ID   FAM3B_MOUSE             Reviewed;         235 AA.
AC   Q9D309; O88417;
DT   19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Protein FAM3B;
DE   AltName: Full=Cytokine-like protein 2-21;
DE   AltName: Full=Pancreatic-derived factor;
DE            Short=PANDER;
DE   Flags: Precursor;
GN   Name=Fam3b; Synonyms=ORF9;
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, PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=C57BL/6J;
RX   PubMed=12160727; DOI=10.1006/geno.2002.6816;
RA   Zhu Y., Xu G., Patel A., McLaughlin M.M., Silverman C., Knecht K.A.,
RA   Sweitzer S., Li X., McDonnell P., Mirabile R., Zimmerman D., Boyce R.,
RA   Tierney L.A., Hu E., Livi G.P., Wolf B.A., Abdel-Meguid S.S., Rose G.D.,
RA   Aurora R., Hensley P., Briggs M., Young P.R.;
RT   "Cloning, expression, and initial characterization of a novel cytokine-like
RT   gene family.";
RL   Genomics 80:144-150(2002).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA   Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S.,
RA   Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.;
RT   "From PREDs and open reading frames to cDNA isolation: revisiting the human
RT   chromosome 21 transcription map.";
RL   Genomics 78:46-54(2001).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-205.
RX   PubMed=9750193; DOI=10.1101/gr.8.9.940;
RA   Cabin D.E., McKee-Johnson J.W., Matesic L.E., Wiltshire T., Rue E.E.,
RA   Mjaatvedt A.E., Huo Y.K., Korenberg J.R., Reeves R.H.;
RT   "Physical and comparative mapping of distal mouse chromosome 16. 5 p5.";
RL   Genome Res. 8:940-950(1998).
RN   [6]
RP   INDUCTION.
RX   PubMed=17962352; DOI=10.1210/en.2007-0106;
RA   Wang O., Cai K., Pang S., Wang T., Qi D., Zhu Q., Ni Z., Le Y.;
RT   "Mechanisms of glucose-induced expression of pancreatic-derived factor in
RT   pancreatic beta-cells.";
RL   Endocrinology 149:672-680(2008).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 46-235, PARTIAL PROTEIN SEQUENCE,
RP   FUNCTION, GLYCOSYLATION, DISULFIDE BONDS, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=23333428; DOI=10.1016/j.str.2012.12.009;
RA   Johansson P., Bernstrom J., Gorman T., Oster L., Backstrom S.,
RA   Schweikart F., Xu B., Xue Y., Schiavone L.H.;
RT   "FAM3B PANDER and FAM3C ILEI Represent a Distinct Class of Signaling
RT   Molecules with a Non-Cytokine-like Fold.";
RL   Structure 21:306-313(2013).
CC   -!- FUNCTION: Induces apoptosis of alpha and beta cells in a dose- and
CC       time-dependent manner. {ECO:0000269|PubMed:23333428}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Present in insulin
CC       secretory granules and likely cosecreted with insulin. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the pancreas and, to a
CC       lesser extent, in small intestine and prostate. Also detected in
CC       stomach, testis and fetal liver. In the pancreas, localized in the
CC       islets of Langerhans; in the testis, found primarily in the round
CC       spermatids; in the CNS, found in the Purkinje cell layer of the
CC       cerebellum and in nerve cell bodies of numerous brainstem nuclei.
CC   -!- INDUCTION: By glucose. {ECO:0000269|PubMed:17962352}.
CC   -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23333428}.
CC   -!- MISCELLANEOUS: It is unclear whether the N-terminus residue of the
CC       mature protein is Glu-30 or Ser-46.
CC   -!- SIMILARITY: Belongs to the FAM3 family. {ECO:0000305}.
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DR   EMBL; AF494380; AAM94281.1; -; mRNA.
DR   EMBL; AK018571; BAB31283.1; -; mRNA.
DR   EMBL; AF360358; AAL34461.1; -; mRNA.
DR   EMBL; BC048949; AAH48949.1; -; mRNA.
DR   EMBL; AF045953; AAC21456.1; -; Genomic_DNA.
DR   CCDS; CCDS37416.1; -.
DR   RefSeq; NP_065647.1; NM_020622.3.
DR   PDB; 2YOP; X-ray; 2.30 A; A/B/C=46-235.
DR   PDB; 2YOQ; X-ray; 2.35 A; A/B/C=30-235.
