RETNB_MOUSE
ID RETNB_MOUSE Reviewed; 105 AA.
AC Q99P86; Q9D286;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Resistin-like beta;
DE AltName: Full=Cysteine-rich secreted protein A12-beta;
DE AltName: Full=Cysteine-rich secreted protein FIZZ2;
DE AltName: Full=RELMbeta;
DE Flags: Precursor;
GN Name=Retnlb; Synonyms=Fizz2;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11209052; DOI=10.1073/pnas.98.2.502;
RA Steppan C.M., Brown E.J., Wright C.M., Bhat S., Banerjee R.R., Dai C.Y.,
RA Enders G.H., Silberg D.G., Wen X., Wu G.D., Lazar M.A.;
RT "A family of tissue-specific resistin-like molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:502-506(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rajala M.W., Scherer P.E.;
RT "Identification of a novel cysteine-rich secreted A12-alpha related
RT protein.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP SUBUNIT, AND MUTAGENESIS OF CYS-25.
RX PubMed=11358969; DOI=10.1074/jbc.m103109200;
RA Banerjee R.R., Lazar M.A.;
RT "Dimerization of resistin and resistin-like molecules is determined by a
RT single cysteine.";
RL J. Biol. Chem. 276:25970-25973(2001).
RN [6]
RP SUBUNIT, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15834545; DOI=10.1007/s00125-005-1735-1;
RA Shojima N., Ogihara T., Inukai K., Fujishiro M., Sakoda H., Kushiyama A.,
RA Katagiri H., Anai M., Ono H., Fukushima Y., Horike N., Viana A.Y.,
RA Uchijima Y., Kurihara H., Asano T.;
RT "Serum concentrations of resistin-like molecules beta and gamma are
RT elevated in high-fat-fed and obese db/db mice, with increased production in
RT the intestinal tract and bone marrow.";
RL Diabetologia 48:984-992(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 25-105, AND DISULFIDE BONDS.
RX PubMed=15155948; DOI=10.1126/science.1093466;
RA Patel S.D., Rajala M.W., Rossetti L., Scherer P.E., Shapiro L.;
RT "Disulfide-dependent multimeric assembly of resistin family hormones.";
RL Science 304:1154-1158(2004).
CC -!- FUNCTION: Probable hormone.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:11358969, PubMed:15834545,
CC PubMed:15155948). Heterodimer with RETNLG (PubMed:15834545).
CC {ECO:0000269|PubMed:11358969, ECO:0000269|PubMed:15155948,
CC ECO:0000269|PubMed:15834545}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11209052}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in colon, and at lower levels in
CC ileum (PubMed:15834545). In colon, found throughout the crypt and
CC surface epithelium and in goblet cells (at protein level)
CC (PubMed:15834545). Specific to the gastrointestinal tract; not detected
CC in other tissues tested (PubMed:11209052, PubMed:15834545).
CC {ECO:0000269|PubMed:11209052, ECO:0000269|PubMed:15834545}.
CC -!- INDUCTION: Up-regulated in colon in response to a high-fat diet. Also
CC up-regulated in obese mice mutant for the leptin receptor LEPR (db/db
CC genotype). {ECO:0000269|PubMed:15834545}.
CC -!- SIMILARITY: Belongs to the resistin/FIZZ family. {ECO:0000305}.
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DR EMBL; AF323083; AAG59826.1; -; mRNA.
DR EMBL; AF290871; AAK83103.1; -; mRNA.
DR EMBL; AK020240; BAB32036.1; -; mRNA.
DR EMBL; BC022650; AAH22650.1; -; mRNA.
DR CCDS; CCDS28210.1; -.
DR RefSeq; NP_076370.3; NM_023881.4.
DR PDB; 1RH7; X-ray; 3.11 A; A/B/C/D/E/F=25-105.
DR PDBsum; 1RH7; -.
DR AlphaFoldDB; Q99P86; -.
DR SMR; Q99P86; -.
DR STRING; 10090.ENSMUSP00000023328; -.
DR PaxDb; Q99P86; -.
DR PRIDE; Q99P86; -.
DR ProteomicsDB; 253222; -.
DR GeneID; 57263; -.
DR KEGG; mmu:57263; -.
DR CTD; 84666; -.
DR MGI; MGI:1888505; Retnlb.
DR eggNOG; ENOG502RTZZ; Eukaryota.
DR InParanoid; Q99P86; -.
DR OrthoDB; 1541877at2759; -.
DR PhylomeDB; Q99P86; -.
DR TreeFam; TF337024; -.
DR BioGRID-ORCS; 57263; 0 hits in 71 CRISPR screens.
DR EvolutionaryTrace; Q99P86; -.
DR PRO; PR:Q99P86; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99P86; protein.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR CDD; cd16333; RELM; 1.
DR Gene3D; 2.60.40.4230; -; 1.
DR InterPro; IPR009714; RELM.
DR InterPro; IPR036262; Resistin-like_sf.
DR PANTHER; PTHR21101; PTHR21101; 1.
DR Pfam; PF06954; Resistin; 1.
DR SUPFAM; SSF111423; SSF111423; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..105
FT /note="Resistin-like beta"
FT /id="PRO_0000030346"
FT DISULFID 25
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:11358969,
FT ECO:0000269|PubMed:15155948, ECO:0007744|PDB:1RH7"
FT DISULFID 49..102
FT /evidence="ECO:0000269|PubMed:15155948,
FT ECO:0007744|PDB:1RH7"
FT DISULFID 61..101
FT /evidence="ECO:0000269|PubMed:15155948,
FT ECO:0007744|PDB:1RH7"
FT DISULFID 70..87
FT /evidence="ECO:0000269|PubMed:15155948,
FT ECO:0007744|PDB:1RH7"
FT DISULFID 72..89
FT /evidence="ECO:0000269|PubMed:15155948,
FT ECO:0007744|PDB:1RH7"
FT DISULFID 76..91
FT /evidence="ECO:0000269|PubMed:15155948,
FT ECO:0007744|PDB:1RH7"
FT MUTAGEN 25
FT /note="C->A: Fails to homodimerize."
FT /evidence="ECO:0000269|PubMed:11358969"
FT CONFLICT 15
FT /note="F -> L (in Ref. 3; BAB32036)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="A -> V (in Ref. 2; AAK83103)"
FT /evidence="ECO:0000305"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:1RH7"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1RH7"
FT STRAND 46..60
FT /evidence="ECO:0007829|PDB:1RH7"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1RH7"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1RH7"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1RH7"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:1RH7"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1RH7"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1RH7"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:1RH7"
SQ SEQUENCE 105 AA; 11278 MW; 2F5FFDA5A28B7141 CRC64;
MKPTLCFLFI LVSLFPLIVP GNAQCSFESL VDQRIKEALS RQEPKTISCT SVTSSGRLAS
CPAGMVVTGC ACGYGCGSWD IRNGNTCHCQ CSVMDWASAR CCRMA
