IF_MOUSE
ID IF_MOUSE Reviewed; 417 AA.
AC P52787; Q8C5C1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
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; Synonyms=Gif {ECO:0000312|MGI:MGI:1202394};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ; TISSUE=Stomach;
RX PubMed=8253786; DOI=10.1016/s0021-9258(19)74349-x;
RA Lorenz R.G., Gordon J.I.;
RT "Use of transgenic mice to study regulation of gene expression in the
RT parietal cell lineage of gastric units.";
RL J. Biol. Chem. 268:26559-26570(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 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 -!- SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins
CC family. {ECO:0000305}.
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DR EMBL; L24192; AAA37881.1; -; Genomic_DNA.
DR EMBL; L24191; AAA37882.1; -; mRNA.
DR EMBL; AK078933; BAC37468.1; -; mRNA.
DR EMBL; CH466534; EDL41439.1; -; Genomic_DNA.
DR EMBL; BC118519; AAI18520.1; -; mRNA.
DR CCDS; CCDS29609.1; -.
DR PIR; A49684; A49684.
DR RefSeq; NP_032144.2; NM_008118.3.
DR AlphaFoldDB; P52787; -.
DR SMR; P52787; -.
DR BioGRID; 199918; 1.
DR STRING; 10090.ENSMUSP00000025585; -.
DR GlyGen; P52787; 3 sites.
DR PhosphoSitePlus; P52787; -.
DR EPD; P52787; -.
DR MaxQB; P52787; -.
DR PaxDb; P52787; -.
DR PRIDE; P52787; -.
DR ProteomicsDB; 267216; -.
DR Antibodypedia; 27824; 317 antibodies from 26 providers.
DR DNASU; 14603; -.
DR Ensembl; ENSMUST00000025585; ENSMUSP00000025585; ENSMUSG00000024682.
DR GeneID; 14603; -.
DR KEGG; mmu:14603; -.
DR UCSC; uc008gsw.1; mouse.
DR CTD; 2694; -.
DR MGI; MGI:1202394; Cblif.
DR VEuPathDB; HostDB:ENSMUSG00000024682; -.
DR eggNOG; ENOG502RXIA; Eukaryota.
DR GeneTree; ENSGT00530000063370; -.
DR HOGENOM; CLU_052188_2_0_1; -.
DR InParanoid; P52787; -.
DR OMA; AYNVEAQ; -.
DR OrthoDB; 1233171at2759; -.
DR PhylomeDB; P52787; -.
DR TreeFam; TF333092; -.
DR Reactome; R-MMU-9758881; Uptake of dietary cobalamins into enterocytes.
DR BioGRID-ORCS; 14603; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Mif; mouse.
DR PRO; PR:P52787; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P52787; protein.
DR Bgee; ENSMUSG00000024682; Expressed in epithelium of stomach and 24 other tissues.
DR Genevisible; P52787; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0098591; C:external side of apical plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0140355; F:cargo receptor ligand activity; IDA:MGI.
DR GO; GO:0031419; F:cobalamin binding; IDA:MGI.
DR GO; GO:0009235; P:cobalamin metabolic process; IDA:MGI.
DR GO; GO:0015889; P:cobalamin transport; ISO:MGI.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..417
FT /note="Cobalamin binding intrinsic factor"
FT /id="PRO_0000005559"
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 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"
FT CONFLICT 86
FT /note="D -> N (in Ref. 1; AAA37881/AAA37882)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="R -> A (in Ref. 1; AAA37881/AAA37882)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="L -> P (in Ref. 1; AAA37881/AAA37882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 45497 MW; BF38663EFC90F34A CRC64;
MAWLTLYLLS VLWAVAGTST RAQSSCSVPP DQQPWVDGLQ ALMENSVTDS DFPNPSILIA
MNLAGAYNVE AQKLLTYQLM ASDSADLTSG QLALTVMALT SSCRDPGSKV STLLKKMENW
SPSSPGAESS AFYGPGLAIL ALCQKSSEAT LPIAVRFAKT LMMEPSPFNV DTGAVATLAL
TCMYNKIPVG SQENYRDLFG QALKAIVEKI SLRIKADGII GDIYSTGLAM QALSVTPEQP
TKKWDCEKTM HTILNEIKQG KFQNPMSIAQ ILPSLKGKTY LDVPQVTCGP DHEVPPTLTD
YPTPVPTSVS NITVIYTINN QLRGVDLLFN VTIEVSVKSG SVLLAVLEEA QRKNSMFKFE
TTMTSWGLIV SSINNIAENV NHKTYWEFLS GKTPLDEGVA YYIPFNHEHI TANFTQY
