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 12-OCT-2022, entry version 142. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 318 antibodies from 25 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; IDA: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 //