ID A0A2K5HMF9_COLAP Unreviewed; 1332 AA.
AC A0A2K5HMF9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pro-interleukin-16 {ECO:0000256|RuleBase:RU363135};
DE Contains:
DE RecName: Full=Interleukin-16 {ECO:0000256|RuleBase:RU363135};
DE Short=IL-16 {ECO:0000256|RuleBase:RU363135};
DE AltName: Full=Lymphocyte chemoattractant factor {ECO:0000256|RuleBase:RU363135};
DE Short=LCF {ECO:0000256|RuleBase:RU363135};
GN Name=IL16 {ECO:0000256|RuleBase:RU363135};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000005520.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000005520.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Interleukin-16 stimulates a migratory response in CD4+
CC lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2
CC and IL-15 responsiveness. Also induces T-lymphocyte expression of
CC interleukin 2 receptor. Ligand for CD4. {ECO:0000256|ARBA:ARBA00024706,
CC ECO:0000256|RuleBase:RU363135}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU363135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU363135}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363135}.
CC Secreted {ECO:0000256|RuleBase:RU363135}.
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DR STRING; 336983.ENSCANP00000005520; -.
DR Ensembl; ENSCANT00000021124.1; ENSCANP00000005520.1; ENSCANG00000018531.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 4.
DR Gene3D; 2.30.42.10; -; 4.
DR InterPro; IPR020450; IL-16.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR48396; PRO-INTERLEUKIN-16; 1.
DR PANTHER; PTHR48396:SF2; PRO-INTERLEUKIN-16; 1.
DR Pfam; PF00595; PDZ; 3.
DR PRINTS; PR01931; INTRLEUKIN16.
DR SMART; SM00228; PDZ; 4.
DR SUPFAM; SSF50156; PDZ domain-like; 4.
DR PROSITE; PS50106; PDZ; 4.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU363135};
KW Cytokine {ECO:0000256|ARBA:ARBA00022514, ECO:0000256|RuleBase:RU363135};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU363135};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363135};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU363135};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 216..302
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 355..425
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1112..1197
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1234..1319
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 27..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1332 AA; 141920 MW; 21BA466A4DD96A26 CRC64;
MESHSRAGKN RKSAKFRSIS RSLMLCNAKT SDDGSSPDEK YPDPSEISLA QGKEGIFHSS
VQLADTSEDG PSSIPDLALA SEAAQLQVAG NDRGKTCRRI FFMKESSTAS SREKPGKPEA
QSSNFLFPKA CHQRARSNST SVNPYCTREV DFPMTKKSAA STDRQPYSLC SNRKSLSQQL
DCPAGKAAET SRPTRSLSTA QLAQPSGGLQ ASVISNIVLM KGQAKGLGFS IVGGKDSIYG
PIGIYVKTIF AGGAAAADGR LQEGDEILEL NGESMAGLTH QDALQKFKQA KKGLLTLTVR
TRLMAPPSLC SHLSPPLCRS LSSSTCITKD SSSFALESPS APISTAKPNY RIMVEVSLQK
EAGVGLGIGL CSVPYFQCIS GIFVHTLSPG SVAHLDGRLR CGDEIVEISD SPVHCLTLNE
VYTILSHCDP GPVPIIVSRH PDPQVSEQQL KEAVAQAVEN TKFAKERHQW SLEGVKRLES
SWHGRPTLEK EREKNSAPPH RRAQKIMIRS SSDSSYMSGS PGGSPGSGSA GKPSSDVDIS
THSPSLPLAR EPVVLSIASS RLPQESPPVP ESQDSHPPLR LKKPFEILVR KPTSSKPKPP
PRKYFKSDSD PQKSLEEREK SSCSSGHTPP TCGQEARELL PLLLPQEDTA GRSPSASASC
PGPGICPQTK SSTEGEPGRR RASPVTQTSP IKHPLLKRQA RMDYSFDTTA EDPWVRISDC
IKNLFSPIMS ENPGHMPLQP NASLSEEDGT QGHPDGTPPK LDTANGTPKV YKSADRSTVK
KGPPVAPKPA WFRQSLKGLR NRASDPRGLP DPALSIQPAP ASREHLGPHI RASSSSSSIK
QRISSFETFG SSQLPDKGAQ RLSLQPSSGE AAKPLGKHEG GRFSGLLGRR AAPTLVPQQP
EQVLPSGSPA AMEARDPGVS ASPPPGLQPN QKTLPTGSDP LLRLLSTQTE KSQGPVLKMP
SQRARSFPLT RSQSCETKLL DEKTSKLYSI SSQVSSAVMK SLLCLPSSLS CAQTPCIPKE
GASPTSSSNE DSAANGSAET SASDTGFSLN LSELREYTEG LTEAKEDDDG DHSSHQSGQS
VFSLLSSEEL KQLIEEVKVL DEATLKQLDS IHVTILHKEE GAGLGFSLAG GADLENKVIT
VHRVFPNGLA SQEGTIQKGN EVLSINGKSL KGTTHNDALA ILRQAREPRQ AVIVTRKLTA
ESMPDLNSTT DSAASASAAS DVSVESSAEA TVYTVTLEKM SAGLGFSLEG GKGSLHGDKP
LTINRIFKGA ASEQSETIQP GDEILQLAGT AMQGLTRFEA WNIIKALPDG PVTIVIRRKS
LQPKETTAAA DS
//
