ID A0A3B4BP08_PYGNA Unreviewed; 761 AA.
AC A0A3B4BP08;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000001308.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000001308.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B4BP08; -.
DR Ensembl; ENSPNAT00000012398.1; ENSPNAP00000001308.1; ENSPNAG00000008133.1.
DR GeneTree; ENSGT00940000160168; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
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; 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; 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; PF00008; EGF; 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 SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 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; 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; 7.
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};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 721..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..154
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 154..190
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 193..254
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 255..317
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 318..379
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 464..522
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 523..584
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 585..646
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 647..716
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 180..189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 225..252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 288..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 350..377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 493..520
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 555..582
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 617..644
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 687..714
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 761 AA; 84032 MW; E8283822A7548417 CRC64;
RWIMMNKDRL SSQNSLFMVF LLTTFYFSLT VEVEAWTYHY RTDGNMDWET ARRWCQQDYT
DMVAIQNQEE IAYLNNTLPY HKQYYWIGIR KVEGQWTWVG TKKPLTDEAA NWAQGEPNNQ
GSGEDCVEIY IKRGKDTAMW NDEKCSKSKA PLCYKASCLN TSCSEHAECV ENIGSYICKC
HPGFTGPRCE EAVQCRPLRQ PIWGFLQCNH VYREFQFSSS CHFHCAHGYT LIGSQNLHCL
ESGDWNSDPP ECQAVQCPPI TVATGGWSMN CSHPINTNSY NSTCTFNCEE GFELVGSLTT
QCDHTGQWTH KTPTCTAVSC STLLAPAKGH MSCDGPLGKF SFRSSCNISC EEGYALRGEN
RITCLKTGNW SAYAPTCEGT VSVHIVHDRT VTVVQLSHYR QYLLRCSPLK SVPHGSLHCM
DPLDEFSYGS TCWMECDLGF QLMSTNFTHC TSQGKWSHSL SVSVQCSPIS GNSSGCADPL
GKFSFRSSCT VSCEEGYTLT GANTLTCLKT GNWTAEAPTC EAVSCGTLLT PVNSHMTCAD
PLGKFSFRSS CDVTCNEGYT LRGENILTCM ETSNWSADTP TCEARQCPLL LSPENGRMNC
SHLHSSFSFG SHCSFGCEDG HVLTGEPTLD CTATGSWSQE MPSCNAVQCE PLAHSPLPQS
HTPPVPFMNC SHPRGNFNFG SQCMFQCSDG YRLNGSNEVV CTSAGIWTDL LPTCMPLGTS
LLVYIATGAA SSLGLLTVGG LFLLLVQRLT KKGKRHALLA Q
//
