ID A0A8J1JYH7_XENTR Unreviewed; 1405 AA.
AC A0A8J1JYH7;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Attractin-like protein 1 {ECO:0000313|RefSeq:XP_031761586.1};
GN Name=atrnl1 {ECO:0000313|RefSeq:XP_031761586.1,
GN ECO:0000313|Xenbase:XB-GENE-6033278};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Proteomes:UP000008143, ECO:0000313|RefSeq:XP_031761586.1};
RN [1] {ECO:0000313|RefSeq:XP_031761586.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_031761586.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_031761586.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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_031761586.1; XM_031905726.1.
DR GeneID; 100495547; -.
DR KEGG; xtr:100495547; -.
DR AGR; Xenbase:XB-GENE-6033278; -.
DR CTD; 26033; -.
DR Xenbase; XB-GENE-6033278; atrnl1.
DR OMA; CSMSVRN; -.
DR OrthoDB; 9998912at2759; -.
DR Proteomes; UP000008143; Chromosome 7.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 FunFam; 2.120.10.80:FF:000072; Attractin; 1.
DR FunFam; 2.10.25.10:FF:000079; Attractin like 1; 1.
DR FunFam; 2.10.25.10:FF:000164; Attractin like 1; 1.
DR FunFam; 2.120.10.80:FF:000022; Attractin like 1; 1.
DR FunFam; 2.60.120.290:FF:000008; Attractin like 1; 1.
DR FunFam; 3.10.100.10:FF:000013; Attractin like 1; 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; IPR056737; Beta-prop_ATRN-MKLN-like.
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.
DR InterPro; IPR056732; GBD_ATRN.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR056863; LMN_ATRN_NET-like_EGF.
DR InterPro; IPR051568; LZTR1/Attractin.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46376:SF4; ATTRACTIN-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR Pfam; PF24981; Beta-prop_ATRN-LZTR1; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF24973; EGF_LMN_ATRN; 1.
DR Pfam; PF23106; EGF_Teneurin; 1.
DR Pfam; PF24972; GBD_ATRN; 1.
DR Pfam; PF00059; Lectin_C; 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; 1.
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; 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:UP000008143};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..1405
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035158889"
FT TRANSMEM 1255..1279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..183
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 181..219
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 730..848
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 989..1034
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 185..195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 209..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1006..1015
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1018..1032
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1405 AA; 156597 MW; 8D6E012B8722EFF6 CRC64;
MLLLRVATMC HNCPGMSLLR SGLFYLLIFA YSSQGRACEK NPCFSGRCVN NTCLCDPGWV
GELCQHCQGR FRLTEPSGYL TDGPINYKYK TKCTWLIEGY PHAVLRLRFN HFATECSWDH
MYIYDGDSIY SPLIAVLSGL IVPEAPGNET VPEVVTTSGF ALLHFFSDAA YNLTGFNIFY
SINSCPSNCS GHGKCTGSSL VPSRVYCECD KYWKGEACDI PYCKNNCGSP DHGYCDLTGE
KLCVCNDSWQ GPDCSLTVPS TDSYWILPNV KPFSPSVGRA SHKAVMHGKF MWVIGGHAFN
YSSFQMVLNY NVESSIWNVV PVLRGPLQRY GHSLALYQDD IYMYGGKIET IGGNVTDELW
VFNISSQSWS TRTPTVLNHG QHYAVEGHTA HIVELDNRDA VMVIIFGYSS VYGYISNVQE
FYLKSNTWLV PETRGAIVQG GYGHTSVYEP ITKAIYIHGG YKALPGNKYG LVDDLYRYEV
NTRTWTILKE SGLSRYLHTA VLISGTMLVF GGNTHNDTAL SNGAKCFSAD FLAYDIACDE
WRVLQKPNLH RDVNRFGHSA VVSNGSMYIF GGFSSVLLND ILVYKPPSCE AFRSEDQCTS
AARGISCLWD KDHCVSWESV RPSRHLFRAN CRNKSAAADD RCYKNTDCAS CTANTNGCQW
CDDKKCVSLY SNCSVSVKNY TKCYVRNEQI CNKLTSCKSC SLNLNCQWDQ RQQECQALPA
HLCGEGWSHV GDSCLRINSS RDSYDNARVY CHNLSGSLAS LTTSKEVDFV LDEMQKYTNQ
KLSPWVGLRK INVSYWGWED MCPFTNTTLQ WLPGEPSDSG FCAYLERAEV AGLKANPCTA
MTDGLVCEKP VVSPNQNARP CKLPCSLRTS CSNCTSNGME CMWCSNAKRC VDSNAYIISF
PYGQCLEWQT TTCSSQNCSG FRTCAQCLEQ PGCGWCNDPS NTGKGSCVEG SSRGPMRPLG
KHSSEMVLDT GLCPREKNYE WSFIHCPACQ CNGHSTCVNT NVCEQCKNLT MGKHCESCMP
GYYGNPTNGG ECEAMLLCTD YCGAGVMAEM DEQPGILFPL HSKLSSLTAP LYVRPETPPP
ICTREMRDYT AFLIDYQFTF SLVQEEDKYH TAINFIANPE QMFMVICVPI LTDSLLIDYQ
FTFSLVQEED KYHTAINFIA NPEQSNKNLD ISINASNNFN LNITWSIGST AGTISGEEVP
LVSRAHIKEY RDSFSCEKFN FRSNPNITFY VYVSNFTWPI KIQIAFSQHN TIMDLVQFFV
TFFSCFLSLL LVAAVVWKIK QTCWASRRRE QLMRERQQMA SRPFATVDVA LEVGPEQGDI
LRAPTEGAPK PIAIEPCSGN KAAVLTVFLC LPRGLSGVPP PGQSGLAIAS ALIDISQQKS
LDCKDKSSCI RNRKQHPPTR QGTCV
//
