URP2_HUMAN
ID URP2_HUMAN Reviewed; 667 AA.
AC Q86UX7; Q8IUA1; Q8N207; Q9BT48;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Fermitin family homolog 3;
DE AltName: Full=Kindlin-3;
DE AltName: Full=MIG2-like protein;
DE AltName: Full=Unc-112-related protein 2;
GN Name=FERMT3; Synonyms=KIND3, MIG2B, URP2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=12697302; DOI=10.1016/s0925-4439(03)00035-8;
RA Weinstein E.J., Bourner M., Head R., Zakeri H., Bauer C., Mazzarella R.;
RT "URP1: a member of a novel family of PH and FERM domain-containing
RT membrane-associated proteins is significantly over-expressed in lung and
RT colon carcinomas.";
RL Biochim. Biophys. Acta 1637:207-216(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 20-35; 424-438 AND 569-577, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12886250; DOI=10.1038/sj.leu.2402993;
RA Boyd R.S., Adam P.J., Patel S., Loader J.A., Berry J., Redpath N.T.,
RA Poyser H.R., Fletcher G.C., Burgess N.A., Stamps A.C., Hudson L., Smith P.,
RA Griffiths M., Willis T.G., Karran E.L., Oscier D.G., Catovsky D.,
RA Terrett J.A., Dyer M.J.S.;
RT "Proteomic analysis of the cell-surface membrane in chronic lymphocytic
RT leukemia: identification of two novel proteins, BCNP1 and MIG2B.";
RL Leukemia 17:1605-1612(2003).
RN [5]
RP POSSIBLE FUNCTION (ISOFORM 2).
RX PubMed=18280249; DOI=10.1016/j.bbrc.2008.02.024;
RA Wang L., Deng W., Shi T., Ma D.;
RT "URP2SF, a FERM and PH domain containing protein, regulates NF-kappaB and
RT apoptosis.";
RL Biochem. Biophys. Res. Commun. 368:899-906(2008).
RN [6]
RP INVOLVEMENT IN LAD3.
RX PubMed=18779414; DOI=10.1182/blood-2008-06-163162;
RA Mory A., Feigelson S.W., Yarali N., Kilic S.S., Bayhan G.I.,
RA Gershoni-Baruch R., Etzioni A., Alon R.;
RT "Kindlin-3: a new gene involved in the pathogenesis of LAD-III.";
RL Blood 112:2591-2591(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP INVOLVEMENT IN LAD3.
RX PubMed=19617577; DOI=10.1182/blood-2009-04-218636;
RA Manevich-Mendelson E., Feigelson S.W., Pasvolsky R., Aker M., Grabovsky V.,
RA Shulman Z., Kilic S.S., Rosenthal-Allieri M.A., Ben-Dor S., Mory A.,
RA Bernard A., Moser M., Etzioni A., Alon R.;
RT "Loss of Kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness
RT developed under shear flow conditions.";
RL Blood 114:2344-2353(2009).
RN [9]
RP INVOLVEMENT IN LAD3.
RX PubMed=19064721; DOI=10.1182/blood-2008-10-182154;
RA Kuijpers T.W., van de Vijver E., Weterman M.A.J., de Boer M., Tool A.T.J.,
RA van den Berg T.K., Moser M., Jakobs M.E., Seeger K., Sanal O., Uenal S.,
RA Cetin M., Roos D., Verhoeven A.J., Baas F.;
RT "LAD-1/variant syndrome is caused by mutations in FERMT3.";
RL Blood 113:4740-4746(2009).
RN [10]
RP INVOLVEMENT IN LAD3, AND FUNCTION.
RX PubMed=19234463; DOI=10.1038/nm.1931;
RA Svensson L., Howarth K., McDowall A., Patzak I., Evans R., Ussar S.,
RA Moser M., Metin A., Fried M., Tomlinson I., Hogg N.;
RT "Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3
RT affecting integrin activation.";
RL Nat. Med. 15:306-312(2009).
RN [11]
RP INVOLVEMENT IN LAD3, AND FUNCTION.
