GenomeNet

Database: UniProt
Entry: Q99J86
LinkDB: Q99J86
Original site: Q99J86 
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   16-JAN-2019, entry version 117.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAB21058.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), NUCLEOTIDE
RP   SEQUENCE [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.,
RA   Kawaguchi S., Ogawa Y., Nakao K., Barsh G.S., Nagao M., Ushijima T.,
RA   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
CC       signaling pathways that regulate energy homeostasis and hair
CC       color. Low-affinity receptor for agouti (By similarity). Has a
CC       critical role in normal myelination in the central nervous system.
CC       {ECO:0000250, 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
CC       protein {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
CC       by progressive hypomyelination and vacuolation in the central
CC       nervous system resulting in early-onset tremor and progressive
CC       flaccid paresis of the hind limb. This is due to an 8-bp deletion
CC       at the splice donor site of intron 12, which results in aberrant
CC       and unstable transcripts. {ECO:0000269|PubMed:11209055}.
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   UniGene; Rn.53846; -.
DR   ProteinModelPortal; Q99J86; -.
DR   SMR; Q99J86; -.
DR   STRING; 10116.ENSRNOP00000028847; -.
DR   PhosphoSitePlus; Q99J86; -.
DR   SwissPalm; Q99J86; -.
DR   UniCarbKB; Q99J86; -.
DR   PaxDb; Q99J86; -.
DR   PRIDE; Q99J86; -.
DR   Ensembl; ENSRNOT00000028847; ENSRNOP00000028847; ENSRNOG00000021240. [Q99J86-1]
DR   GeneID; 83526; -.
DR   KEGG; rno:83526; -.
DR   UCSC; RGD:69063; rat. [Q99J86-1]
DR   CTD; 8455; -.
DR   RGD; 69063; Atrn.
DR   eggNOG; KOG1388; Eukaryota.
DR   eggNOG; ENOG410XRW4; LUCA.
DR   GeneTree; ENSGT00940000157346; -.
DR   HOGENOM; HOG000231727; -.
DR   HOVERGEN; HBG004312; -.
DR   InParanoid; Q99J86; -.
DR   OMA; GIRCVWD; -.
DR   OrthoDB; 49565at2759; -.
DR   PhylomeDB; Q99J86; -.
DR   TreeFam; TF321873; -.
DR   PRO; PR:Q99J86; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000021240; Expressed in 9 organ(s), highest expression level in liver.
DR   Genevisible; Q99J86; RN.
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; IEA:Ensembl.
DR   GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0042552; P:myelination; IEA:Ensembl.
DR   GO; GO:0043473; P:pigmentation; IMP:CACAO.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR   CDD; cd00041; CUB; 1.
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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR002049; Laminin_EGF.
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; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Inflammatory response;
KW   Kelch repeat; Laminin EGF-like domain; Lectin; Membrane; Receptor;
KW   Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   PROPEP       24     86       {ECO:0000250}.
FT                                /FTId=PRO_0000394773.
FT   CHAIN        87   1432       Attractin.
FT                                /FTId=PRO_0000007485.
FT   TOPO_DOM     87   1282       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1283   1303       Helical. {ECO:0000255}.
FT   TOPO_DOM   1304   1432       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      100    133       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      135    251       CUB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      249    286       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      355    405       Kelch 1. {ECO:0000255}.
FT   REPEAT      406    454       Kelch 2. {ECO:0000255}.
FT   REPEAT      464    511       Kelch 3. {ECO:0000255}.
FT   REPEAT      516    567       Kelch 4. {ECO:0000255}.
FT   REPEAT      569    627       Kelch 5. {ECO:0000255}.
FT   REPEAT      628    674       Kelch 6. {ECO:0000255}.
FT   DOMAIN      706    751       PSI 1.
FT   DOMAIN      758    797       PSI 2.
FT   DOMAIN      798    922       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      935    986       PSI 3.
FT   DOMAIN      989   1064       PSI 4.
FT   DOMAIN     1066   1111       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1112   1160       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   COMPBIAS    932   1143       Cys-rich.
FT   CARBOHYD    216    216       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    240    240       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    245    245       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    256    256       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    267    267       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    303    303       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    328    328       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    365    365       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    386    386       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    419    419       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    431    431       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    578    578       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    626    626       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    734    734       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    866    866       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    917    917       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    926    926       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    989    989       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1046   1046       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1057   1057       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1076   1076       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1201   1201       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1209   1209       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1253   1253       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1262   1262       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    104    114       {ECO:0000250|UniProtKB:Q9WU60}.
FT   DISULFID    108    121       {ECO:0000250|UniProtKB:Q9WU60}.
FT   DISULFID    123    132       {ECO:0000250|UniProtKB:Q9WU60}.
FT   DISULFID    135    161       {ECO:0000250}.
FT   DISULFID    253    263       {ECO:0000250}.
FT   DISULFID    257    274       {ECO:0000250}.
FT   DISULFID    276    285       {ECO:0000250}.
FT   DISULFID    819    921       {ECO:0000250}.
FT   DISULFID   1066   1074       {ECO:0000250|UniProtKB:Q9WU60}.
FT   DISULFID   1068   1080       {ECO:0000250|UniProtKB:Q9WU60}.
FT   DISULFID   1083   1092       {ECO:0000250|UniProtKB:Q9WU60}.
FT   DISULFID   1095   1109       {ECO:0000250|UniProtKB:Q9WU60}.
FT   DISULFID   1112   1121       {ECO:0000250}.
FT   DISULFID   1114   1128       {ECO:0000250}.
FT   DISULFID   1130   1140       {ECO:0000250}.
FT   DISULFID   1143   1158       {ECO:0000250}.
FT   VAR_SEQ    1271   1275       IAFSQ -> VRVTS (in isoform 2).
FT                                {ECO:0000303|PubMed:11209055}.
FT                                /FTId=VSP_051674.
FT   VAR_SEQ    1276   1432       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11209055}.
FT                                /FTId=VSP_051675.
FT   CONFLICT    350    350       V -> E (in Ref. 1; BAB21018).
FT                                {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
//
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