ID   IF_CANLF                Reviewed;         417 AA.
AC   Q5XWD5;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   AltName: Full=Pancreatic intrinsic factor;
DE   Flags: Precursor;
GN   Name=CBLIF; Synonyms=GIF;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Fyfe J.C., Gearhart P.;
RT   "cDNA sequence of canine pancreatic intrinsic factor.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins
CC       family. {ECO:0000305}.
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DR   EMBL; AY730674; AAU44784.1; -; mRNA.
DR   RefSeq; NP_001005759.1; NM_001005759.1.
DR   AlphaFoldDB; Q5XWD5; -.
DR   SMR; Q5XWD5; -.
DR   STRING; 9615.ENSCAFP00000015184; -.
DR   PaxDb; Q5XWD5; -.
DR   Ensembl; ENSCAFT00845034354; ENSCAFP00845026895; ENSCAFG00845019472.
DR   GeneID; 449477; -.
DR   KEGG; cfa:449477; -.
DR   CTD; 2694; -.
DR   VEuPathDB; HostDB:ENSCAFG00845019472; -.
DR   VGNC; VGNC:41212; CBLIF.
DR   eggNOG; ENOG502RXIA; Eukaryota.
DR   GeneTree; ENSGT00530000063370; -.
DR   InParanoid; Q5XWD5; -.
DR   OrthoDB; 1233171at2759; -.
DR   Proteomes; UP000002254; Chromosome 21.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR   GO; GO:0031419; F:cobalamin binding; IBA:GO_Central.
DR   GO; GO:0015889; P:cobalamin transport; IBA:GO_Central.
DR   GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002157; Cbl-bd_prot.
DR   InterPro; IPR027954; DUF4430.
DR   Pfam; PF01122; Cobalamin_bind; 1.
DR   Pfam; PF14478; DUF4430; 1.
DR   PROSITE; PS00468; COBALAMIN_BINDING; 1.
PE   2: Evidence at transcript level;
KW   Cobalt; Cobalt transport; Disulfide bond; Glycoprotein; Ion transport;
KW   Phosphoprotein; Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..417
FT                   /note="Cobalamin binding intrinsic factor"
FT                   /id="PRO_0000005557"
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:0000250|UniProtKB:P17267"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  44982 MW;  E94323452E889C16 CRC64;
     MAWFSLHLLH LLWAAAGTST WARSSCSVPQ AAQHLVDGLQ VLLEDSVSSA APPNPSVLIA
     MNLAGALSAE ARELLADRLG ASDSAGLSVG QLALTIMALN SSCRDPGNKV SVLYGQMEAW
     PPSSPSAPAW TFYGPSLAVL ALCQEHPGRA LPVAARLAKI LAAGLSPFNT DTGAMVTLAL
     TCMYNKIPEG SEEGYRTLFS QVLKDVVENI SMRIKDNGII GDVYSTGLAM QALSVTPEPP
     NKEWDCKKTM DTILKEIEQG KFHNPMSIAQ ILPSLKGKTY LDVPYVSCSP GHQVQPTLPS
     QPSPVPTSAS NITVAYTINN QLKGVELVFN ETIDVSVKDG SVLLVVLEEA QRRNPMFKFV
     TTMTSWGLVV SSINNIAESV HDRTYWQFLS GKTPLNEGVA DYTPRDHEHI TANFTQY