NEUFC_MOUSE
ID NEUFC_MOUSE Reviewed; 263 AA.
AC Q5SSH8; A0AUN6; Q0VGS6; Q8BHV3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Neuferricin;
DE AltName: Full=Cytochrome b5 domain-containing protein 2;
DE Flags: Precursor;
GN Name=Cyb5d2 {ECO:0000312|MGI:MGI:2684848};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-84 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Blood vessel, Kidney, and Retina;
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 [4]
RP HEME-BINDING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=19968755; DOI=10.1111/j.1471-4159.2009.06522.x;
RA Kimura I., Nakayama Y., Konishi M., Kobayashi T., Mori M., Ito M.,
RA Hirasawa A., Tsujimoto G., Ohta M., Itoh N., Fujimoto M.;
RT "Neuferricin, a novel extracellular heme-binding protein, promotes
RT neurogenesis.";
RL J. Neurochem. 112:1156-1167(2010).
CC -!- FUNCTION: Heme-binding protein which promotes neuronal but not
CC astrocyte differentiation. {ECO:0000269|PubMed:19968755}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19968755}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SSH8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SSH8-2; Sequence=VSP_029827;
CC -!- TISSUE SPECIFICITY: Expressed in various tissues including brain,
CC heart, adrenal gland, and kidney. In the brain, mainly expressed in
CC pyramidal cells around the CA3 region of Ammon horn in hippocampus.
CC Present in brain (at protein level). {ECO:0000269|PubMed:19968755}.
CC -!- DEVELOPMENTAL STAGE: Abundantly expressed in the developing brain, in
CC subventricular and ventricular zones of the cerebrum, where neural stem
CC cells and neural precursor cells primarily exist. Expression levels
CC gradually increase during brain development, between 14.5 dpc and P49.
CC {ECO:0000269|PubMed:19968755}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain was proven to bind heme,
CC although it lacks the conserved iron-binding His residues at position
CC 73 and 106.
CC -!- MISCELLANEOUS: Non-classical progesterone receptors involved in
CC extranuclear signaling are classified in 2 groups: the class II
CC progestin and adipoQ receptor (PAQR) family (also called mPRs) (PAQR5,
CC PAQR6, PAQR7, PAQR8 and PAQR9) and the b5-like heme/steroid-binding
CC protein family (also called MAPRs) (PGRMC1, PGRMC2, NENF and CYB5D2).
CC {ECO:0000250|UniProtKB:Q8WUJ1}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37998.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAE23849.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAE25095.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AL663082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086682; AAH86682.1; -; mRNA.
DR EMBL; BC117721; AAI17722.2; -; mRNA.
DR EMBL; AK080730; BAC37998.1; ALT_SEQ; mRNA.
DR EMBL; AK138991; BAE23849.1; ALT_SEQ; mRNA.
DR EMBL; AK142515; BAE25095.1; ALT_SEQ; mRNA.
DR CCDS; CCDS24990.2; -. [Q5SSH8-1]
DR RefSeq; NP_001020097.2; NM_001024926.3. [Q5SSH8-1]
DR AlphaFoldDB; Q5SSH8; -.
DR SMR; Q5SSH8; -.
DR STRING; 10090.ENSMUSP00000078623; -.
DR PhosphoSitePlus; Q5SSH8; -.
DR SwissPalm; Q5SSH8; -.
DR MaxQB; Q5SSH8; -.
DR PaxDb; Q5SSH8; -.
DR PeptideAtlas; Q5SSH8; -.
DR PRIDE; Q5SSH8; -.
DR ProteomicsDB; 287481; -. [Q5SSH8-1]
DR ProteomicsDB; 287482; -. [Q5SSH8-2]
DR Antibodypedia; 23235; 73 antibodies from 15 providers.
DR DNASU; 192986; -.
DR Ensembl; ENSMUST00000079681; ENSMUSP00000078623; ENSMUSG00000057778. [Q5SSH8-1]
DR Ensembl; ENSMUST00000156294; ENSMUSP00000131961; ENSMUSG00000057778. [Q5SSH8-2]
DR GeneID; 192986; -.
DR KEGG; mmu:192986; -.
DR UCSC; uc007jzi.2; mouse. [Q5SSH8-1]
DR UCSC; uc007jzj.2; mouse. [Q5SSH8-2]
DR CTD; 124936; -.
DR MGI; MGI:2684848; Cyb5d2.
DR VEuPathDB; HostDB:ENSMUSG00000057778; -.
DR eggNOG; KOG1108; Eukaryota.
DR GeneTree; ENSGT00940000160156; -.
DR HOGENOM; CLU_065455_2_0_1; -.
DR InParanoid; Q5SSH8; -.
DR OMA; GHKHYGP; -.
DR OrthoDB; 1355837at2759; -.
DR PhylomeDB; Q5SSH8; -.
DR TreeFam; TF313943; -.
DR BioGRID-ORCS; 192986; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cyb5d2; mouse.
DR PRO; PR:Q5SSH8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SSH8; protein.
DR Bgee; ENSMUSG00000057778; Expressed in hindlimb stylopod muscle and 182 other tissues.
DR Genevisible; Q5SSH8; MM.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Neurogenesis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..263
FT /note="Neuferricin"
FT /id="PRO_0000312322"
FT DOMAIN 35..134
FT /note="Cytochrome b5 heme-binding"
FT REGION 220..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029827"
FT CONFLICT 76
FT /note="G -> V (in Ref. 2; AAH86682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29162 MW; 41156B54DBF3218E CRC64;
MLRICGLGVV LSLAVAAVAV MAVWLMDWWG PRPGIRLFLP EELARYRGGP GDPGLYLALL
GRVYDVSSGR RHYEPGAHYS GFAGRDASRA FVTGDYSEAG LVDDINGLSS SEILTLHNWL
SFYEKNYVFV GRLVGRFYRK DGLPTSELTQ VEAMVTKGME ANEQEQREKQ KFPPCNSEWS
SAKGSRLWCS QKSGGVHRDW IGVPRKLYKP GAKEPHCVCV RTTGPPSDQQ DNPRHSNHGD
LDNPNLEEYT GCPPLATTCS FPL