RX PubMed=19234460; DOI=10.1038/nm.1917;
RA Malinin N.L., Zhang L., Choi J., Ciocea A., Razorenova O., Ma Y.-Q.,
RA Podrez E.A., Tosi M., Lennon D.P., Caplan A.I., Shurin S.B., Plow E.F.,
RA Byzova T.V.;
RT "A point mutation in KINDLIN3 ablates activation of three integrin
RT subfamilies in humans.";
RL Nat. Med. 15:313-318(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11 AND TYR-504, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND THR-591, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP STRUCTURE BY NMR OF 349-478.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PH domain of kindlin-3 from human.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [17]
RP VARIANT LAD3 SER-599, CHARACTERIZATION OF VARIANT LAD3 SER-599, AND
RP FUNCTION.
RX PubMed=26359933; DOI=10.1111/pai.12485;
RA Suratannon N., Yeetong P., Srichomthong C., Amarinthnukrowh P.,
RA Chatchatee P., Sosothikul D., van Hagen P.M., van der Burg M., Wentink M.,
RA Driessen G.J., Suphapeetiporn K., Shotelersuk V.;
RT "Adaptive immune defects in a patient with leukocyte adhesion deficiency
RT type III with a novel mutation in FERMT3.";
RL Pediatr. Allergy Immunol. 27:214-217(2016).
CC -!- FUNCTION: Plays a central role in cell adhesion in hematopoietic cells
CC (PubMed:19234463, PubMed:26359933). Acts by activating the integrin
CC beta-1-3 (ITGB1, ITGB2 and ITGB3) (By similarity). Required for
CC integrin-mediated platelet adhesion and leukocyte adhesion to
CC endothelial cells (PubMed:19234460). Required for activation of
CC integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By
CC similarity). {ECO:0000250|UniProtKB:Q8K1B8,
CC ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463,
CC ECO:0000269|PubMed:26359933}.
CC -!- FUNCTION: Isoform 2 may act as a repressor of NF-kappa-B and apoptosis.
CC {ECO:0000269|PubMed:19064721, ECO:0000269|PubMed:19234460,
CC ECO:0000269|PubMed:19234463}.
CC -!- SUBUNIT: Interacts with ITGB1, ITGB2 and ITGB3 (via cytoplasmic tails).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q86UX7-2; Q8N6D5: ANKRD29; NbExp=3; IntAct=EBI-12915620, EBI-17439331;
CC Q86UX7-2; Q99633: PRPF18; NbExp=3; IntAct=EBI-12915620, EBI-2798416;
CC -!- SUBCELLULAR LOCATION: Cell projection, podosome {ECO:0000250}.
CC Note=Present in the F-actin surrounding ring structure of podosomes,
CC which are specialized adhesion structures of hematopoietic cells.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long, URP2LF;
CC IsoId=Q86UX7-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, URP2SF;
CC IsoId=Q86UX7-2; Sequence=VSP_009226;
CC -!- TISSUE SPECIFICITY: Highly expressed in lymph node. Expressed in
CC thymus, spleen and leukocytes. Weakly expressed in placenta, small
CC intestine, stomach, testis and lung. Overexpressed in B-cell
CC malignancies. {ECO:0000269|PubMed:12697302,
CC ECO:0000269|PubMed:12886250}.
CC -!- DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam
CC techniques because it contains the insertion of a PH domain.
CC -!- DISEASE: Leukocyte adhesion deficiency 3 (LAD3) [MIM:612840]: A
CC disorder characterized by recurrent bacterial infections without pus
CC formation, leukocytosis and major bleeding disorders.
CC {ECO:0000269|PubMed:18779414, ECO:0000269|PubMed:19064721,
CC ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463,
CC ECO:0000269|PubMed:19617577, ECO:0000269|PubMed:26359933}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}.
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DR EMBL; AY093951; AAM19736.1; -; mRNA.
DR EMBL; AY093952; AAM19737.1; -; mRNA.
DR EMBL; AK093719; BAC04220.1; -; mRNA.
DR EMBL; BC004347; AAH04347.2; -; mRNA.
DR EMBL; BC013366; AAH13366.1; -; mRNA.
DR EMBL; BC015584; AAH15584.1; -; mRNA.
