ID A0A3Q4BXX1_MOLML Unreviewed; 671 AA.
AC A0A3Q4BXX1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMOP00000027232.1};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000027232.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000027232.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q4BXX1; -.
DR STRING; 94237.ENSMMOP00000027232; -.
DR Ensembl; ENSMMOT00000027695.1; ENSMMOP00000027232.1; ENSMMOG00000020587.1.
DR OMA; APNKRIT; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR CDD; cd03600; CLECT_thrombomodulin_like; 1.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR PANTHER; PTHR14789:SF4; ENDOSIALIN; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..671
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018644376"
FT TRANSMEM 610..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..168
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 336..372
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 373..412
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 512..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 74775 MW; DD2855DF33FC6FDF CRC64;
MGSLLSSTAV LLSAFLLSLL FGFSSVLCQD LRERDAICNE DGCFVVYFQR KTFLDSWKSC
KEKGGNLATI KRKEDASVIA SLFSTIDLRN SRTKVRVWIG LQRQPRQCTT TWPLRGFSWT
TGDQDTEYTN WQKEDSLLCS APRCVVMGYG NQEEEQSDNF KWLDGSCSVT VDGYLCHYAY
KGMCAALWNI GAGNALYITP FNLLSTLLTH VPLGSVANMP CPSDTKEEQS ALCMLKEDGS
VGWSYVSSSC LDPPASHNWC DQDNGGCEHF CRLTGVHFYC ECAEGYHLGE NGQNCELSNV
CQGTSCEFEC VPLSDGYRCV CPEGYMLATD RHGCLDVDEC LQNPCEQLCV NVPGTFECQC
REGYQPDDAV CEDIDECIND PCEHACENTP GSHICHCHLG YSPMPEDTSR CQDTDECRIH
GTCAHDPPTQ EPERDAVYIE NGETNLLEWG QTSQPELEVL TNIINTTPQP TTKSLSTPHW
YEGNERETTT AFPFISNSTQ SEGVWNWLVE PTTSSQKEGN SEDSPIDHNM VTVSSNHSQG
KEKQNQFSEN FQFPVEDLME KDYFENTHSP DSALPTQITP SQRPLKESGL SGDNLDSIQA
DRERRHSNNW LLVGLLVAIC ICIVVMVAVG IVYCNHCAVQ TRNKNANDCY HWISGALTKL
LKSGFDCSVE L
//
