ID A0A1S3F949_DIPOR Unreviewed; 1285 AA.
AC A0A1S3F949;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Attractin-like protein 1 {ECO:0000313|RefSeq:XP_012873066.1};
GN Name=Atrnl1 {ECO:0000313|RefSeq:XP_012873066.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012873066.1};
RN [1] {ECO:0000313|RefSeq:XP_012873066.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012873066.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_012873066.1; XM_013017612.1.
DR STRING; 10020.ENSDORP00000002906; -.
DR GeneID; 105986615; -.
DR KEGG; dord:105986615; -.
DR CTD; 26033; -.
DR InParanoid; A0A1S3F949; -.
DR OrthoDB; 5471913at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; IPR011043; Gal_Oxase/kelch_b-propeller.
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; 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; SSF50965; Galactose oxidase, central domain; 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; 1.
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:UP000081671};
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 1136..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..117
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 115..153
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 661..779
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 920..965
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1258..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 119..129
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 143..152
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 937..946
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 949..963
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1285 AA; 142959 MW; 20EAC833551A3982 CRC64;
MDFSNRLTEP SGYLTDGPIN YKYKTKCTWL IEGYPNAVLR LRFNHFATEC SWDHMYVYDG
DSIYAPLIAV LSGLIVPEVR GNETVPEVVT TSGYALLHFF SDAAYNLTGF NIFYSINSCP
NNCSGHGKCT TSISVASQVY CECDKYWKGE ACDIPYCKAN CGSPDHGYCD LTGEKLCVCN
DSWQGPDCSL NVPSTESYWI LPNVKPFSPS VGRASHKAVL HGKFMWVIGG YTFNYSSFQM
VLNYNLESSI WNVGALSRGP LQRYGHSLAL YQENIFMYGG RIETNDGNVT DELWVFNIHS
QSWSTKTPTV LGHGQQYAVE GHSAHIMELD SRDVVMIIIF GYSAIYGYTS SIQEYHISSN
TWLVPETKGA IVQGGYGHTS VYDEITKSIY VHGGYKALPG NKYGLVDDLY KYEVNTKTWT
ILKESGFARY LHSAVLINGA MLIFGGNTHN DTSLSNGAKC FSADFLAYDI ACDEWKTLPK
PNLHRDVNRF GHSAVVINGS MYIFGGFSSV LLNDILVYKP PNCKAFRDEE LCKNAGPGIK
CFWNKNHCES WESGNNILRA KCPSKTAASD DRCYRYADCA SCTANTNGCQ WCDDKKCISA
NSNCSVSVRN YTKCHVRNEQ ICNKLTSCKS CSLNLNCQWD QRQQECQALP AHLCGEGWNH
IGDACLRINS SRESYDNAKL YCYNLSGNLA SLTTLKEVEF VLDEIQKYTQ QKISPWVGLR
KINISYWGWE DMSPFTNTTL QWLPGEPNDS GFCAYLERAA VAGLKANPCT SMVDGLVCEK
PVVSPNQNAR PCKKPCSLRT TCSNCTSNGM ECMWCSSTKR CVDSNAYIIS FPYGQCLEWQ
TATCSPQNCS GLRTCGQCLE QPGCGWCNDP SNTGRGHCIE GSSRGPMRLV GMHNSEMILD
TNLCPKEKNY EWSFIQCPAC QCNGHSTCIN TNVCEQCKNL TTGKQCQDCM PGYYGDPTNG
GQCTACTCSG HANICHLHTG KCFCTTKGIK GDQCQLCDSE NRYVGNPLRG TCYYSLLIDY
QFTFSLLQED DRHHTAINFI ANPEQSNKNL DISINASNNF NLNITWSMGS TGGTISGEET
PIVSKTNIKE YRDSFSYEKF NFRSNPNITF YVYVSNFSWP IKIQIAFSQH NTIMDLVQFF
VTFFSCFLSL LLVAAVVWKI KQTCWASRRR EQLLRERQQM ASRPFASVDV ALEVGAEQTD
FLRGSLEGVP KPIAIEPCAG NRAAVLTVFL CLPRGSSGAP PPGQSGLAIA SALVDISQQK
PSDNKDKTSG VRNRKHLSTR QGTCV
//
