ID   Q5R345_HUMAN            Unreviewed;       768 AA.
AC   Q5R345;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 119.
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|Ensembl:ENSP00000356762.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000356762.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000356762.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H.,
RA   Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C.,
RA   Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R.,
RA   Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.,
RA   Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.,
RA   Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R.,
RA   Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D.,
RA   Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A.,
RA   Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S.,
RA   Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A.,
RA   Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S.,
RA   Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G.,
RA   Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A.,
RA   Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L.,
RA   Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z.,
RA   Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C.,
RA   Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M.,
RA   Langford C.F., Pandian R.D., Porter K.M., Prigmore E.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000356762.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AL022146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF455060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z99572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q5R345; -.
DR   SMR; Q5R345; -.
DR   MassIVE; Q5R345; -.
DR   PeptideAtlas; Q5R345; -.
DR   ProteomicsDB; 63703; -.
DR   Antibodypedia; 794; 1461 antibodies from 45 providers.
DR   Ensembl; ENST00000367788.6; ENSP00000356762.1; ENSG00000174175.17.
DR   UCSC; uc057nef.1; human.
DR   HGNC; HGNC:10721; SELP.
DR   VEuPathDB; HostDB:ENSG00000174175; -.
DR   GeneTree; ENSGT00940000161063; -.
DR   ChiTaRS; SELP; human.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000174175; Expressed in right coronary artery and 129 other cell types or tissues.
DR   ExpressionAtlas; Q5R345; baseline and differential.
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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|MaxQB:Q5R345,
KW   ECO:0007829|PeptideAtlas:Q5R345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW   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;  84330 MW;  07A271AD47925125 CRC64;
     MANCQIAILY QRFQRVVFGI SQLLCFSALI SELTNQKEVA AWTYHYSTKA YSWNISRKYC
     QNRYTDLVAI QNKNEIDYLN KVLPYYSSYY WIGIRKNNKT WTWVGTKKAL TNEAENWADN
     EPNNKRNNED CVEIYIKSPS APGKWNDEHC LKKKHALCYT ASCQDMSCSK QGECLETIGN
     YTCSCYPGFY GPECEYVREC GELELPQHVL MNCSHPLGNF SFNSQCSFHC TDGYQVNGPS
     KLECLASGIW TNKPPQCLAV QCQHLEAPSE GTMDCVHPLT AFAYGSSCKF ECQPGYRVRG
     LDMLRCIDSG HWSAPLPTCE AISCEPLESP VHGSMDCSPS LRAFQYDTNC SFRCAEGFML
     RGADIVRCDN LGQWTAPAPV CQALQCQDLP VPNEARVNCS HPFGAFRYQS VCSFTCNEGL
     LLVGASVLQC LATGNWNSVP PECQAIPCTP LLSPQNGTMT CVQPLGSSSY KSTCQFICDE
     GYSLSGPERL DCTRSGRWTD SPPMCEAIKC PELFAPEQGS LDCSDTRGEF NVGSTCHFSC
     DNGFKLEGPN NVECTTSGRW SATPPTCKGI ASLPTPGVQC PALTTPGQGT MYCRHHPGTF
     GFNTTCYFGC NAGFTLIGDS TLSCRPSGQW TAVTPACRAV KCSELHVNKP IAMNCSNLWG
     NFSYGSICSF HCLEGQLLNG SAQTACQENG HWSTTVPTCQ AGPLTIQEAL TYFGGAVAST
     IGLIMGGTLL ALLRKRFRQK DDGKCPLNPH SHLGTYGVFT NAAFDPSP
//