ID TNF13_MOUSE Reviewed; 241 AA.
AC Q9D777; Q9ERP1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 08-NOV-2023, entry version 135.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 13;
DE AltName: Full=A proliferation-inducing ligand;
DE Short=APRIL;
DE AltName: CD_antigen=CD256;
DE Flags: Precursor;
GN Name=Tnfsf13; Synonyms=April;
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].
RC TISSUE=Lung;
RX PubMed=10973284; DOI=10.1038/79802;
RA Yu G., Boone T., Delaney J., Hawkins N., Kelley M.J., Ramakrishnan M.,
RA McCabe S., Qiu W.R., Kornuc M., Xia X.-Z., Guo J., Stolina M., Boyle W.J.,
RA Sarosi I., Hsu H., Senaldi G., Theill L.E.;
RT "APRIL and TALL-I and receptors BCMA and TACI: system for regulating
RT humoral immunity.";
RL Nat. Immunol. 1:252-256(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 MRNA].
RC STRAIN=129; TISSUE=Mammary gland;
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 [4]
RP FUNCTION, AND TRANSGENIC MICE.
RX PubMed=15488762; DOI=10.1016/j.ccr.2004.08.033;
RA Planelles L., Carvalho-Pinto C.E., Hardenberg G., Smaniotto S., Savino W.,
RA Gomez-Caro R., Alvarez-Mon M., de Jong J., Eldering E., Martinez-A C.,
RA Medema J.P., Hahne M.;
RT "APRIL promotes B-1 cell-associated neoplasm.";
RL Cancer Cell 6:399-408(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 104-241 IN COMPLEX WITH HUMAN
RP TNFRSF17, AND DISULFIDE BONDS.
RX PubMed=15542592; DOI=10.1074/jbc.m411714200;
RA Hymowitz S.G., Patel D.R., Wallweber H.J., Runyon S., Yan M., Yin J.,
RA Shriver S.K., Gordon N.C., Pan B., Skelton N.J., Kelley R.F.,
RA Starovasnik M.A.;
RT "Structures of APRIL-receptor complexes: like BCMA, TACI employs only a
RT single cysteine-rich domain for high affinity ligand binding.";
RL J. Biol. Chem. 280:7218-7227(2005).
CC -!- FUNCTION: Cytokine that binds to TNFRSF13B/TACI and to TNFRSF17/BCMA.
CC Plays a role in the regulation of tumor cell growth. May be involved in
CC monocyte/macrophage-mediated immunological processes.
CC {ECO:0000269|PubMed:15488762}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- MISCELLANEOUS: Transgenic mice develop lymphoid tumors that originate
CC from expansion of the peritoneal B-1 B-cell population. Aging
CC transgenic mice develop progressive hyperplasia in mesenteric lymph
CC nodes and Peyer patches, disorganization of affected lymphoid tissues,
CC mucosal and capsular infiltration, and eventual tumor cell infiltration
CC into non-lymphoid tissues such as kidney and liver (PubMed:15488762).
CC {ECO:0000305|PubMed:15488762}.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; AF294825; AAG22534.1; -; mRNA.
DR EMBL; AK009514; BAB26332.1; -; mRNA.
DR EMBL; BC069900; AAH69900.1; -; mRNA.
DR RefSeq; NP_001152977.1; NM_001159505.1.
DR RefSeq; NP_076006.2; NM_023517.2.
DR PDB; 1U5X; X-ray; 1.80 A; A=104-241.
DR PDB; 1U5Y; X-ray; 2.30 A; A/B/D=104-241.
DR PDB; 1U5Z; X-ray; 2.40 A; A=104-241.
DR PDB; 1XU1; X-ray; 1.90 A; A/B/D=104-241.
DR PDB; 1XU2; X-ray; 2.35 A; A/B/D=104-241.
DR PDB; 3K48; X-ray; 2.80 A; A/B/D=104-241.
DR PDBsum; 1U5X; -.
DR PDBsum; 1U5Y; -.
DR PDBsum; 1U5Z; -.
DR PDBsum; 1XU1; -.
DR PDBsum; 1XU2; -.
DR PDBsum; 3K48; -.
DR AlphaFoldDB; Q9D777; -.
DR SMR; Q9D777; -.
DR IntAct; Q9D777; 2.
DR STRING; 10090.ENSMUSP00000018896; -.
DR GlyCosmos; Q9D777; 1 site, No reported glycans.
DR GlyGen; Q9D777; 1 site.
DR PhosphoSitePlus; Q9D777; -.
DR MaxQB; Q9D777; -.
DR PaxDb; 10090-ENSMUSP00000018896; -.
DR DNASU; 69583; -.
DR GeneID; 69583; -.
DR KEGG; mmu:69583; -.
DR UCSC; uc007jrd.1; mouse.
DR AGR; MGI:1916833; -.
DR CTD; 8741; -.
DR MGI; MGI:1916833; Tnfsf13.
DR eggNOG; ENOG502SAX4; Eukaryota.
DR InParanoid; Q9D777; -.
DR OrthoDB; 5358224at2759; -.
DR PhylomeDB; Q9D777; -.
DR Reactome; R-MMU-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR BioGRID-ORCS; 69583; 3 hits in 113 CRISPR screens.
DR EvolutionaryTrace; Q9D777; -.
DR PRO; PR:Q9D777; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D777; Protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0048018; F:receptor ligand activity; IBA:GO_Central.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0002467; P:germinal center formation; IMP:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0002636; P:positive regulation of germinal center formation; IMP:MGI.
DR GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IMP:MGI.
DR GO; GO:0050776; P:regulation of immune response; IMP:MGI.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR021184; TNF_CS.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR15151; PROTEIN EIGER; 1.
DR PANTHER; PTHR15151:SF12; TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13; 1.
DR Pfam; PF00229; TNF; 1.
DR SUPFAM; SSF49842; TNF-like; 1.
DR PROSITE; PS00251; TNF_1; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Cytokine; Disulfide bond;
KW Glycoprotein; Immunity; Reference proteome; Secreted.
FT PROPEP 1..95
FT /evidence="ECO:0000250"
FT /id="PRO_0000034526"
FT CHAIN 96..241
FT /note="Tumor necrosis factor ligand superfamily member 13"
FT /id="PRO_0000034527"
FT SITE 95..96
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 187..202
FT /evidence="ECO:0000269|PubMed:15542592"
FT CONFLICT 120
FT /note="Missing (in Ref. 2; AAG22534)"
FT /evidence="ECO:0000305"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:1U5X"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1XU2"
FT STRAND 125..142
FT /evidence="ECO:0007829|PDB:1U5X"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1U5X"
FT STRAND 152..162
FT /evidence="ECO:0007829|PDB:1U5X"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1U5X"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1U5X"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1U5X"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1XU1"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:1U5X"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:1U5X"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:1U5X"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:1U5X"
SQ SEQUENCE 241 AA; 26889 MW; 4B96D03BDBC712A4 CRC64;
MPASSPGHMG GSVREPALSV ALWLSWGAVL GAVTCAVALL IQQTELQSLR REVSRLQRSG
GPSQKQGERP WQSLWEQSPD VLEAWKDGAK SRRRRAVLTQ KHKKKHSVLH LVPVNITSKA
DSDVTEVMWQ PVLRRGRGLE AQGDIVRVWD TGIYLLYSQV LFHDVTFTMG QVVSREGQGR
RETLFRCIRS MPSDPDRAYN SCYSAGVFHL HQGDIITVKI PRANAKLSLS PHGTFLGFVK
L
//