DR CCDS; CCDS8059.1; -. [Q86UX7-2]
DR CCDS; CCDS8060.1; -. [Q86UX7-1]
DR RefSeq; NP_113659.3; NM_031471.5. [Q86UX7-2]
DR RefSeq; NP_848537.1; NM_178443.2. [Q86UX7-1]
DR RefSeq; XP_011543596.1; XM_011545294.2.
DR RefSeq; XP_016873887.1; XM_017018398.1.
DR PDB; 2YS3; NMR; -; A=349-482.
DR PDB; 6V97; X-ray; 2.38 A; A/B=1-667.
DR PDB; 6V9G; X-ray; 2.35 A; A/B=1-667.
DR PDB; 7C3M; X-ray; 3.60 A; A/B/C=1-667.
DR PDBsum; 2YS3; -.
DR PDBsum; 6V97; -.
DR PDBsum; 6V9G; -.
DR PDBsum; 7C3M; -.
DR AlphaFoldDB; Q86UX7; -.
DR SMR; Q86UX7; -.
DR BioGRID; 123735; 60.
DR CORUM; Q86UX7; -.
DR IntAct; Q86UX7; 39.
DR STRING; 9606.ENSP00000279227; -.
DR iPTMnet; Q86UX7; -.
DR PhosphoSitePlus; Q86UX7; -.
DR BioMuta; FERMT3; -.
DR DMDM; 41018464; -.
DR EPD; Q86UX7; -.
DR jPOST; Q86UX7; -.
DR MassIVE; Q86UX7; -.
DR MaxQB; Q86UX7; -.
DR PaxDb; Q86UX7; -.
DR PeptideAtlas; Q86UX7; -.
DR PRIDE; Q86UX7; -.
DR ProteomicsDB; 69932; -. [Q86UX7-1]
DR ProteomicsDB; 69933; -. [Q86UX7-2]
DR Antibodypedia; 29146; 282 antibodies from 37 providers.
DR DNASU; 83706; -.
DR Ensembl; ENST00000279227.9; ENSP00000279227.5; ENSG00000149781.13. [Q86UX7-1]
DR Ensembl; ENST00000345728.10; ENSP00000339950.5; ENSG00000149781.13. [Q86UX7-2]
DR GeneID; 83706; -.
DR KEGG; hsa:83706; -.
DR MANE-Select; ENST00000345728.10; ENSP00000339950.5; NM_031471.6; NP_113659.3. [Q86UX7-2]
DR UCSC; uc001nyl.3; human. [Q86UX7-1]
DR CTD; 83706; -.
DR DisGeNET; 83706; -.
DR GeneCards; FERMT3; -.
DR HGNC; HGNC:23151; FERMT3.
DR HPA; ENSG00000149781; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; FERMT3; -.
DR MIM; 607901; gene.
DR MIM; 612840; phenotype.
DR neXtProt; NX_Q86UX7; -.
DR OpenTargets; ENSG00000149781; -.
DR Orphanet; 99844; Leukocyte adhesion deficiency type III.
DR PharmGKB; PA162388384; -.
DR VEuPathDB; HostDB:ENSG00000149781; -.
DR eggNOG; KOG3727; Eukaryota.
DR GeneTree; ENSGT00390000013444; -.
DR HOGENOM; CLU_011611_0_0_1; -.
DR InParanoid; Q86UX7; -.
DR OMA; AMAGMKT; -.
DR OrthoDB; 248494at2759; -.
DR PhylomeDB; Q86UX7; -.
DR TreeFam; TF314677; -.
DR PathwayCommons; Q86UX7; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q86UX7; -.
DR SIGNOR; Q86UX7; -.
DR BioGRID-ORCS; 83706; 30 hits in 1073 CRISPR screens.
DR ChiTaRS; FERMT3; human.
DR EvolutionaryTrace; Q86UX7; -.
DR GeneWiki; FERMT3; -.
DR GenomeRNAi; 83706; -.
DR Pharos; Q86UX7; Tbio.
DR PRO; PR:Q86UX7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86UX7; protein.
DR Bgee; ENSG00000149781; Expressed in granulocyte and 119 other tissues.
DR ExpressionAtlas; Q86UX7; baseline and differential.
DR Genevisible; Q86UX7; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0030055; C:cell-substrate junction; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0033622; P:integrin activation; IDA:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IDA:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd01237; PH_fermitin; 1.
