ID A0A3Q0CU15_MESAU Unreviewed; 768 AA.
AC A0A3Q0CU15;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=p-selectin {ECO:0000256|ARBA:ARBA00044174};
DE AltName: Full=CD62 antigen-like family member P {ECO:0000256|ARBA:ARBA00044221};
DE AltName: Full=Granule membrane protein 140 {ECO:0000256|ARBA:ARBA00044337};
DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 3 {ECO:0000256|ARBA:ARBA00044355};
DE AltName: Full=Platelet activation dependent granule-external membrane protein {ECO:0000256|ARBA:ARBA00044292};
GN Name=Selp {ECO:0000313|RefSeq:XP_021083584.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021083584.1};
RN [1] {ECO:0000313|RefSeq:XP_021083584.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: Interacts with SNX17. Interacts with SELPLG/PSGL1 and PODXL2
CC and mediates neutrophil adhesion and leukocyte rolling. This
CC interaction requires the sialyl-Lewis X epitope of SELPLG and PODXL2,
CC and specific tyrosine sulfation on SELPLG.
CC {ECO:0000256|ARBA:ARBA00044001}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family.
CC {ECO:0000256|ARBA:ARBA00007360}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_021083584.1; XM_021227925.1.
DR AlphaFoldDB; A0A3Q0CU15; -.
DR STRING; 10036.ENSMAUP00000015841; -.
DR KEGG; maua:101834270; -.
DR OrthoDB; 3035244at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 8.
DR CDD; cd03592; CLECT_selectins_like; 1.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 8.
DR Gene3D; 2.10.25.10; Laminin; 1.
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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR033991; Selectin_CTLD.
DR InterPro; IPR002396; Selectin_superfamily.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR19325:SF484; P-SELECTIN; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 8.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 8.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50923; SUSHI; 8.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 709..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..159
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 159..195
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 198..259
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 260..321
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 322..383
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 384..445
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 446..507
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 508..569
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 578..639
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 640..701
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 185..194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 230..257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 292..319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 354..381
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 416..443
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 478..505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 540..567
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 610..637
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 672..699
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 768 AA; 83571 MW; 75A84113B2263E3E CRC64;
MANCLKASWK PRLRSVVLGG AQLIWLIALI SEFVNQKEVT AWTYNYSVKA YSWNYSRAFC
QKHFTDLVAI QNKNEIAHLN DVIPYYNSYY WIGIRKINNK WTWVGTNKTL TKEAENWADN
EPNNKRNNQD CVEIYIKSNS APGKWNDEPC TKRKRALCYT ASCQDMSCNK QGECIETIGN
YTCSCYPGFY GPECEYVQEC GEFDLPQHVS MSCRHPVGDF SFSSQCSFHC AEGYELNGPS
KLECLASGSW TSNPPQCKAV QCQSLETPIH GTMDCMHPLA AFAYGSSCKF ECHPGYQVRG
SDTLHCTGSG QWTEPLPTCE AIACEALETP AHGSMDCHPS TAALEYNSSC TFSCAEGFVL
KGNDSIRCSD LGQWTAPTPV CEALQCQDFP VPSKAQVTCS DPFGALKYQS VCSFSCAEGS
LLVGASAIRC LATGHWSGAP PECQAVTCTP LLSPQNGTMT CIQPPEGSAY KSTCQFVCDE
GFYLSGPERV DCSPSGHWTG TPPTCEAIKC PGMFAPDQGS LDCSHDNGEF IVGSTCRFSC
NNDFELLGSK TVECMVSGRW SAPPPTCKVV TSPPNPEVRC PALTTPGQGT MSCRHHLGSF
GPNTTCYFGC KTGFTIRGAN WLRCKTSGQW TAVTPVCRAI KCSELHMDTP VLMNCSNPWG
NFSYGSTCNF NCPEGQLLNG SARATCRENG QWSATMPLCQ AGPLTIQEAL TYLGGAVAST
TGLAVGGTLL ALLRKRLRKK DDGKCPLSPH SHLGTYGVFT NAAFDPTP
//
