IF_RAT
ID IF_RAT Reviewed; 417 AA.
AC P17267; O35801;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cobalamin binding intrinsic factor {ECO:0000305};
DE AltName: Full=Gastric intrinsic factor {ECO:0000305};
DE AltName: Full=Intrinsic factor;
DE Short=IF;
DE Short=INF;
DE Flags: Precursor;
GN Name=Cblif {ECO:0000312|RGD:62084}; Synonyms=Gif {ECO:0000312|RGD:62084};
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 [MRNA], AND PROTEIN SEQUENCE OF 262-276 AND 384-392.
RX PubMed=3422425; DOI=10.1073/pnas.85.1.46;
RA Dieckgraefe B.K., Seetharam B., Banaszak L., Leykam J.F., Alpers D.H.;
RT "Isolation and structural characterization of a cDNA clone encoding rat
RT gastric intrinsic factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:46-50(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-170.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7490275; DOI=10.1093/oxfordjournals.jbchem.a124859;
RA Maeda M., Asahara S., Nishi T., Mushiake S., Oka T., Shimada S., Chiba T.,
RA Tohyama M., Futai M.;
RT "The rat intrinsic factor gene: its 5'-upstream region and chief cell-
RT specific transcription.";
RL J. Biochem. 117:1305-1311(1995).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Promotes absorption of the essential vitamin cobalamin (Cbl)
CC in the ileum. After interaction with CUBN, the CBLIF-cobalamin complex
CC is internalized via receptor-mediated endocytosis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CUBN (via CUB domains). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Gastric mucosa.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41361.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA08140.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J03577; AAA41361.1; ALT_INIT; mRNA.
DR EMBL; D45200; BAA08140.1; ALT_INIT; Genomic_DNA.
DR PIR; A34003; A34003.
DR RefSeq; NP_058858.1; NM_017162.3.
DR AlphaFoldDB; P17267; -.
DR SMR; P17267; -.
DR STRING; 10116.ENSRNOP00000028507; -.
DR GlyGen; P17267; 4 sites.
DR iPTMnet; P17267; -.
DR PhosphoSitePlus; P17267; -.
DR PaxDb; P17267; -.
DR GeneID; 29319; -.
DR KEGG; rno:29319; -.
DR UCSC; RGD:62084; rat.
DR CTD; 2694; -.
DR RGD; 62084; Cblif.
DR eggNOG; ENOG502RXIA; Eukaryota.
DR InParanoid; P17267; -.
DR OrthoDB; 1233171at2759; -.
DR PhylomeDB; P17267; -.
DR TreeFam; TF333092; -.
DR Reactome; R-RNO-9758881; Uptake of dietary cobalamins into enterocytes.
DR PRO; PR:P17267; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0098591; C:external side of apical plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005902; C:microvillus; ISO:RGD.
DR GO; GO:0140355; F:cargo receptor ligand activity; ISO:RGD.
DR GO; GO:0031419; F:cobalamin binding; IDA:RGD.
DR GO; GO:0019842; F:vitamin binding; TAS:RGD.
DR GO; GO:0009235; P:cobalamin metabolic process; IDA:RGD.
DR GO; GO:0015889; P:cobalamin transport; ISO:RGD.
DR GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR002157; Cbl-bd_prot.
DR Pfam; PF01122; Cobalamin_bind; 1.
DR PROSITE; PS00468; COBALAMIN_BINDING; 1.
PE 1: Evidence at protein level;
KW Cobalt; Cobalt transport; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Ion transport; Phosphoprotein; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT CHAIN 19..417
FT /note="Cobalamin binding intrinsic factor"
FT /id="PRO_0000005560"
FT BINDING 171
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 365..370
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT BINDING 386..395
FT /ligand="cob(II)alamin"
FT /ligand_id="ChEBI:CHEBI:16304"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..246
FT /evidence="ECO:0000250"
FT DISULFID 103..288
FT /evidence="ECO:0000250"
FT DISULFID 143..182
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 45956 MW; 881BF5B2C77563C3 CRC64;
MAWLSFYLLN VLWAVAGTST RAQRSCSVPP DQQPWVNGLQ LLMENSVTES DLPNPSILIA
MNLASTYNLE AQKLLTYQLM ASDSADLTNG QLALTIMALT SSCRDPGSKV SILQKNMESW
TPSNLGAESS SFYGPALAIL ALCQKNSEAT LPIAVRFAKT LMMESSPFSV DTGAVATLAL
TCMYNRIPVG SQENYRDLFG QALKVIVDNI SLRIKADGII GDIYSTGLAM QALSVTPEQP
TKEWDCEKTM YTILKEIKQG KFQNPMSIAQ ILPSLKGKTY LDVPQVTCGP DHEVPPTLTD
YPTPVPTSIS NITVIYTINN QLRGVDLLFN VTIEVSVKSG SVLLAVLEEA QRRNHMFKFE
TTMTSWGLIV SSINNIAENV KHKTYWEFLS GKTPLGEGVA YYIPFNYEHI TANFTQY
