ATRN_RAT
ID ATRN_RAT Reviewed; 1432 AA.
AC Q99J86; Q99PW0;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Attractin;
DE AltName: Full=Protein zitter;
DE Flags: Precursor;
GN Name=Atrn {ECO:0000312|RGD:69063};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAB21058.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [MRNA] (ISOFORM 2), FUNCTION, AND DISEASE.
RC STRAIN=WTC {ECO:0000312|EMBL:BAB21017.1};
RC TISSUE=Brain {ECO:0000269|PubMed:11209055};
RX PubMed=11209055; DOI=10.1073/pnas.98.2.559;
RA Kuramoto T., Kitada K., Inui T., Sasaki Y., Ito K., Hase T., Kawaguchi S.,
RA Ogawa Y., Nakao K., Barsh G.S., Nagao M., Ushijima T., Serikawa T.;
RT "Attractin/mahogany/zitter plays a critical role in myelination of the
RT central nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:559-564(2001).
CC -!- FUNCTION: Involved in the initial immune cell clustering during
CC inflammatory response and may regulate chemotactic activity of
CC chemokines (By similarity). May play a role in melanocortin signaling
CC pathways that regulate energy homeostasis and hair color. Low-affinity
CC receptor for agouti (By similarity). Has a critical role in normal
CC myelination in the central nervous system. {ECO:0000250,
CC ECO:0000269|PubMed:11209055}.
CC -!- SUBUNIT: Monomer and homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000250|UniProtKB:O75882}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:O75882}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000250|UniProtKB:O75882}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11209055};
CC IsoId=Q99J86-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11209055};
CC IsoId=Q99J86-2; Sequence=VSP_051674, VSP_051675;
CC -!- PTM: Heavily glycosylated. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Atrn (isoform 1) are the cause of the
CC autosomal recessive phenotype zitter (zi), which is characterized by
CC progressive hypomyelination and vacuolation in the central nervous
CC system resulting in early-onset tremor and progressive flaccid paresis
CC of the hind limb. This is due to an 8-bp deletion at the splice donor
CC site of intron 12, which results in aberrant and unstable transcripts.
CC {ECO:0000269|PubMed:11209055}.
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DR EMBL; AB038387; BAB21017.1; -; mRNA.
DR EMBL; AB038388; BAB21018.1; -; mRNA.
DR EMBL; AB049248; BAB21058.1; -; Genomic_DNA.
DR RefSeq; NP_112641.1; NM_031351.1. [Q99J86-1]
DR AlphaFoldDB; Q99J86; -.
DR SMR; Q99J86; -.
DR STRING; 10116.ENSRNOP00000028847; -.
DR GlyGen; Q99J86; 25 sites, 4 N-linked glycans (1 site).
DR PhosphoSitePlus; Q99J86; -.
DR SwissPalm; Q99J86; -.
DR PaxDb; Q99J86; -.
DR PRIDE; Q99J86; -.
DR GeneID; 83526; -.
DR KEGG; rno:83526; -.
DR UCSC; RGD:69063; rat. [Q99J86-1]
DR CTD; 8455; -.
DR RGD; 69063; Atrn.
DR VEuPathDB; HostDB:ENSRNOG00000021240; -.
DR eggNOG; KOG1388; Eukaryota.
DR HOGENOM; CLU_003930_0_0_1; -.
DR InParanoid; Q99J86; -.
DR OMA; EACNIAA; -.
DR OrthoDB; 49565at2759; -.
DR PhylomeDB; Q99J86; -.
DR TreeFam; TF321873; -.
DR PRO; PR:Q99J86; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000021240; Expressed in liver and 19 other tissues.