DR   PDBsum; 2YOP; -.
DR   PDBsum; 2YOQ; -.
DR   AlphaFoldDB; Q9D309; -.
DR   SMR; Q9D309; -.
DR   STRING; 10090.ENSMUSP00000062006; -.
DR   GlyCosmos; Q9D309; 1 site, No reported glycans.
DR   GlyGen; Q9D309; 1 site.
DR   PhosphoSitePlus; Q9D309; -.
DR   MaxQB; Q9D309; -.
DR   PaxDb; 10090-ENSMUSP00000062006; -.
DR   PeptideAtlas; Q9D309; -.
DR   ProteomicsDB; 275586; -.
DR   Antibodypedia; 2683; 336 antibodies from 29 providers.
DR   DNASU; 52793; -.
DR   Ensembl; ENSMUST00000049721.9; ENSMUSP00000062006.8; ENSMUSG00000022938.9.
DR   GeneID; 52793; -.
DR   KEGG; mmu:52793; -.
DR   UCSC; uc008adj.1; mouse.
DR   AGR; MGI:1270150; -.
DR   MGI; MGI:1270150; Fam3b.
DR   VEuPathDB; HostDB:ENSMUSG00000022938; -.
DR   eggNOG; ENOG502QW7Y; Eukaryota.
DR   GeneTree; ENSGT00950000183004; -.
DR   HOGENOM; CLU_099478_1_1_1; -.
DR   InParanoid; Q9D309; -.
DR   OMA; APRRQKC; -.
DR   OrthoDB; 5350600at2759; -.
DR   PhylomeDB; Q9D309; -.
DR   TreeFam; TF353414; -.
DR   BioGRID-ORCS; 52793; 2 hits in 75 CRISPR screens.
DR   ChiTaRS; Fam3b; mouse.
DR   PRO; PR:Q9D309; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9D309; Protein.
DR   Bgee; ENSMUSG00000022938; Expressed in mucosa of stomach and 58 other cell types or tissues.
DR   ExpressionAtlas; Q9D309; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005641; C:nuclear envelope lumen; ISO:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; NAS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0030073; P:insulin secretion; IDA:UniProtKB.
DR   CDD; cd13939; PANDER_FAM3B; 1.
DR   InterPro; IPR039220; FAM3.
DR   InterPro; IPR039477; ILEI/PANDER_dom.
DR   PANTHER; PTHR14592:SF2; PROTEIN FAM3B; 1.
DR   PANTHER; PTHR14592; UNCHARACTERIZED FAM3; 1.
DR   Pfam; PF15711; ILEI; 1.
DR   PROSITE; PS52031; GG_LECTIN; 1.
DR   Genevisible; Q9D309; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Cytokine; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Lectin; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..235
FT                   /note="Protein FAM3B"
FT                   /id="PRO_0000008751"
FT   DOMAIN          72..233
FT                   /note="GG-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01375"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..91
FT                   /evidence="ECO:0000269|PubMed:23333428"
FT   DISULFID        69..229
FT                   /evidence="ECO:0000269|PubMed:23333428"
FT   CONFLICT        162
FT                   /note="K -> R (in Ref. 5; AAC21456)"
FT                   /evidence="ECO:0000305"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   TURN            100..103
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   STRAND          107..115
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   STRAND          121..127
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   HELIX           135..144
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   STRAND          147..157
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   HELIX           165..172
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   TURN            173..175
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:2YOQ"
FT   STRAND          187..196
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   TURN            212..214
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   STRAND          225..231
FT                   /evidence="ECO:0007829|PDB:2YOP"
FT   TURN            232..235
FT                   /evidence="ECO:0007829|PDB:2YOP"
SQ   SEQUENCE   235 AA;  26152 MW;  2539E5ED009D9C3C CRC64;
     MRPVATGIFK ALVFIFSSLC AWYSGYLLAE LIPDVPLSST LYNIRSIGER PVLKAPAPKR
     QKCDHWSPCP PDTYAYRLLS GGGRDKYAKI CFEDEVLIGE KTGNVARGIN IAVVNYETGK
     VIATKYFDMY EGDNSGPMAK FIQSTPSKSL LFMVTHDDGS SKLKAQAKDA IEALGSKEIK
     NMKFRSSWVF VAAKGFELPS EIEREKINHS DQSRNRYAGW PAEIQIEGCI PKGLR
//