ARTN_MOUSE
ID ARTN_MOUSE Reviewed; 224 AA.
AC Q9Z0L2; Q3SXF4; Q3SXF5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Artemin;
DE Flags: Precursor;
GN Name=Artn;
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] (ISOFORM 1).
RX PubMed=9883723; DOI=10.1016/s0896-6273(00)80649-2;
RA Baloh R.H., Tansey M.G., Lampe P.A., Fahrner T.J., Enomoto H.,
RA Simburger K.S., Leitner M.L., Araki T., Johnson E.M. Jr., Milbrandt J.;
RT "Artemin, a novel member of the GDNF ligand family, supports peripheral and
RT central neurons and signals through the GFRalpha3-RET receptor complex.";
RL Neuron 21:1291-1302(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Oviduct, Spleen, and Testis;
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] (ISOFORMS 2 AND 3).
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 IN PEYER'S PATCH ORGANOGENESIS, AND INTERACTION WITH RET.
RX PubMed=17322904; DOI=10.1038/nature05597;
RA Veiga-Fernandes H., Coles M.C., Foster K.E., Patel A., Williams A.,
RA Natarajan D., Barlow A., Pachnis V., Kioussis D.;
RT "Tyrosine kinase receptor RET is a key regulator of Peyer's patch
RT organogenesis.";
RL Nature 446:547-551(2007).
CC -!- FUNCTION: Ligand for the GFR-alpha-3-RET receptor complex but can also
CC activate the GFR-alpha-1-RET receptor complex. Supports the survival of
CC sensory and sympathetic peripheral neurons in culture and also supports
CC the survival of dopaminergic neurons of the ventral mid-brain (By
CC similarity). Strong attractant of gut hematopoietic cells thus
CC promoting the formation Peyer's patch-like structures, a major
CC component of the gut-associated lymphoid tissue. {ECO:0000250,
CC ECO:0000269|PubMed:17322904}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Binds to RET.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Z0L2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0L2-2; Sequence=VSP_019338, VSP_019340;
CC Name=3;
CC IsoId=Q9Z0L2-3; Sequence=VSP_019337, VSP_019339, VSP_019340;
CC -!- SIMILARITY: Belongs to the TGF-beta family. GDNF subfamily.
CC {ECO:0000305}.
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DR EMBL; AF109402; AAC98691.1; -; mRNA.
DR EMBL; AK015393; BAB29827.1; -; mRNA.
DR EMBL; AK053914; BAC35590.1; -; mRNA.
DR EMBL; AK156507; BAE33737.1; -; mRNA.
DR EMBL; BC104328; AAI04329.1; -; mRNA.
DR EMBL; BC104329; AAI04330.1; -; mRNA.
DR CCDS; CCDS18543.1; -. [Q9Z0L2-1]
DR RefSeq; NP_001271120.1; NM_001284191.1. [Q9Z0L2-1]
DR RefSeq; NP_001271121.1; NM_001284192.1.
DR RefSeq; NP_001271122.1; NM_001284193.1. [Q9Z0L2-1]
DR RefSeq; NP_033841.1; NM_009711.4. [Q9Z0L2-1]
DR RefSeq; XP_006502753.1; XM_006502690.3. [Q9Z0L2-1]
DR RefSeq; XP_006502754.1; XM_006502691.3. [Q9Z0L2-1]
DR RefSeq; XP_006502755.1; XM_006502692.3. [Q9Z0L2-1]
DR RefSeq; XP_006502756.1; XM_006502693.3. [Q9Z0L2-1]
DR RefSeq; XP_011238721.1; XM_011240419.2. [Q9Z0L2-1]
DR AlphaFoldDB; Q9Z0L2; -.
DR SMR; Q9Z0L2; -.
DR BioGRID; 198213; 2.
DR STRING; 10090.ENSMUSP00000064521; -.
DR GlyGen; Q9Z0L2; 1 site.
DR PhosphoSitePlus; Q9Z0L2; -.
DR PaxDb; Q9Z0L2; -.
DR PeptideAtlas; Q9Z0L2; -.
DR PRIDE; Q9Z0L2; -.
DR Antibodypedia; 18382; 365 antibodies from 31 providers.
DR DNASU; 11876; -.
DR Ensembl; ENSMUST00000070816; ENSMUSP00000064521; ENSMUSG00000028539. [Q9Z0L2-1]
DR Ensembl; ENSMUST00000097913; ENSMUSP00000095526; ENSMUSG00000028539. [Q9Z0L2-1]
DR GeneID; 11876; -.
DR KEGG; mmu:11876; -.
DR UCSC; uc008ujh.2; mouse. [Q9Z0L2-1]
DR CTD; 9048; -.
DR MGI; MGI:1333791; Artn.
DR VEuPathDB; HostDB:ENSMUSG00000028539; -.
DR eggNOG; ENOG502S53F; Eukaryota.
DR GeneTree; ENSGT00950000182993; -.
DR HOGENOM; CLU_102221_0_0_1; -.
DR InParanoid; Q9Z0L2; -.
DR OMA; VTQPCCR; -.
DR OrthoDB; 1373819at2759; -.
DR PhylomeDB; Q9Z0L2; -.
DR TreeFam; TF332366; -.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-8853659; RET signaling.
DR BioGRID-ORCS; 11876; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9Z0L2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z0L2; protein.
DR Bgee; ENSMUSG00000028539; Expressed in seminiferous tubule of testis and 60 other tissues.
DR Genevisible; Q9Z0L2; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0030116; F:glial cell-derived neurotrophic factor receptor binding; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0050930; P:induction of positive chemotaxis; IDA:MGI.
DR GO; GO:0097021; P:lymphocyte migration into lymphoid organs; IMP:UniProtKB.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR GO; GO:0061146; P:Peyer's patch morphogenesis; IMP:UniProtKB.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR043401; GDNF_fam.
DR InterPro; IPR001839; TGF-b_C.
DR PANTHER; PTHR12173; PTHR12173; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Growth factor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT PROPEP 40..111
FT /evidence="ECO:0000255"
FT /id="PRO_0000240288"
FT CHAIN 112..224
FT /note="Artemin"
FT /id="PRO_0000240289"
FT REGION 43..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127..192
FT /evidence="ECO:0000250"
FT DISULFID 154..220
FT /evidence="ECO:0000250"
FT DISULFID 158..222
FT /evidence="ECO:0000250"
FT DISULFID 191
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019337"
FT VAR_SEQ 67..79
FT /note="GGHTAHLCSERTL -> AGYGGCRAQAPGR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019338"
FT VAR_SEQ 67..79
FT /note="GGHTAHLCSERTL -> GYGGCRAQAPGR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019339"
FT VAR_SEQ 80..224
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019340"
SQ SEQUENCE 224 AA; 23726 MW; 3328FB794581DF0B CRC64;
MELGLAEPTA LSHCLRPRWQ SAWWPTLAVL ALLSCVTEAS LDPMSRSPAA RDGPSPVLAP
PTDHLPGGHT AHLCSERTLR PPPQSPQPAP PPPGPALQSP PAALRGARAA RAGTRSSRAR
TTDARGCRLR SQLVPVSALG LGHSSDELIR FRFCSGSCRR ARSQHDLSLA SLLGAGALRS
PPGSRPISQP CCRPTRYEAV SFMDVNSTWR TVDHLSATAC GCLG
