ID   Q5R349_HUMAN            Unreviewed;       789 AA.
AC   Q5R349;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   27-MAR-2024, entry version 129.
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};
DE   Flags: Fragment;
GN   Name=SELP {ECO:0000313|Ensembl:ENSP00000391694.2};
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:ENSP00000391694.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000391694.2, 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:ENSP00000391694.2}
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; Q5R349; -.
DR   SMR; Q5R349; -.
DR   MassIVE; Q5R349; -.
DR   PeptideAtlas; Q5R349; -.
DR   ProteomicsDB; 63705; -.
DR   Antibodypedia; 794; 1461 antibodies from 45 providers.
DR   Ensembl; ENST00000426706.6; ENSP00000391694.2; ENSG00000174175.17.
DR   UCSC; uc001ggh.4; human.
DR   HGNC; HGNC:10721; SELP.
DR   PharmGKB; PA35643; -.
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; Q5R349; 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; 9.
DR   CDD; cd03592; CLECT_selectins_like; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 9.
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; 9.
DR   PRINTS; PR00343; SELECTIN.
DR   SMART; SM00032; CCP; 9.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 9.
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; 9.
DR   Genevisible; Q5R349; HS.
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};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Proteomics identification {ECO:0007829|MaxQB:Q5R349,
KW   ECO:0007829|PeptideAtlas:Q5R349};
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}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          38..158
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          158..194
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          197..258
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          259..320
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          321..382
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          383..444
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          445..506
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          507..568
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          569..630
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          639..700
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          701..762
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DISULFID        184..193
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        229..256
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        291..318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        353..380
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        415..442
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        477..504
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        539..566
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        601..628
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        671..698
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        733..760
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000391694.2"
SQ   SEQUENCE   789 AA;  86473 MW;  1B58814AF00C5B9E CRC64;
     ANCQIAILYQ RFQRVVFGIS QLLCFSALIS ELTNQKEVAA WTYHYSTKAY SWNISRKYCQ
     NRYTDLVAIQ NKNEIDYLNK VLPYYSSYYW IGIRKNNKTW TWVGTKKALT NEAENWADNE
     PNNKRNNEDC VEIYIKSPSA PGKWNDEHCL KKKHALCYTA SCQDMSCSKQ GECLETIGNY
     TCSCYPGFYG PECEYVRECG ELELPQHVLM NCSHPLGNFS FNSQCSFHCT DGYQVNGPSK
     LECLASGIWT NKPPQCLAAQ CPPLKIPERG NMTCLHSAKA FQHQSSCSFS CEEGFALVGP
     EVVQCTASGV WTAPAPVCKA VQCQHLEAPS EGTMDCVHPL TAFAYGSSCK FECQPGYRVR
     GLDMLRCIDS GHWSAPLPTC EAISCEPLES PVHGSMDCSP SLRAFQYDTN CSFRCAEGFM
     LRGADIVRCD NLGQWTAPAP VCQALQCQDL PVPNEARVNC SHPFGAFRYQ SVCSFTCNEG
     LLLVGASVLQ CLATGNWNSV PPECQAIPCT PLLSPQNGTM TCVQPLGSSS YKSTCQFICD
     EGYSLSGPER LDCTRSGRWT DSPPMCEAIK CPELFAPEQG SLDCSDTRGE FNVGSTCHFS
     CDNGFKLEGP NNVECTTSGR WSATPPTCKG IASLPTPGVQ CPALTTPGQG TMYCRHHPGT
     FGFNTTCYFG CNAGFTLIGD STLSCRPSGQ WTAVTPACRA VKCSELHVNK PIAMNCSNLW
     GNFSYGSICS FHCLEGQLLN GSAQTACQEN GHWSTTVPTC QDDGKCPLNP HSHLGTYGVF
     TNAAFDPSP
//