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Database: UniProt
Entry: A0A1S3GJ09_DIPOR
LinkDB: A0A1S3GJ09_DIPOR
Original site: A0A1S3GJ09_DIPOR 
ID   A0A1S3GJ09_DIPOR        Unreviewed;      1468 AA.
AC   A0A1S3GJ09;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=C-type mannose receptor 2 {ECO:0000313|RefSeq:XP_012888781.1};
GN   Name=Mrc2 {ECO:0000313|RefSeq:XP_012888781.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012888781.1};
RN   [1] {ECO:0000313|RefSeq:XP_012888781.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012888781.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_012888781.1; XM_013033327.1.
DR   STRING; 10020.ENSDORP00000023436; -.
DR   GeneID; 105998557; -.
DR   KEGG; dord:105998557; -.
DR   CTD; 9902; -.
DR   InParanoid; A0A1S3GJ09; -.
DR   OrthoDB; 4271106at2759; -.
DR   Proteomes; UP000081671; 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; 7.
DR   CDD; cd03590; CLECT_DC-SIGN_like; 1.
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; IPR033989; CD209-like_CTLD.
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:SF69; C-TYPE MANNOSE RECEPTOR 2; 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; 3.
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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00479}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_012888781.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
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        1402..1425
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          170..218
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          232..348
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          377..493
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          516..623
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          666..797
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          820..939
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          967..1089
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1120..1226
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1261..1372
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          122..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1046..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1438..1468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        175..201
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        189..216
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|RefSeq:XP_012888781.1"
SQ   SEQUENCE   1468 AA;  165669 MW;  34152F79D82C5A42 CRC64;
     PGHLLRCALL LGGLRLGRPR DSTAALPEAD IFLIFSHGLQ GCLESQGAKV RVTPACNTSL
     PAQRWKWVSR NRLFNLGAMQ CLGTGWPGTN STASLGMYEC DREALSLRWQ CRTLGDQLSH
     LLGGSTGNAS KPGPLERGDH TRSGQWRIYG SEEDLCARPY YEVYTIQGNS HGKPCTIPFK
     YDNQWFHGCT STGREDGHLW CATTQDYGKD ERWGFCPIKS NDCETFWDKD QLTDSCYQFN
     FQSTLSWREA WASCEQQGAD LLSITEIHEQ TYINGLLTGY SSTLWIGLND LDTSGGWQWS
     DNSPLKYLNW ESDQPDNPNE ENCGVIRTES SGGWQNRDCS IALPYVCKKK PNSTTELTPP
     DRWANVKVDC EPSWQPFQGH CYRLQAEKRS WQESKKACLR GGGDLLSIHS MAELEFITKQ
     IKQEVEELWI GLNDLKLQMN FEWSDGSLVS FTHWHPFEPN NFRDSLEDCV TIWGPEGRWN
     DSPCNQSLPS ICKKAGQLSQ GAAEEDHGCR KGWTWHSPSC YWLGEDQVTY SEARRLCTDH
     GSQLVTITNR FEQAFVSSLI YNWEGQYFWT ALQDLNGTGS FHWLSGDEVM YTHWNRDQPG
     YSRGGCVALA TGSAMGLWEV KNCTSFRARY ICRQSLGTPV TPELPGPDPT PSLAGSCPQG
     WASDPKLRYC YKVFSSERLQ DKKSWIQAQG NCQELGAQLL SLASYEEEHF VANMLNKIFG
     ESEPEIHEQH WFWIGLNRRD PREGQSWRWS DGLGFSYHNF DRSRHDDDDI RGCAVLDLAS
     LQWVAMQCET QLDWICKIPR GTEVRKPDVS PQGRREWLRF QDAEYKFFEH HSTWAQAQRI
     CTWFQAELTS VHSQDELDFL GHNLQKFSRG QEQHWWIGLH TSESDGRFRW TDGSIINFIS
     WAAGKPRPPG KEKKCVYMTA SREDWGDQRC LTALPYICKR TNNTGQTQLP DLPPPALGGC
     PSGWSQFLNK CFRIQGQHPQ DRVKWSEAQF FCEQQEAQLI TIANPLEQAF ITAKLPNVTF
     DLWTGLHASQ RDFQWVEQEP LLYTNWAPGE PSGPSPAPSG NKPTSCAVVL HSPSAHFTGR
     WDDRSCTEEA HGFICQKGTD LSLSPSPAAS PPAPGTELSY LNGTFRLLQK PLRWHDALLL
     CESRNTSLAH VPDPYTQAFL TQAARGLRVP LWIGLASEEG SRQYSWVSEE PLSYMNWQDG
     EPQHSGGCTY LDVDGAWHTT SCDTKLQGAV CGVNRGPPPP RRINYHGSCP QGLADSAWIP
     FREHCYSFHM ELLLGHKEAL QRCQRVGGAV LSILDEMENV FVWEHLQSSE GQNRGAWLGM
     NFNPKGGTLV WQDNTVVNYS NWGSPGLGPS MLSHNSCYWI QSNSGLWRPG ACTNITMGVV
     CKLPRVEESS FSPSAALPEN PAALVVVLMA VLLLLALITA ALILYRRRQS VERGTFEGAR
     YSRSSSGPGE ATEKNILVSD MEMNEQQE
//
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