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Protein

Resistin-like beta

Gene

Retnlb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probable hormone.

Keywords - Molecular functioni

Hormone

Names & Taxonomyi

Protein namesi
Recommended name:
Resistin-like beta
Alternative name(s):
Cysteine-rich secreted protein A12-beta
Cysteine-rich secreted protein FIZZ2
RELMbeta
Gene namesi
Name:Retnlb
Synonyms:Fizz2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1888505. Retnlb.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 10582Resistin-like betaPRO_0000030346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 – 25Interchain1 Publication
Disulfide bondi49 ↔ 102By similarity
Disulfide bondi61 ↔ 101By similarity
Disulfide bondi70 ↔ 87By similarity
Disulfide bondi72 ↔ 89By similarity
Disulfide bondi76 ↔ 91By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ99P86.
PRIDEiQ99P86.

Expressioni

Tissue specificityi

Expressed only in the gastrointestinal tract, particularly the colon.

Gene expression databases

BgeeiQ99P86.
CleanExiMM_RETNLB.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023328.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 357Combined sources
Turni36 – 383Combined sources
Beta strandi46 – 6015Combined sources
Beta strandi66 – 727Combined sources
Helixi73 – 753Combined sources
Beta strandi79 – 824Combined sources
Turni83 – 853Combined sources
Beta strandi86 – 894Combined sources
Beta strandi91 – 933Combined sources
Beta strandi96 – 10510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH7X-ray3.11A/B/C/D/E/F25-105[»]
ProteinModelPortaliQ99P86.
SMRiQ99P86. Positions 25-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99P86.

Family & Domainsi

Sequence similaritiesi

Belongs to the resistin/FIZZ family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J40Z. Eukaryota.
ENOG410ZE8R. LUCA.
HOGENOMiHOG000137607.
HOVERGENiHBG018297.
InParanoidiQ99P86.
OrthoDBiEOG7CVQ14.
PhylomeDBiQ99P86.
TreeFamiTF337024.

Family and domain databases

InterProiIPR009714. Resistin.
[Graphical view]
PANTHERiPTHR21101. PTHR21101. 1 hit.
PfamiPF06954. Resistin. 1 hit.
[Graphical view]
SUPFAMiSSF111423. SSF111423. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99P86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPTLCFLFI LVSLFPLIVP GNAQCSFESL VDQRIKEALS RQEPKTISCT
60 70 80 90 100
SVTSSGRLAS CPAGMVVTGC ACGYGCGSWD IRNGNTCHCQ CSVMDWASAR

CCRMA
Length:105
Mass (Da):11,278
Last modified:June 1, 2001 - v1
Checksum:i2F5FFDA5A28B7141
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151F → L in BAB32036 (PubMed:16141072).Curated
Sequence conflicti105 – 1051A → V in AAK83103 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323083 mRNA. Translation: AAG59826.1.
AF290871 mRNA. Translation: AAK83103.1.
AK020240 mRNA. Translation: BAB32036.1.
BC022650 mRNA. Translation: AAH22650.1.
CCDSiCCDS28210.1.
RefSeqiNP_076370.3. NM_023881.4.
UniGeneiMm.21123.

Genome annotation databases

GeneIDi57263.
KEGGimmu:57263.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323083 mRNA. Translation: AAG59826.1.
AF290871 mRNA. Translation: AAK83103.1.
AK020240 mRNA. Translation: BAB32036.1.
BC022650 mRNA. Translation: AAH22650.1.
CCDSiCCDS28210.1.
RefSeqiNP_076370.3. NM_023881.4.
UniGeneiMm.21123.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH7X-ray3.11A/B/C/D/E/F25-105[»]
ProteinModelPortaliQ99P86.
SMRiQ99P86. Positions 25-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023328.

Proteomic databases

PaxDbiQ99P86.
PRIDEiQ99P86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi57263.
KEGGimmu:57263.

Organism-specific databases

CTDi84666.
MGIiMGI:1888505. Retnlb.

Phylogenomic databases

eggNOGiENOG410J40Z. Eukaryota.
ENOG410ZE8R. LUCA.
HOGENOMiHOG000137607.
HOVERGENiHBG018297.
InParanoidiQ99P86.
OrthoDBiEOG7CVQ14.
PhylomeDBiQ99P86.
TreeFamiTF337024.

Miscellaneous databases

EvolutionaryTraceiQ99P86.
PROiQ99P86.
SOURCEiSearch...

Gene expression databases

BgeeiQ99P86.
CleanExiMM_RETNLB.

Family and domain databases

InterProiIPR009714. Resistin.
[Graphical view]
PANTHERiPTHR21101. PTHR21101. 1 hit.
PfamiPF06954. Resistin. 1 hit.
[Graphical view]
SUPFAMiSSF111423. SSF111423. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of a novel cysteine-rich secreted A12-alpha related protein."
    Rajala M.W., Scherer P.E.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Colon.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  5. "Dimerization of resistin and resistin-like molecules is determined by a single cysteine."
    Banerjee R.R., Lazar M.A.
    J. Biol. Chem. 276:25970-25973(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "Disulfide-dependent multimeric assembly of resistin family hormones."
    Patel S.D., Rajala M.W., Rossetti L., Scherer P.E., Shapiro L.
    Science 304:1154-1158(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 25-105, DISULFIDE BONDS.

Entry informationi

Entry nameiRETNB_MOUSE
AccessioniPrimary (citable) accession number: Q99P86
Secondary accession number(s): Q9D286
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.