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Database: UniProt
Entry: A0A2K5EIC5_AOTNA
LinkDB: A0A2K5EIC5_AOTNA
Original site: A0A2K5EIC5_AOTNA 
ID   A0A2K5EIC5_AOTNA        Unreviewed;       757 AA.
AC   A0A2K5EIC5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=CD248 molecule {ECO:0000313|Ensembl:ENSANAP00000032977.1};
GN   Name=CD248 {ECO:0000313|Ensembl:ENSANAP00000032977.1};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000032977.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000032977.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K5EIC5; -.
DR   STRING; 37293.ENSANAP00000032977; -.
DR   Ensembl; ENSANAT00000051031.1; ENSANAP00000032977.1; ENSANAG00000034174.1.
DR   GeneTree; ENSGT00940000162405; -.
DR   OMA; APNKRIT; -.
DR   Proteomes; UP000233020; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR   GO; GO:0060033; P:anatomical structure regression; IEA:Ensembl.
DR   GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR   GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR   GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR   CDD; cd03600; CLECT_thrombomodulin_like; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
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; IPR016187; CTDL_fold.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   PANTHER; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR   PANTHER; PTHR14789:SF4; ENDOSIALIN; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..757
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014386379"
FT   TRANSMEM        686..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..147
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          409..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  80636 MW;  113F89315AC6C351 CRC64;
     MLLRLLLAWA AAGPTLGQDS RTPEPRAACG PGSCYALFPK RRTFLEAWRA CRELGGNLAT
     PRTPEEARRV DSLVGAGPAS RLLWIGLQRQ ARQCQPQRPL RGFTWTTGDQ DTAFTNWAQP
     ATGGPCPAQR CVALEAGGEH RWLEGSCTLA VDGYLCQFGF EGACPALQEE AGQAGPAVYT
     TPFHLVSTEF EWLPFGSVAA VQCQAGRGAS LLCVKQPEGG VGWSRAGPLC PGTGCGPDNG
     GCEHECVEEV DGHVSCRCTE GFRLAADGQS CEDPCAQAPC EQQCEPGGAQ GYSCHCRLGF
     RPAEDDPHRC VDTDECQIAG VCQQMCVNYV GGFECYCSEG HELEADGISC SPAGAIGARA
     SPDLEDELLV DGEDEEDEDE AWEAIDGGWT EMPGILWMEP TQPPDFALAY RPSFPEDGDP
     QKPHPEPTWP PPLSAPRVPY HSSVLSVTRP VVVSATRPTL PSAHQPPVIP ATHPDLPRDH
     QIPVIAANYP DLPSAYQPGI LSVSHPARPP AHQPPMISTK YPELFPAHRS PMFPDTQVTG
     TQTTTHLPGI PPNRAPLITT LGAHQPPLAP DVPILRTQAT QLPIIPTAQA SVTTASRSPV
     SPAHQVSVPA ATQPPAPPTL LASQSPTNQT LPISPTHPHS KAPQIPREGG PHPKLAPWLP
     SAAPTAAPTA LGEAGLTGHS QRDDRWLLVA LLVPTCVFLV VLLALGIVYC TRCGPHAPNK
     RITDCYRWVT HAGSKSPTEP MPPRGSLTGV QTCRTSV
//
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