ID A0A8B7SQG9_HIPAR Unreviewed; 1241 AA.
AC A0A8B7SQG9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Attractin-like protein 1 {ECO:0000256|ARBA:ARBA00074817};
GN Name=ATRNL1 {ECO:0000313|RefSeq:XP_019515646.1};
OS Hipposideros armiger (Great Himalayan leaf-nosed bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Rhinolophoidea;
OC Hipposideridae; Hipposideros.
OX NCBI_TaxID=186990 {ECO:0000313|Proteomes:UP000694851, ECO:0000313|RefSeq:XP_019515646.1};
RN [1] {ECO:0000313|RefSeq:XP_019515646.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_019515646.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: May play a role in melanocortin signaling pathways that
CC regulate energy homeostasis. {ECO:0000256|ARBA:ARBA00054004}.
CC -!- SUBUNIT: Interacts with MC4R. {ECO:0000256|ARBA:ARBA00065314}.
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_019515646.1; XM_019660101.1.
DR AlphaFoldDB; A0A8B7SQG9; -.
DR GeneID; 109392039; -.
DR CTD; 26033; -.
DR OrthoDB; 9998912at2759; -.
DR Proteomes; UP000694851; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:TreeGrafter.
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; 2.10.25.10:FF:000860; Attractin; 1.
DR FunFam; 2.10.25.10:FF:000079; Attractin like 1; 1.
DR FunFam; 2.120.10.80:FF:000022; Attractin like 1; 1.
DR FunFam; 2.120.10.80:FF:000116; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000694851};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 92..208
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 206..244
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 754..872
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1013..1058
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DISULFID 210..220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 234..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1030..1039
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1042..1056
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1241 AA; 137838 MW; B8F95620CF902616 CRC64;
MEPGGPALAG PPQPPAPGLC RARSAGSGGG ASFWLLDGNN WLLCYGFLYL ALYAQVSQSK
PCERTGSCFS GRCINSTCLC DPGWVGDQCQ HCQGRFKLTE PSGYLTDGPI NYKYKTKCTW
LIEGYPNAVL RLRFNHFATE CSWDHMYVYD GDSIYAPLIA VLSGLIVPEI RGNETVPEVV
TTSGYALLHF FSDAAYNLTG FNIFYSINSC PNNCSGHGKC TTSISVPSQV YCECDKYWKG
EACDIPYCKA NCGSPDHGYC DLTGEKLCVC NDSWQGPDCS LNVPSTESYW ILPNVKPFSP
SVGRASHKAV LHGKFMWVIG GYTFNYSSFQ MVLNYNLENS IWNVGTLSRG PLQRYGHSLA
LYQENIFMYG GRIETNDGNV TDELWVFNIH SQSWSTKTPT VLGHGQQYAV EGHTAHIMEL
DSRDVVMIII FGYSAIYGYT SSIQEYHISS NTWLVPETKG AIVQGGYGHT SVYDEITKSI
YVHGGYKALP GNKYGLVDDL YKYEVNTKTW TILKESGFAR YLHSAVLING AMLIFGGNTH
NDTSLSNGAK CFSADFLAYD IACDEWKILP KPNLHRDVNR FGHSAVVING SMYIFGGFSS
VLLNDILVYK PPNCKAFRDE ELCKNAGPGI KCIWNKNYCE SWESGNTNNI LRAKCPRKTA
AADDRCYRYA DCASCTANTN GCQWCDDKKC ISANSNCSMS VKNYTKCHVR NEQICNKLTS
CKSCSLNLNC QWDQRQQECQ ALPAHLCGEG WNHIGDACLR INSSRESYDN AKLYCYNLSG
NLASLTTSKE VEFVLDEIQK YTQQKVSPWV GLRKINISYW GWEDMSPFTN TTLQWLPGEP
NDSGFCAYLE RAAVAGLKAN PCTSMADGLV CEKPVVSPNQ NARPCKKPCS LRTSCSNCTS
NGMECMWCSS TKRCVDSNAY IISFPYGQCL EWQTATCSPQ NCSGLRTCGQ CLEQPGCGWC
NDPSNTGRGH CIEGSSRGPM KLVGMHSNEM VLDPGLCPKE KNYEWSFIQC PACQCNGHST
CINNNVCEQC KNLTTGKQCQ DCMPGYYGDP TNGGQCTACT CSGHANICHM HTGKCFCTTK
GIKGDQCQLC DSENRYVGNP LRGTCYYSLL IDYQFTFSLL QEDDRHHTAI NFIANPEQSN
KNLDISINAS NNFNLNITWS VGSTAGTISG EETPIVSKTN IKEYRDSFSY EKFNFRSNPN
ITFYVYVSNF SWPIKIQIVL FPASDSSFTS KWYSPEDSRE P
//