DR Genevisible; Q99J86; RN.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0043473; P:pigmentation; IMP:CACAO.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 3.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF01344; Kelch_1; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF01437; PSI; 2.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00423; PSI; 5.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Inflammatory response; Kelch repeat; Laminin EGF-like domain;
KW Lectin; Membrane; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..86
FT /evidence="ECO:0000250"
FT /id="PRO_0000394773"
FT CHAIN 87..1432
FT /note="Attractin"
FT /id="PRO_0000007485"
FT TOPO_DOM 87..1282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1283..1303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1304..1432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 100..133
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 135..251
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 249..286
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 355..405
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 406..454
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 464..511
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 516..567
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 569..627
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT REPEAT 628..674
FT /note="Kelch 6"
FT /evidence="ECO:0000255"
FT DOMAIN 706..751
FT /note="PSI 1"
FT DOMAIN 758..797
FT /note="PSI 2"
FT DOMAIN 798..922
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 935..986
FT /note="PSI 3"
FT DOMAIN 989..1064
FT /note="PSI 4"
FT DOMAIN 1066..1111
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1112..1160
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 917
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..114
FT /evidence="ECO:0000250|UniProtKB:Q9WU60"
FT DISULFID 108..121
FT /evidence="ECO:0000250|UniProtKB:Q9WU60"
FT DISULFID 123..132
FT /evidence="ECO:0000250|UniProtKB:Q9WU60"
FT DISULFID 135..161
FT /evidence="ECO:0000250"
FT DISULFID 253..263
FT /evidence="ECO:0000250"
FT DISULFID 257..274
FT /evidence="ECO:0000250"
FT DISULFID 276..285
FT /evidence="ECO:0000250"
FT DISULFID 819..921
FT /evidence="ECO:0000250"
FT DISULFID 1066..1074
FT /evidence="ECO:0000250|UniProtKB:Q9WU60"
FT DISULFID 1068..1080
FT /evidence="ECO:0000250|UniProtKB:Q9WU60"
FT DISULFID 1083..1092
FT /evidence="ECO:0000250|UniProtKB:Q9WU60"
FT DISULFID 1095..1109
FT /evidence="ECO:0000250|UniProtKB:Q9WU60"
FT DISULFID 1112..1121
FT /evidence="ECO:0000250"
FT DISULFID 1114..1128
FT /evidence="ECO:0000250"
FT DISULFID 1130..1140
FT /evidence="ECO:0000250"
FT DISULFID 1143..1158
FT /evidence="ECO:0000250"
FT VAR_SEQ 1271..1275
FT /note="IAFSQ -> VRVTS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11209055"
FT /id="VSP_051674"
FT VAR_SEQ 1276..1432
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11209055"
FT /id="VSP_051675"
FT CONFLICT 350
FT /note="V -> E (in Ref. 1; BAB21018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1432 AA; 158673 MW; DE4177EE5D55E866 CRC64;
MVAAAAAAEA TEARLRGYTT ATAAPAGWKE RQHRPCAATG AWRPWPRAGL CLPRVLSRAL
SPPPLLPLLP LLFSLLLLPL PREAEAAAVA AAVSGSAAAE AKECDRPCVN GGRCNPGTGQ
CVCPTGWVGE QCQHCGGRFR LTGSSGFVTD GPGNYKYKTK CTWLIEGQPN KIMRLRFNHF
ATECSWDHLY VYDGDSIYAP LIAAFSGLIV PERDGNETAP EVTVTSGYAL LHFFSDAAYN
LTGFNITYNF DMCPNNCSGR GECKSSNSSS TVECECSENW KGESCDIPHC TDNCGFPHRG
ICNASDTRGC SCFPHWQGPG CSIPVPANQS FWTREEYSDL KLPRASHKAV VNGNIMWVVG
GYMFNHSDYS MVLAYDLASR EWLSLNHSVN SVVVRYGHSL ALHKDKIYMY GGKIDSTGNV
TNELRVFHIH NESWVLLTPK AKDQYAVVGH SAHIVTLSSG RVVMLVIFGH CPLYGYISVV
QEYDLEKNTW SILQTQGALV QGGYGHSSVY DHRTKALYVH GGYKAFSANK YRLADDLYRY
HVDTQMWTIL KDSRFFRYLH TAVIVSGTML VFGGNTHNDT SMSHGAKCFS SDFMAYDIAC
DRWSVLPRPE LHHDVNRFGH SAVLHNSTMY VFGGFNSLLL SDVLVFTSEQ CDAHRSEAAC
VAAGPGIRCL WDTQSSRCTS WELATEEQAE KLKSECFSKR TLDHDRCDQH TDCYSCTANT
NDCHWCNDHC VPVNHSCTEG QISIAKYDNC PKDNPMYYCN KKTSCRSCAL DQNCQWEPRN
QECIALPENI CGIGWHLVGN SCLKITTAKE NYDNAKLSCR NHNAFLASLT SQKKVEFVLK
QLRLMQSSQS TSKLTLTPWV GLRKINVSYW CWEDMSPFTN SLLQWMPSEP SDAGFCGILS
EPSTRGLKAA TCINPLNGSV CERPANHSAK QCRTPCALRT ACGECTSSSS ECMWCSNMKQ
CVDSNAYVAS FPFGQCMEWY TMSSCPPENC SGYCTCSHCL EQPGCGWCTD PSNTGKGKCI
EGSYKGPVKM PSHASTGNVY PQPLLNSSMC LEDSRYNWSF IHCPACQCNG HSKCINQSIC
EKCEDLTTGK HCETCISGFY GDPTNGGKCQ PCKCNGHASL CNTNTGKCFC TTKGVKGEEC
QLCEVENRYQ GNPLKGTCYY TLLIDYQFTF SLSQEDDRYY TAINFVATPD EQNRDLDMFI
NASKNFNLNI TWATSFPAGT QTGEEVPVVS KTNIKEYKDS FSNEKFDFRN HPNITFFVYV
SNFTWPIKIQ IAFSQHSNFM DLVQFFVTFF SCFLSLLLVA AVVWKIKQSC WASRRREQLL
REMQQMASRP FASVNVALET DEEPPDLIGG SIKTVPKPIA LEPCFGNKAA VLSVFVRLPR
GLGGIPPPGQ SGLAVASALV DISQQMPIVY KEKSGAVRNR KQQPPAQPGT CI