DR DisProt; DP01784; -.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR037843; Kindlin/fermitin.
DR InterPro; IPR040790; Kindlin_2_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037837; PH_Kindlin/fermitin.
DR PANTHER; PTHR16160; PTHR16160; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF18124; Kindlin_2_N; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW Cell projection; Direct protein sequencing; Disease variant;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..667
FT /note="Fermitin family homolog 3"
FT /id="PRO_0000219454"
FT DOMAIN 229..558
FT /note="FERM"
FT DOMAIN 354..457
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 504
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 360..363
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12697302,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_009226"
FT VARIANT 599
FT /note="Q -> S (in LAD3; unknown pathological significance;
FT decreases cell adhesion in hematopoietic cells; requires 2
FT nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:26359933"
FT /id="VAR_074597"
FT CONFLICT 472
FT /note="A -> P (in Ref. 2; BAC04220)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="Q -> R (in Ref. 2; BAC04220)"
FT /evidence="ECO:0000305"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:6V9G"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 91..103
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:6V9G"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 265..280
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 288..306
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2YS3"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:2YS3"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:2YS3"
FT TURN 391..395
FT /evidence="ECO:0007829|PDB:2YS3"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:2YS3"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2YS3"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:2YS3"
FT STRAND 419..427
FT /evidence="ECO:0007829|PDB:2YS3"
FT STRAND 429..441
FT /evidence="ECO:0007829|PDB:2YS3"
FT HELIX 442..456
FT /evidence="ECO:0007829|PDB:2YS3"
FT HELIX 465..480
FT /evidence="ECO:0007829|PDB:2YS3"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 509..514
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 517..529
FT /evidence="ECO:0007829|PDB:6V9G"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 536..548
FT /evidence="ECO:0007829|PDB:6V9G"
FT TURN 551..554
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 556..562
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 575..581
FT /evidence="ECO:0007829|PDB:6V9G"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 587..593
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 597..603
FT /evidence="ECO:0007829|PDB:6V9G"
FT TURN 604..607
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 608..613
FT /evidence="ECO:0007829|PDB:6V9G"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:6V9G"
FT STRAND 617..626
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 628..641
FT /evidence="ECO:0007829|PDB:6V9G"
FT TURN 642..645
FT /evidence="ECO:0007829|PDB:6V9G"
FT TURN 647..649
FT /evidence="ECO:0007829|PDB:6V9G"
FT HELIX 654..660
FT /evidence="ECO:0007829|PDB:6V9G"
SQ SEQUENCE 667 AA; 75953 MW; 5ACE15EB689B91B5 CRC64;
MAGMKTASGD YIDSSWELRV FVGEEDPEAE SVTLRVTGES HIGGVLLKIV EQINRKQDWS
DHAIWWEQKR QWLLQTHWTL DKYGILADAR LFFGPQHRPV ILRLPNRRAL RLRASFSQPL
FQAVAAICRL LSIRHPEELS LLRAPEKKEK KKKEKEPEEE LYDLSKVVLA GGVAPALFRG
MPAHFSDSAQ TEACYHMLSR PQPPPDPLLL QRLPRPSSLS DKTQLHSRWL DSSRCLMQQG
IKAGDALWLR FKYYSFFDLD PKTDPVRLTQ LYEQARWDLL LEEIDCTEEE MMVFAALQYH
INKLSQSGEV GEPAGTDPGL DDLDVALSNL EVKLEGSAPT DVLDSLTTIP ELKDHLRIFR
IPRRPRKLTL KGYRQHWVVF KETTLSYYKS QDEAPGDPIQ QLNLKGCEVV PDVNVSGQKF
CIKLLVPSPE GMSEIYLRCQ DEQQYARWMA GCRLASKGRT MADSSYTSEV QAILAFLSLQ
RTGSGGPGNH PHGPDASAEG LNPYGLVAPR FQRKFKAKQL TPRILEAHQN VAQLSLAEAQ
LRFIQAWQSL PDFGISYVMV RFKGSRKDEI LGIANNRLIR IDLAVGDVVK TWRFSNMRQW
NVNWDIRQVA IEFDEHINVA FSCVSASCRI VHEYIGGYIF LSTRERARGE ELDEDLFLQL
TGGHEAF
