPro; IPR001581; Leukemia_IF/oncostatin.
DR   InterPro; IPR019827; Leukemia_IF/oncostatin_CS.
DR   PANTHER; PTHR10633; PTHR10633; 1.
DR   Pfam; PF01291; LIF_OSM; 1.
DR   PRINTS; PR01883; LEUKAEMIAIF.
DR   SMART; SM00080; LIF_OSM; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00590; LIF_OSM; 1.
PE   2: Evidence at transcript level;
KW   Cytokine; Disulfide bond; Glycoprotein; Growth factor; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..202
FT                   /note="Leukemia inhibitory factor"
FT                   /id="PRO_0000017717"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..156
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..153
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..185
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   202 AA;  22114 MW;  B54DCD53F8138AFB CRC64;
     MKVLAAGVVP LLLVLHWKHG AGTPLPITPV NATCATRHPC HSNLMNQIRN QLAHVNGSAN
     ALFILYYTAQ GEPFPNNLDK LCGPNVTDFP PFHRNGTEKT RLVELYRIIA YLGASLGNIT
     RDQKVLNPNA LSLHSKLKAT ADILRGLLSN VLCRLCNKYH VAHVDVAYGP DTSGKDVFQK
     KKLGCQLLGK YKQVIAVVAQ AF