INTLP_ALLMI
ID INTLP_ALLMI Reviewed; 313 AA.
AC P86928;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Intelectin-like protein {ECO:0000305|PubMed:22085437};
DE AltName: Full=Mannose-specific lectin {ECO:0000303|PubMed:22085437};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Serum {ECO:0000269|PubMed:22085437};
RX PubMed=22085437; DOI=10.1016/j.cbpb.2011.11.001;
RA Darville L.N., Merchant M.E., Maccha V., Siddavarapu V.R., Hasan A.,
RA Murray K.K.;
RT "Isolation and determination of the primary structure of a lectin protein
RT from the serum of the American alligator (Alligator mississippiensis).";
RL Comp. Biochem. Physiol. 161B:161-169(2012).
CC -!- FUNCTION: Binds mannan, mannose and, to a lesser degree, D-lactose, N-
CC acetylgalactosamine, N-acetylglucosamine and beta-D-glucose.
CC {ECO:0000269|PubMed:22085437}.
CC -!- SUBUNIT: Monomer, homodimer, homotrimer and homotetramer. Mostly
CC monomeric or dimeric. {ECO:0000269|PubMed:22085437}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22085437}.
CC -!- MASS SPECTROMETRY: Mass=34640; Method=Electrospray; Note=Monomer.;
CC Evidence={ECO:0000269|PubMed:22085437};
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DR AlphaFoldDB; P86928; -.
DR SMR; P86928; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:2001065; F:mannan binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR SUPFAM; SSF56496; SSF56496; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Lectin;
KW Mannose-binding; Metal-binding; Secreted.
FT CHAIN 1..313
FT /note="Intelectin-like protein"
FT /id="PRO_0000415413"
FT DOMAIN 33..251
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5PPM0"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 262..263
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 274
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT DISULFID 94..280
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT DISULFID 199..259
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT DISULFID 251..265
FT /evidence="ECO:0000250|UniProtKB:Q8WWA0"
SQ SEQUENCE 313 AA; 34001 MW; ED27319E1BE0F6AF CRC64;
NNQLALKLAA TGGSTNSLPA LALQNLLNTW EDTSCCSQTS PGQQSWPRDG AQDGLYTLST
ADGEIYQTFC DMSTHGGGWT LVASVHENNA HGKCTVGDRW SSQQGNSPLY PEGDGNWANN
NIFGSAMGST SDDYKNPGYY DLQAGDLSVW HVPDRAPLRK EMIESSVLLF YRTGFLSSEG
GNLLRLYEKY PVKYGAGSCK VDNGPAVPIV YDFGSAEKTA AYYSPSGRGE FTAGFVQFRV
FNNEKAPMAL CSGLKVTGCN TEHHCIGGGG FFPEGNPRQC GDFPAFDWDG YGTHQSWSTS
REMIESSVLL FYR
