ID A0A3Q3VSG6_MOLML Unreviewed; 1406 AA.
AC A0A3Q3VSG6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMOP00000005376.1};
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:ENSMMOP00000005376.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000005376.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 94237.ENSMMOP00000005376; -.
DR Ensembl; ENSMMOT00000005472.1; ENSMMOP00000005376.1; ENSMMOG00000004254.1.
DR OMA; SWHQARK; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 8.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 8.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR22803:SF151; MACROPHAGE MANNOSE RECEPTOR 1-LIKE; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 8.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 4.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1341..1363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 156..204
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 216..332
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 358..475
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 501..616
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 645..761
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 784..899
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 929..1040
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1062..1173
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1202..1315
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 161..187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 175..202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1406 AA; 160127 MW; 4DD7C36B51234B26 CRC64;
MCTVVLKLFF SRPDNGSFLI FNENHNKCIK AESSTSITVA TCNPHAKEQQ FRWASESRVL
SISLKLCLGA AEIKDWVKVL LFECDEKNNL QHWQCKNETL FGLKDQELYL NWGNRNERNL
MIYKGSGLWS RWRIFGTKGD LCSKGFQEVF TIGGNAFSMP CQFPFKFLDK WYAECTRDGR
SDGEMWCATE KDYDTQKKWG FCATKAITSG WDTDPVTGVQ YRRNLQSVLT WHQARKSCQQ
QGADLLSIVE LHEQSYISGL TNFLGTSLWI GLNSLDLENG WQWSNGNPFR YLNWAPGHPS
SEPGHTCAIL NTGKASKWES SACNKKLGYI CRKGSLTSLT PPPIKNQPSF CPSHWVPYAG
KCYYLERSKK MWKDALAVCR KEGGDLASIP NIEEQSFIIS QLGYLPTDVL WIGLNDQRND
NLFEWSDHSQ VTFTQWETDE PSHATNLQED CVLIRGKDGK WADHMCEKTY GYICKKMAST
KPSPGAQEET KPGCKLGSIR FGSYCYNIGS ETKTFDDAKR ACSEAGAYLV DVADRYENAL
LVSLVGLRPE KYFWTSLSNT EDKHTFKWAT KRKVTFTNFN VGMPDRRQGC VAMTTGIFAG
LWDVVSCSKK EKYICKKPAE GALMTTVPPT TPALSCEPGW TPVEGRNICI KFYENKNDVK
KTWQEALDFC RAIGGDLMSV HSSKDLLDLE NPMYKVAWIG FSLSASKGFV WSDGSASNFE
NWGFGEPNNH NDNEHCAEIY IYYSKRWNDR HCEAYNDWIC QIRKGNCFVP FTVFNTTEDG
WIIYNDTQYF INKDKTDMEA ARAFCKKNFG DLVVITGESE RTFLWKQITK DSFGQYYIGM
TVNLDKSFSW VDGTSVTYTA WEKNEPNFAN NDENCVTIYK SMGYWNDINC GLEMPSICKR
SNSFVNSTVA PTIVPTGGCA PEWVAFQGKN WKEARDYCLN QGGNLISILS EKEQAFLLTQ
MVKYEDDLWI GMNDINWDMR FVWTDGRGIS YTNWAKGQPV SHIDNDKKKF EFWSMYIFVS
RSTGLWRVED CYSKHGFICK RNIDSQVAVP PTTALPKAFV KFGNDSYKLV AQKMRWDEAR
RQCQADDADL ASILNPFSQA FITLQISKHK EPVWIGLNSN VTGGRFKWVD NWLLSFTKWG
INEPRNNYGC VYMDRDQKWK TAPCTNTYYS LCKRSPDVAP TDPPQLAGNC PEPKNQKTWI
PFRGHCYFFV SSNVDNWAHA SVECLKMGAS LVSIVDPQES LFIKQNLELL QDNAQSFWIG
LYKTHEGEWM WLDNSVVDYT NWKSVPTSDT CVDISSESGK WSTSRCTRYK SYICKRAKVI
TPTEKPPEIA KVIIEPARSS AGITVAVILV VIAIAGLGAF LFFRKRIPSS VLGESTFDNK
LYFNNPLRAP VDTKGLVANI EQNEQA
//
