ID M3XCX9_FELCA Unreviewed; 1354 AA.
AC M3XCX9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Attractin like 1 {ECO:0000313|Ensembl:ENSFCAP00000024485.4};
GN Name=ATRNL1 {ECO:0000313|Ensembl:ENSFCAP00000024485.4,
GN ECO:0000313|VGNC:VGNC:60034};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000024485.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000024485.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000024485.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000024485.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000024485.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000024485.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000024485.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AANG04000273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9685.ENSFCAP00000024485; -.
DR Ensembl; ENSFCAT00000027729.4; ENSFCAP00000024485.4; ENSFCAG00000025583.4.
DR VGNC; VGNC:60034; ATRNL1.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00940000155790; -.
DR HOGENOM; CLU_003930_0_0_1; -.
DR InParanoid; M3XCX9; -.
DR OMA; NCSMSVR; -.
DR Proteomes; UP000011712; Chromosome D2.
DR Bgee; ENSFCAG00000025583; Expressed in brain and 10 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR CDD; cd03597; CLECT_attractin_like; 1.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR034011; Attractin-like_CTLD.
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 PANTHER; PTHR46376:SF2; DISTRACTED, ISOFORM B; 1.
DR PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR Pfam; PF01437; PSI; 1.
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; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1238..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..217
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 215..253
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 763..881
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1022..1067
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 219..229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 243..252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1039..1048
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1051..1065
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1354 AA; 149518 MW; 7791CDDDF787FADA CRC64;
MEPGGRGRIG PPQPAAPGLW RARPAGGGGG GGGGGGGGGA SSWLLDGNSW LLCYGFLYLA
LYAQVSQSKP CERTGSCFSG RCVNSTCLCD PGWVGDQCQH CQGRFKLTEP SGYLTDGPIN
YKYKTKCTWL IEGYPNAVLR LRFNHFATEC SWDHMYVYDG DSIYAPLIAV LSGLIVPEIR
GNETVPEVVT TSGYALLHFF SDAAYNLTGF NIFYSINSCP NNCSGHGKCT TSVSVPSQVY
CECDKYWKGE ACDIPYCKAN CGSPDHGYCD LTGEKLCVCN DSWQGPDCSL NVPSTESYWI
LPNVKPFSPS VGRASHKAVL YGKFMWVIGG YTFNYSSFQM VLNYNLESSI WNVGSLSRGP
LQRYGHSLAL HQENIFMYGG RIETNDGNVT DELWVFNIHS QSWSTKTPTV LGHGQQYAVE
GHSAHIMELD SRDVVMIVIF GYSAIYGYTS SIQEYHISSN TWLVPETKGA IVQGGYGHTS
VYDEITKSIY VHGGYKALPG NKYGLVDDLY KYEVNTKTWT ILKESGFARY LHSAVLINGA
MLIFGGNTHN DTSLSNGAKC FSADFLAYDI ACDEWKILPK PNLHRDVNRF GHSAVVINGS
MYIFGGFSSV LLNDILVYKP PNCKAFRDEE LCKNAGPGIK CIWNKNHCES WESGNTNNIL
RAKCPPKTAA PDDRCYRYAD CASCTANTNG CQWCDEKKCI SANSNCSVSV KNYTKCHVRN
EQICNKLTSC KSCSLNLNCQ WDQRQQECQA LPAHLCGEGW NHIGDACLRI NSSRESYDNA
KLYCYNLSGN LASLTTSKEV EFVLDEIQKY TQQKVSPWVG LRKINISYWG WEDMSPFTNT
TLQWLPGEPN DSGFCAYLEK AAVAGLKANP CTSMADGLVC EKPVVSPNQN ARPCKKPCSL
RTSCSNCTSN GMECMWCSST RRCVDSNAYI ISFPYGQCLE WQTATCSPQN CSGLRTCGHC
LEQPGCGWCN DPSNTGRGHC IEGSSRGPMK LVGMHSSEMV LDSSLCPKEK NYEWSFIQCP
ACQCNGHSTC VNNNVCEQCK NLTTGNQCQD CMPGYYGDPT NGGQCTACTC SGHANICHMH
TGKCFCTTKG IKGDQCQLCD SENRYVGNPL RGTCYYSLLI DYQFTFSLLQ EDDRHHTAIN
FIANPEQSNK NLDISINASN NFNLNITWSV GSTAGTISGE ETPIVSKTNI KEYRDSFSYE
KFNFRSNPNI TFYVYVSNFS WPIKIQIAFS QHNTIMDLVQ FFVTFFSCFL SLLLVAAVVW
KIKQTCWASR RREQLLRERQ QMASRPFASV DVALEVGAEQ TEYLRGPVEG APKPIAIEPC
AGNRAAVLTV FLCLPRGSSG APPPGQSGAA WILK
//
